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        <title>Cell Stress and Chaperones via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'Cell Stress and Chaperones' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Cell+Stress+and+Chaperones&t=Cell+Stress+and+Chaperones&s=Search&f=source]]></link>
        <lastBuildDate>Tue, 07 Feb 2012 08:48:54 +0100</lastBuildDate>
        <item>
            <title>Molecular characterization and mRNA expression of grp78 and hsp90A in the estuarine copepod Eurytemora affinis.</title>
            <link>http://www.medworm.com/index.php?rid=5659131&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22302500%26dopt%3DAbstract</link>
            <description>Authors: Xuereb B, Forget-Leray J, Souissi S, Glippa O, Devreker D, Lesueur T, Marie S, Danger JM, Boulangé-Lecomte C
    Abstract
    The present study aimed to develop a method of quantification of heat shock protein transcript levels in the estuarine copepod Eurytemora affinis. For that, the full-length cDNA of the 78-kDa glucose-regulated protein (Ea-grp78) and the cytosolic 90-kDa heat shock protein (Ea-hsp90A) from this species have been cloned. These cDNA revealed, respectively, 2,370 and 2,299 bp with 1,971 and 2,124 bp open reading frames encoding 656 and 707 amino acids. Main features, sequence identities and phylogenetic analysis with other species were described. Then, the expression profiles were analysed using reverse transcription/real-time quantitative PCR method from co...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659131</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Impairment of cellular immunity is associated with overexpression of heat shock protein 70 in neonatal pigs with intrauterine growth retardation.</title>
            <link>http://www.medworm.com/index.php?rid=5640287&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270614%26dopt%3DAbstract</link>
            <description>In conclusion, IUGR impairs immune functions in neonatal pigs. An inefficient immunity in IUGR piglets is associated with overexpression of Hsp70, which impairs NF-κB signaling and upregulates FoxO3a expression.
    PMID: 22270614 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640287</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640287</guid>        </item>
        <item>
            <title>Protective effects of leukemia inhibitory factor against oxidative stress during high glucose-induced apoptosis in podocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5640317&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270613%26dopt%3DAbstract</link>
            <description>Authors: Xu J, Li Z, Xu P, Yang Z
    Abstract
    Leukemia inhibitory factor (LIF) is a pleiotropic glycoprotein belonging to the interleukin-6 family of cytokines. In kidney, LIF regulates nephrogenesis, involves in tubular regeneration, responds to pro- and anti-inflammatory stimuli, and so on. LIF also plays an essential role in protective mechanisms triggered by preconditioning-induced oxidative stress. Although LIF shows a wide range of biologic activities, effects of LIF on high glucose-induced oxidative stress in podocytes remain unclear. The aim of the study was to assess whether LIF can attenuate high glucose-induced apoptosis in podocytes. The result of 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay indicated that LIF protected podocytes against high glucose-...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640317</comments>
            <pubDate>Sun, 22 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640317</guid>        </item>
        <item>
            <title>Herpes simplex virus-1 disarms the unfolded protein response in the early stages of infection.</title>
            <link>http://www.medworm.com/index.php?rid=5640318&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270612%26dopt%3DAbstract</link>
            <description>Authors: Burnett HF, Audas TE, Liang G, Lu RR
    Abstract
    Accumulation of mis- and unfolded proteins during viral replication can cause stress in the endoplasmic reticulum (ER) and trigger the unfolded protein response (UPR). If unchecked, this process may induce cellular changes detrimental to viral replication. In the report, we investigated the impact of HSV-1 on the UPR during lytic replication. We found that HSV-1 effectively disarms the UPR in early stages of viral infection. Only ATF6 activation was detected during early infection, but with no upregulation of target chaperone proteins. Activity of the eIF2α/ATF4 signaling arm increased at the final stage of HSV-1 replication, which may indicate completion of virion assembly and egress, thus releasing suppression of the UPR. We...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640318</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640318</guid>        </item>
        <item>
            <title>Cynoglossus semilaevis thioredoxin: a reductase and an antioxidant with immunostimulatory property.</title>
            <link>http://www.medworm.com/index.php?rid=5640319&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270611%26dopt%3DAbstract</link>
            <description>In this study, we identified and analyzed the function of a Trx homologue, CsTrx1, from half-smooth tongue sole (Cynoglossus semilaevis). The deduced amino acid sequence of CsTrx1 is composed of 107 residues and shares 54.1-60.8% overall identities with the Trx of other teleosts. CsTrx1 contains the highly conserved CXXC motif, which in mammals is known to be the active site, in the form of CQPC. Expression of CsTrx1 as determined by quantitative real-time reverse transcriptase PCR was highest in liver and upregulated in time-dependent manners by bacterial infection and by exposure to iron, copper, and hydrogen peroxide. Purified recombinant CsTrx1 (rCsTrx1) exhibited insulin disulfide reductase activity and antioxidant activity, both which, however, were lost when the two cysteine residue...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5640319</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5640319</guid>        </item>
        <item>
            <title>Ferruccio Ritossa's scientific legacy 50 years after his discovery of the heat shock response: a new view of biology, a new society, and a new journal.</title>
            <link>http://www.medworm.com/index.php?rid=5623188&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22252402%26dopt%3DAbstract</link>
            <description>This article is based on a session of the Fifth CSSI Congress held in Québec commemorating Professor Ritossa and his discovery.
    PMID: 22252402 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5623188</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5623188</guid>        </item>
        <item>
            <title>Stress levels over time in the introduced ascidian Styela plicata: the effects of temperature and salinity variations on hsp70 gene expression.</title>
            <link>http://www.medworm.com/index.php?rid=5602354&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249790%26dopt%3DAbstract</link>
            <description>Authors: Pineda MC, Turon X, López-Legentil S
    Abstract
    Species distribution, abundance, and long-term survival are determined by biotic and abiotic regimes. However, little is known about the importance of these factors in species range expansion. Styela plicata is a solitary ascidian introduced all over the world by ship fouling, including salt marsh habitats, where introduced populations must tolerate high seasonal variations in temperature and salinity. To determine the seasonal stress levels in a salt marsh population of S. plicata, we quantified heat shock protein (hsp70) gene expression using quantitative real-time PCR throughout a 2-year cycle. Results showed that hsp70 expression varied over time, with higher stress levels recorded in summer and winter. Periodic conditions...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5602354</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5602354</guid>        </item>
        <item>
            <title>Plasma Hsp72 (HSPA1A) and Hsp27 (HSPB1) expression under heat stress: influence of exercise intensity.</title>
            <link>http://www.medworm.com/index.php?rid=5578528&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22222935%26dopt%3DAbstract</link>
            <description>This study examined the influence of exercise at various intensities to elucidate this relationship, and investigated the association between eHsp72 and eHsp27. Sixteen male subjects cycled to exhaustion at 60% and 75% of maximal oxygen uptake in hot conditions (40°C, 50% RH). Core temperature, heart rate, oxidative stress, and blood lactate and glucose levels were measured to determine the predictor variables associated with eHsp expression. At exhaustion, heart rate exceeded 96% of maximum in both conditions. Core temperature reached 39.7°C in the 60% trial (58.9 min) and 39.0°C in the 75% trial (27.2 min) (P &amp;lt; 0.001). The rate of rise in core temperature was 2.1°C h(-1) greater in the 75% trial than in the 60% trial (P &amp;lt; 0.001). A significant increase and correlatio...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5578528</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5578528</guid>        </item>
        <item>
            <title>Proteotoxic stress and circulating cell stress proteins in the cardiovascular diseases.</title>
            <link>http://www.medworm.com/index.php?rid=5560294&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215517%26dopt%3DAbstract</link>
            <description>Authors: Henderson B, Pockley AG
    Abstract
    The cardiovasculature is one of the major body systems and probably the one most exposed to stress. There is clear evidence that increasing levels of cell stress proteins within the heart is cardioprotective. In addition, there is rapidly emerging evidence that secreted cell stress proteins play a role in the function of the cardiovascular tissues. Those secreted proteins have three potential functions: (1) as normal homeostatic cardiovascular signals (e.g. protein disulphide isomerase); (2) as anti-inflammatory molecules, which are able to inhibit cardiovascular pathology (e.g. Hsp27); and (iii) as pro-inflammatory signals that can induce and promote cardiovascular pathology (e.g. Hsp60). As all of these various proteins may be released-at...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5560294</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5560294</guid>        </item>
        <item>
            <title>Involvement of molecular chaperones and the transcription factor Nrf2 in neuroprotection mediated by para-substituted-4,5-diaryl-3-thiomethyl-1,2,4-triazines.</title>
            <link>http://www.medworm.com/index.php?rid=5560296&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22212523%26dopt%3DAbstract</link>
            <description>Authors: Khodagholi F, Ansari N, Amini M, Tusi SK
    Abstract
    Much evidence supports that oxidative stress plays an important role in the pathogenesis of neurodegenerative diseases, such as Alzheimer's disease. Herein, we studied the compensatory/adaptive mechanisms involved in 3-thiomethyl-5,6-(diphenyl)-1,2,4-triazine and 3-thiomethyl-5,6-(dichlorophenyl)-1,2,4-triazine neuroprotection. We found that these compounds could counteract H(2)O(2)-induced rupture of neurite outgrowth in differentiated PC12 cells. In addition, we found that pretreatment of cells with triazine derivatives could modulate the expression of heat shock proteins Hsp70, Hsp90, and Hsp32 in H(2)O(2)-treated PC12 cells. These compounds could also increase nuclear level of stress sensing transcription factor, NF-E2 ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5560296</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5560296</guid>        </item>
        <item>
            <title>Heat-shock protein 60 kDa and atherogenic dyslipidemia in patients with untreated mild periodontitis: a pilot study.</title>
            <link>http://www.medworm.com/index.php?rid=5560295&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215516%26dopt%3DAbstract</link>
            <description>Authors: Rizzo M, Cappello F, Marfil R, Nibali L, Marino Gammazza A, Rappa F, Bonaventura G, Galindo-Moreno P, O'Valle F, Zummo G, Conway de Macario E, Macario AJ, Mesa F
    Abstract
    Identification of predictors of cardiovascular risk can help in the prevention of pathologic episodes and the management of patients at all stages of illness. Here, we investigated the relationships between serum levels of Hsp60 and dyslipidemia in patients with periodontitis by performing a cross-sectional study of 22 patients with mild periodontitis without any prior treatment for it (i.e., drug naïve) and 22 healthy controls, matched for age and body mass index (BMI). All subjects were evaluated for periodontal status, gingival inflammation, and oral hygiene. Levels of circulating Hsp60, C-reactive pr...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5560295</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5560295</guid>        </item>
        <item>
            <title>Divergence of intracellular and extracellular HSP72 in type 2 diabetes: does fat matter?</title>
            <link>http://www.medworm.com/index.php?rid=5560293&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215518%26dopt%3DAbstract</link>
            <description>Authors: Rodrigues-Krause J, Krause M, O'Hagan C, De Vito G, Boreham C, Murphy C, Newsholme P, Colleran G
    PMID: 22215518 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5560293</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5560293</guid>        </item>
        <item>
            <title>Increased immunogenicity is an integral part of the heat shock response following renal ischemia.</title>
            <link>http://www.medworm.com/index.php?rid=5535212&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22180342%26dopt%3DAbstract</link>
            <description>This study therefore tested the hypothesis that upregulation of renal tubular immunogenicity is an integral part of the heat shock response after renal ischemia. Expressions of 70 kDa heat shock protein (Hsp70), major histocompatibility complex (MHC) class II, and intercellular adhesion molecule-1 (ICAM-1) were assessed in normal rat kidney (NRK) cells following ATP depletion (antimycin A for 3 h) and heat (42°C for 24 h). In vitro, transient Hsp70 transfection and heat shock factor-1 (HSF-1) transcription factor decoy treatment were performed. In vivo, ischemic renal cortex was investigated in Sprague-Dawley rats following unilateral renal artery clamping for 45 min and 24 h recovery. Upregulation of Hsp70 was closely and significantly correlated with upregulation of MHC class II an...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535212</comments>
            <pubDate>Sat, 17 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535212</guid>        </item>
        <item>
            <title>Plasma heat shock protein 72 as a biomarker of sarcopenia in elderly people.</title>
            <link>http://www.medworm.com/index.php?rid=5535214&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22144131%26dopt%3DAbstract</link>
            <description>Authors: Ogawa K, Kim HK, Shimizu T, Abe S, Shiga Y, Calderwood SK
    Abstract
    Sarcopenia is a geriatric syndrome in which there is a decrease of muscle mass and strength with aging. In age-related loss of muscle strength, there are numerous observations supporting the assertion that neural factors mediate muscle strength. A possible contributing cause may be that aging changes systemic extracellular heat shock protein (eHsp)72 activity. The present study was designed to assess the plasma levels of eHsp72 in elderly people and to investigate its potential interaction with components of sarcopenia. A total of 665 men and women participated in an official medical health examination and an integrated health examination, including psychological and physical fitness tests. Blood samples we...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535214</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535214</guid>        </item>
        <item>
            <title>Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities.</title>
            <link>http://www.medworm.com/index.php?rid=5535213&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22144132%26dopt%3DAbstract</link>
            <description>Authors: Nowicki L, Leźnicki P, Morawiec E, Litwińczuk N, Liberek K
    Abstract
    Besides its beneficial role in thermotolerance, the chaperone protein Hsp104 is involved in the inheritance of yeast Saccharomyces cerevisiae prions. Guanidine hydrochloride was previously shown to interfere with Hsp104 chaperone activity in vivo, thus impairing thermotolerance and resulting in prion curing. It was also reported that guanidine inhibits Hsp104 ATPase and disaggregation activity. We show that in vitro guanidine significantly inhibits the disaggregation activity of ClpB, the bacterial orthologue of Hsp104. However, guanidine exerts opposite effects on the ATPase activities of Hsp104 and ClpB. While the ATPase activity of Hsp104 is inhibited, the analogous ClpB activity is stimulated several...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535213</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535213</guid>        </item>
        <item>
            <title>A case of mistaken identity: HSPs are no DAMPs but DAMPERs.</title>
            <link>http://www.medworm.com/index.php?rid=5535215&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22139593%26dopt%3DAbstract</link>
            <description>Authors: van Eden W, Spiering R, Broere F, van der Zee R
    Abstract
    Until recently, the immune system was seen solely as a defense system with its primary task being the elimination of unwanted microbial invaders. Currently, however, the functional significance of the immune system has obtained a much wider perspective, to include among others the maintenance and restoration of homeostasis following tissue damage. In this latter aspect, there is a growing interest in the identification of molecules involved, such as the so-called danger or damage-associated molecular patterns (DAMPs), also called alarmins. Since heat shock proteins are archetypical molecules produced under stressful conditions, such as tissue damage or inflammation, they are frequently mentioned as prime examples of ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535215</comments>
            <pubDate>Sat, 03 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535215</guid>        </item>
        <item>
            <title>Short (GT)                   (                      n                             ) repeats in heme oxygenase-1 gene promoter are associated with lower risk of coronary heart disease in subjects with high levels of oxidative stress.</title>
            <link>http://www.medworm.com/index.php?rid=5535216&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22120665%26dopt%3DAbstract</link>
            <description>Short (GT)          (           n               ) repeats in heme oxygenase-1 gene promoter are associated with lower risk of coronary heart disease in subjects with high levels of oxidative stress.
    Cell Stress Chaperones. 2011 Nov 27;
    Authors: Chen M, Zhou L, Ding H, Huang S, He M, Zhang X, Cheng L, Wang D, Hu FB, Wu T
    Abstract
    Although (GT)           (             n           ) repeats in heme oxygenase-1 (HO-1) promoter may modulate gene transcriptional activity, the association between (GT)           (             n           ) repeats polymorphism and risk of coronary heart disease (CHD) from different levels of oxidative stress (OS) is unknown. We determined the allelic frequencies of (GT)           (             n           ) repeats in the HO-1 gene promoter and pla...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535216</comments>
            <pubDate>Sun, 27 Nov 2011 05:00:00 +0100</pubDate>
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        <item>
            <title>Response of preosteoblasts to thermal stress conditioning and osteoinductive growth factors.</title>
            <link>http://www.medworm.com/index.php?rid=5535217&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22116637%26dopt%3DAbstract</link>
            <description>In this study, a preosteoblast cell line (MC3T3-E1) was exposed to treatment with water bath heating (44°C, 4 and 8 min) and osteoinductive GFs (bone morphogenetic protein-2 and transforming growth factor-β1) individually or in combination to investigate whether these stimuli could promote induction of bone-related markers, an angiogenic factor, and heat shock proteins (HSPs). Cells remained viable when heating durations were less than 20 min at 40ºC, 16 min at 42ºC, and 10 min at 44ºC. Increasing heating duration at 44°C, promoted gene expression of HSPs, osteocalcin (OCN), and osteopontin (OPN) at 8 h post-heating (PH). Heating in combination with GFs caused the greatest gene induction of osteoprotegerin (OPG; 6.9- and 1.6-fold induction compared to sham-treated and GF only trea...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535217</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535217</guid>        </item>
        <item>
            <title>Protein deprivation attenuates Hsp expression in fat tissue.</title>
            <link>http://www.medworm.com/index.php?rid=5421446&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22081321%26dopt%3DAbstract</link>
            <description>Authors: Eitam H, Agmon R, Asher A, Brosh A, Orlov A, Izhaki I, Shabtay A
    Abstract
    For ruminants, dietary protein is the first limiting component to the utilization of low-quality forage. Throughout gestation, low-protein intake may result in prenatal programming that causes various metabolic disturbances and physiological modulations to dams and their developing embryos. We studied the effect of long-term low-protein diet (LPD) on physiological, biochemical, and molecular parameters of the energy status in gestating beef cows. LPD resulted in significant reductions in feed intake and heart rate and promoted a negative retained energy status already after 3 weeks. Elevated levels of plasma creatinine and non-esterified fatty acids indicate endogenous degradation of fat and protein...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5421446</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5421446</guid>        </item>
        <item>
            <title>Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK).</title>
            <link>http://www.medworm.com/index.php?rid=5421447&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22076723%26dopt%3DAbstract</link>
            <description>Authors: Thompson AD, Bernard SM, Skiniotis G, Gestwicki JE
    Abstract
    The molecular chaperone DnaK binds to exposed hydrophobic segments in proteins, protecting them from aggregation. DnaK interacts with protein substrates via its substrate-binding domain, and the affinity of this interaction is allosterically regulated by its nucleotide-binding domain. In addition to regulating interdomain allostery, the nucleotide state has been found to influence homo-oligomerization of DnaK. However, the architecture of oligomeric DnaK and its potential functional relevance in the chaperone cycle remain undefined. Towards that goal, we examined the structures of DnaK by negative stain electron microscopy. We found that DnaK samples contain an ensemble of monomers, dimers, and other small, define...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5421447</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5421447</guid>        </item>
        <item>
            <title>Immunomodulatory effect of NSAID in geriatric patients with acute infection: effects of piroxicam on chemokine/cytokine secretion patterns and levels of heat shock proteins. A double-blind randomized controlled trial. (ISRCTN58517443).</title>
            <link>http://www.medworm.com/index.php?rid=5421448&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057579%26dopt%3DAbstract</link>
            <description>Authors: Beyer I, Njemini R, Bautmans I, Demanet C, Mets T
    Abstract
    Inflammation in older persons is associated with frailty, cachexia, and disability. We hypothesized that NSAID treatment in addition to antibiotics in older patients with acute infection might rapidly reduce inflammatory cytokines and might be of therapeutic potential to improve outcomes. A double-blind controlled trial was conducted in geriatric patients admitted for acute infection. Patients were randomized to receive either 10 mg piroxicam or placebo. Patients ≥70 years with CRP levels &amp;gt;10 mg/L of acute infectious origin were eligible. Twenty-five cyto-/chemokines as well as heat shock proteins Hsp27 (HSPB1) and Hsp70 (HSPA1A) were measured the first 4 days and then weekly until discharge, with a maximu...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5421448</comments>
            <pubDate>Sat, 05 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5421448</guid>        </item>
        <item>
            <title>Prevention and treatment of alopecia areata with quercetin in the C3H/HeJ mouse model.</title>
            <link>http://www.medworm.com/index.php?rid=5380038&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22042611%26dopt%3DAbstract</link>
            <description>In this study, we tested the effects of quercetin, a bioflavonoid with anti-inflammatory properties, on AA development and HSP70 expression in the C3H/HeJ model. Mice with spontaneous AA were treated with subcutaneous quercetin or sham injections. Hair regrowth was observed in lesional areas in all the quercetin-treated mice, but in none of the sham-treated mice. In addition, non-alopecic C3H/HeJ mice were heat-treated to induce alopecia, along with quercetin or sham injections. Whereas 24% of the heat-treated mice with sham injections developed alopecia, none of the mice receiving quercetin injections did. As expected, the level of HSP70 expression in quercetin-treated areas was comparable to control. Furthermore, we showed that systemic delivery of quercetin by intraperitoneal injections...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380038</comments>
            <pubDate>Tue, 01 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380038</guid>        </item>
        <item>
            <title>A quantitative method for detection of spliced X-box binding protein-1 (XBP1) mRNA as a measure of endoplasmic reticulum (ER) stress.</title>
            <link>http://www.medworm.com/index.php?rid=5380039&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22038282%26dopt%3DAbstract</link>
            <description>Authors: van Schadewijk A, Van't Wout EF, Stolk J, Hiemstra PS
    Abstract
    Endoplasmic reticulum (ER) stress is increasingly recognized as an important mechanism in a wide range of diseases including cystic fibrosis, alpha-1 antitrypsin deficiency, Parkinson's and Alzheimer's disease. Therefore, there is an increased need for reliable and quantitative markers for detection of ER stress in human tissues and cells. Accumulation of unfolded or misfolded proteins in the endoplasmic reticulum can cause ER stress, which leads to the activation of the unfolded protein response (UPR). UPR signaling involves splicing of X-box binding protein-1 (XBP1) mRNA, which is frequently used as a marker for ER stress. In most studies, the splicing of the XBP1 mRNA is visualized by gel electrophoresis whi...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380039</comments>
            <pubDate>Mon, 31 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380039</guid>        </item>
        <item>
            <title>Comparison of epitope specificity of anti-heat shock protein 60/65 IgG type antibodies in the sera of healthy subjects, patients with coronary heart disease and inflammatory bowel disease.</title>
            <link>http://www.medworm.com/index.php?rid=5380041&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22038196%26dopt%3DAbstract</link>
            <description>Authors: Füst G, Uray K, Bene L, Hudecz F, Karádi I, Prohászka Z
    Abstract
    Previously, we reported on the presence of antibodies to linear epitopes of human and mycobacterial 60 kD heat shock proteins (HSP) in the sera of healthy blood donors. Since many recent findings indicate that the levels of these antibodies may be altered in coronary heart disease (CHD) and also inflammatory bowel diseases (IBD), it seemed worthwhile to compare the epitope specificity of the anti-HSP60 and anti-HSP65 antibodies in the sera of patients with these diseases to those in healthy subjects. The multipin enzyme-linked immunosorbent assay method was applied with a large overlapping set of synthetic 10-mer peptides covering selected regions of human HSP60 and Mycobacterium bovis HSP65. Sera of 12 h...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380041</comments>
            <pubDate>Sat, 29 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380041</guid>        </item>
        <item>
            <title>Molecular and functional characterization of the only known hemiascomycete ortholog of the carboxyl terminus of Hsc70-interacting protein CHIP in the yeast Yarrowia lipolytica.</title>
            <link>http://www.medworm.com/index.php?rid=5380040&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22038197%26dopt%3DAbstract</link>
            <description>Authors: Martineau CN, Le Dall MT, Melki R, Beckerich JM, Kabani M
    Abstract
    The carboxyl terminus of Hsc70-interacting protein (CHIP) is an Hsp70 co-chaperone and a U-box ubiquitin ligase that plays a crucial role in protein quality control in higher eukaryotes. The yeast Yarrowia lipolytica is the only known hemiascomycete where a CHIP ortholog is found. Here, we characterize Y. lipolytica's CHIP ortholog (Yl.Chn1p) and document its interactions with components of the protein quality control machinery. We show that Yl.Chn1p is non-essential unless Y. lipolytica is severely stressed. We sought for genetic interactions among key components of the Y. lipolytica protein quality control arsenal, including members of the Ssa-family of Hsp70 molecular chaperones, the Yl.Bag1p Hsp70 nucle...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380040</comments>
            <pubDate>Sat, 29 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380040</guid>        </item>
        <item>
            <title>Heat shock protein expression in canine osteosarcoma.</title>
            <link>http://www.medworm.com/index.php?rid=5361322&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22015573%26dopt%3DAbstract</link>
            <description>In conclusion, absence of Hsp72 immunosignal appears to be associated with a favourable prognosis whilst the widespread Hsp90 immunoreactivity detected in all tumour cases as well as in neoplastic emboli, suggests this protein could be targeted in the therapy of canine OSA, and likewise in its human counterpart.
    PMID: 22015573 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5361322</comments>
            <pubDate>Fri, 21 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5361322</guid>        </item>
        <item>
            <title>Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop).</title>
            <link>http://www.medworm.com/index.php?rid=5329238&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22005844%26dopt%3DAbstract</link>
            <description>In this study, recombinant P. falciparum Hop (PfHop) was heterologously produced in E. coli and purified by nickel affinity chromatography. Using specific anti-PfHop antisera, the expression and localisation of PfHop in P. falciparum was investigated. PfHop was shown to co-localise with PfHsp70 and PfHsp90 in parasites at the trophozoite stage. Gel filtration and co-immunoprecipitation experiments suggested that PfHop was present in a complex together with PfHsp70 and PfHsp90. The association of PfHop with both PfHsp70 and PfHsp90 suggests that this protein may mediate the functional interaction between the two chaperones.
    PMID: 22005844 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329238</comments>
            <pubDate>Tue, 18 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329238</guid>        </item>
        <item>
            <title>Heterooligomeric complexes of human small heat shock proteins.</title>
            <link>http://www.medworm.com/index.php?rid=5329239&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22002549%26dopt%3DAbstract</link>
            <description>Authors: Mymrikov EV, Seit-Nebi AS, Gusev NB
    Abstract
    Oligomeric association of human small heat shock proteins HspB1, HspB5, HspB6 and HspB8 was analyzed by means of size-exclusion chromatography, analytical ultracentrifugation and chemical cross-linking. Wild-type HspB1 and Cys mutants of HspB5, HspB6 and HspB8 containing a single Cys residue in position homologous to that of Cys137 of human HspB1 were able to generate heterodimers cross-linked by disulfide bond. Cross-linked heterodimers between HspB1/HspB5, HspB1/HspB6 and HspB5/HspB6 were easily produced upon mixing, whereas formation of any heterodimers with participation of HspB8 was significantly less efficient. The size of heterooligomers formed by HspB1/HspB6 and HspB5/HspB6 was different from the size of the correspondin...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329239</comments>
            <pubDate>Mon, 17 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329239</guid>        </item>
        <item>
            <title>Phage display biopanning identifies the translation initiation and elongation factors (IF1α-3 and eIF-3) as components of Hsp70-peptide complexes in breast tumour cells.</title>
            <link>http://www.medworm.com/index.php?rid=5329240&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22002548%26dopt%3DAbstract</link>
            <description>Authors: Siebke C, James TC, Cummins R, O'Grady T, Kay E, Bond U
    Abstract
    The heat shock protein, HSP70, is over-expressed in many tumours and acts at the crossroads of key intracellular processes in its role as a molecular chaperone. HSP70 associates with a vast array of peptides, some of which are antigenic and can mount adaptive immune responses against the tumour from which they are derived. The pool of peptides associated with HSP70 represents a unique barcode of protein metabolism in tumour cells. With a view to identifying unique protein targets that may be developed as tumour biomarkers, we used purified HSP70 and its associated peptide pool (HSP70-peptide complexes, HSP70-PCs) from different human breast tumour cell lines as targets for phage display biopanning. Our result...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329240</comments>
            <pubDate>Sun, 16 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329240</guid>        </item>
        <item>
            <title>The identification and characterization of IbpA, a novel α-crystallin-type heat shock protein from mycoplasma.</title>
            <link>http://www.medworm.com/index.php?rid=5329241&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22002515%26dopt%3DAbstract</link>
            <description>In this report, we describe the cloning and functional characterization of a novel sHsp orthologue, IbpA protein, present in Acholeplasma laidlawii. Importantly, similar to the endogenously expressed sHsp proteins, the recombinant IbpA protein was able to spontaneously generate oligomers in vitro and to rescue chemically denatured bovine insulin from irreversible denaturation and aggregation. Collectively, these data suggest that IbpA is a bona fide member of the sHsps family. The immune-electron microscopy data using specific antibodies against IbpA have revealed different intracellular localization of this protein in A. laidlawii cells upon heat shock, which suggests that IbpA not only may participate in the stabilization of individual polypeptides, but may also play a protective role in...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5329241</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5329241</guid>        </item>
        <item>
            <title>Adenovirus-mediated expression of the HO-1 protein within MSCs decreased cytotoxicity and inhibited apoptosis induced by oxidative stresses.</title>
            <link>http://www.medworm.com/index.php?rid=5313245&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21993906%26dopt%3DAbstract</link>
            <description>In this study, we manipulated MSCs to express a cytoprotective factor, heme oxygenase-1 (HO-1), to address this issue. Full-length cDNA of human HO-1 was isolated and cloned into TOPO vector by TOPO cloning reaction. Then, the construct was ligated to gateway adapted adenovirus expression vector by LR recombination reaction. Afterwards, the recombinant virus expressing HO-1 was produced in appropriate mammalian cell line and used to infect MSCs. The HO-1 engineered MSCs were exposed to hypoxic and oxidative stress conditions followed by evaluation of the cells' viability and apoptosis. Transient expression of HO-1 was detected within MSCs. It was observed that HO-1 expression could protect MSCs against cell death and the apoptosis triggered by hypoxic and oxidative stress conditions. The M...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5313245</comments>
            <pubDate>Thu, 13 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5313245</guid>        </item>
        <item>
            <title>Dietary oxidative stress and antioxidant defense with an emphasis on plant extract administration.</title>
            <link>http://www.medworm.com/index.php?rid=5281363&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21956695%26dopt%3DAbstract</link>
            <description>Authors: Veskoukis AS, Tsatsakis AM, Kouretas D
    Abstract
    Eukaryotic cells generally function in a reduced state, but an amount of reactive species is essential for several biochemical processes. The antioxidant network is the defensive mechanism that occurs when the concentration of reactive species exceeds a threshold. Polyphenolic compounds present in plant extracts are potent antioxidants in vitro, but they may promote oxidative stress when administered in animals and humans, especially when given as supplements in exercise, a modality usually adopted as an oxidant stimulus. This is mainly observed when antioxidant molecules are administered separately and not as part of a diet. Exercise is usually adopted as a physiological model for examining the effects of reactive species in...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5281363</comments>
            <pubDate>Fri, 30 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5281363</guid>        </item>
        <item>
            <title>Heat shock protein 70 inhibits hydrogen peroxide-induced nucleolar fragmentation via suppressing cleavage and down-regulation of nucleolin.</title>
            <link>http://www.medworm.com/index.php?rid=5281362&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21960124%26dopt%3DAbstract</link>
            <description>Authors: Wang K, Deng G, Chen G, Liu M, Yi Y, Yang T, McMillan DR, Xiao X
    Abstract
    It has been reported that nucleolar fragmentation is a part of the overall apoptotic morphology, however, it is currently obscure whether and how nucleolar fragmentation can be induced by hydrogen peroxide (H(2)O(2)) and heat shock protein 70 (Hsp70) can prevent nucleolar fragmentation. To dissect these two questions, C(2)C(12) myogenic cells and immortalized mouse embryonic fibroblasts (MEFs) with heat shock transcriptional factor 1 (HSF1) null mutation were treated with heat shock response (HS) (42.5 ± 0.5°C for 1 h and recovery at 37°C for 24 h) and then were insulted with 0.5 mmol/L H(2)O(2). Morphological changes of nucleoli were observed under contrast microscope or electronic microsc...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5281362</comments>
            <pubDate>Fri, 30 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5281362</guid>        </item>
        <item>
            <title>hsp70 mRNA temporal localization in rat skeletal myofibers and blood vessels post-exercise.</title>
            <link>http://www.medworm.com/index.php?rid=5281364&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953294%26dopt%3DAbstract</link>
            <description>Authors: Silver JT, Kowalchuk H, Noble EG
    Abstract
    Rapid transcription of the survival transcript, inducible heat shock protein 70 (hsp70), is critical for mounting cytoprotection against severe cellular stress, like elevated temperature. Previous investigations have demonstrated that exercise-induced expression of Hsp70 protein occurs in a fiber-specific pattern; however, the activation pattern of hsp70 mRNA expression remains unclear in skeletal muscle. Consequentially, the temporal localization of hsp70 mRNA was characterized via in situ hybridization (ISH) experiments examining fast-muscle, white vastus: 1, 3, 10, and 24 h after a single bout of intense treadmill running (1 h, 30 m/min, 6% grade) in rats. The role that the physiologic temperature stress associated with exerc...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5281364</comments>
            <pubDate>Wed, 28 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5281364</guid>        </item>
        <item>
            <title>Regulation of survival gene hsp70.</title>
            <link>http://www.medworm.com/index.php?rid=5193040&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21874533%26dopt%3DAbstract</link>
            <description>Authors: Silver JT, Noble EG
    Abstract
    Rapid expression of the survival gene, inducible heat shock protein 70 (hsp70), is critical for mounting cytoprotection against severe cellular stress, like elevated temperature. Hsp70 protein chaperones the refolding of heat-denatured peptides to minimize proteolytic degradation as a part of an eukaryotically conserved phenomenon referred to as the heat shock response. The physiologic stress associated with exercise, which can include elevated temperature, mechanical damage, hypoxia, lowered pH, and reactive oxygen species generation, may promote protein unfolding, leading to hsp70 gene expression in skeletal myofibers. Although the pre-transcriptional activation of hsp70 gene expression has been thoroughly reviewed, discussion of downstream h...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5193040</comments>
            <pubDate>Sat, 27 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5193040</guid>        </item>
        <item>
            <title>Thermotolerance and molecular chaperone function of the small heat shock protein HSP20 from hyperthermophilic archaeon, Sulfolobus solfataricus P2.</title>
            <link>http://www.medworm.com/index.php?rid=5157451&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21853411%26dopt%3DAbstract</link>
            <description>Authors: Li DC, Yang F, Lu B, Chen DF, Yang WJ
    Abstract
    Small heat shock proteins are ubiquitous in all three domains (Archaea, Bacteria and Eukarya) and possess molecular chaperone activity by binding to unfolded polypeptides and preventing aggregation of proteins in vitro. The functions of a small heat shock protein (S.so-HSP20) from the hyperthermophilic archaeon, Sulfolobus solfataricus P2 have not been described. In the present study, we used real-time polymerase chain reaction analysis to measure mRNA expression of S.so-HSP20 in S. solfataricus P2 and found that it was induced by temperatures that were substantially lower (60°C) or higher (80°C) than the optimal temperature for S. solfataricus P2 (75°C). The expression of S.so-HSP20 mRNA was also up-regulated by cold shock...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5157451</comments>
            <pubDate>Fri, 19 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5157451</guid>        </item>
        <item>
            <title>Recombinant human Hsp70 protects against lipoteichoic acid-induced inflammation manifestations at the cellular and organismal levels.</title>
            <link>http://www.medworm.com/index.php?rid=5141588&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21845530%26dopt%3DAbstract</link>
            <description>In this study, we demonstrated that preconditioning with human recombinant Hsp70 ameliorates various manifestations of systematic inflammation, including reactive oxygen species, TNFα, and CD11b/CD18 adhesion receptor expression induction observed in different myeloid cells after LTA addition. Therefore, exogenous Hsp70 may provide a mechanism for controlling excessive inflammatory responses after macrophage activation. Furthermore, in a rat model of LTA-induced sepsis, we demonstrated that prophylactic administration of exogenous human Hsp70 significantly exacerbated numerous homeostatic and hemodynamic disturbances induced by LTA challenge and partially normalized the coagulation system and multiple biochemical blood parameters, including albumin and bilirubin concentrations, which were...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141588</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141588</guid>        </item>
        <item>
            <title>Cloning of the heat shock protein 90 and 70 genes from the beet armyworm, Spodoptera exigua, and expression characteristics in relation to thermal stress and development.</title>
            <link>http://www.medworm.com/index.php?rid=5141589&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21842334%26dopt%3DAbstract</link>
            <description>Authors: Jiang X, Zhai H, Wang L, Luo L, Sappington TW, Zhang L
    Abstract
    Two full-length cDNAs of heat shock protein (HSP) genes (Se-hsp90 and Se-hsp70) were cloned from the beet armyworm, Spodoptera exigua, and their expression was investigated in relation to cold shock, heat shock, and development. The open reading frames of Se-hsp90 and Se-hsp70 are 2,154 and 2,004 bp in length, encoding polypeptides of 717 and 667 amino acids with a molecular mass of 82.6 and 72.5 kDa, respectively. Both genes showed high similarity to their counterparts in other species. Transcriptional expression profiles revealed that both genes were significantly up-regulated under thermal stress. However, the temperature at which expression level became significantly higher than that of controls varied b...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141589</comments>
            <pubDate>Fri, 12 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141589</guid>        </item>
        <item>
            <title>Effects of chronic heat stress on the expressions of heat shock proteins 60, 70, 90, A2, and HSC70 in the rabbit testis.</title>
            <link>http://www.medworm.com/index.php?rid=5141590&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21830018%26dopt%3DAbstract</link>
            <description>The objective of this study was to investigate the effect of chronic high temperature-humidity index treatment on the expressions of HSP60, HSP70, HSP90, HSPA2 and HSC70, in the Rex rabbit testis and the expressions of these proteins after recovery from the chronic heat shock. Thirty mature male rabbits of the same age were randomly divided into three groups: control, heat stress, and recovery. The western blot results showed that the expressional levels of HSP60, HSP90, and HSC70 increased significantly and HSPA2 was elevated slightly after a 9-week heat treatment. HSP70 was absent in the control testis and had a high level of expression after heat stress. All of these proteins partially reverted back to normal levels after a 9-week recovery. The immunohistochemical results indicated that...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141590</comments>
            <pubDate>Tue, 09 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141590</guid>        </item>
        <item>
            <title>Role of Streptococcus intermedius DnaK chaperone system in stress tolerance and pathogenicity.</title>
            <link>http://www.medworm.com/index.php?rid=5141591&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21822788%26dopt%3DAbstract</link>
            <description>Authors: Tomoyasu T, Tabata A, Imaki H, Tsuruno K, Miyazaki A, Sonomoto K, Whiley RA, Nagamune H
    Abstract
    Streptococcus intermedius is a facultatively anaerobic, opportunistic pathogen that causes purulent infections and abscess formation. The DnaK chaperone system has been characterized in several pathogenic bacteria and seems to have important functions in stress resistance and pathogenicity. However, the role of DnaK in S. intermedius remains unclear. Therefore, we constructed a dnaK knockout mutant that exhibited slow growth, thermosensitivity, accumulation of GroEL in the cell, and reduced cytotoxicity to HepG2 cells. The level of secretion of a major pathogenic factor, intermedilysin, was not affected by dnaK mutation. We further examined the function and property of the S. i...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141591</comments>
            <pubDate>Fri, 05 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141591</guid>        </item>
        <item>
            <title>Reactivation of protein aggregates by mortalin and Tid1-the human mitochondrial Hsp70 chaperone system.</title>
            <link>http://www.medworm.com/index.php?rid=5103933&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21811887%26dopt%3DAbstract</link>
            <description>Authors: Iosefson O, Sharon S, Goloubinoff P, Azem A
    The mitochondrial 70-kDa heat shock protein (mtHsp70), also known in humans as mortalin, is a central component of the mitochondrial protein import motor and plays a key role in the folding of matrix-localized mitochondrial proteins. MtHsp70 is assisted by a member of the 40-kDa heat shock protein co-chaperone family named Tid1 and a nucleotide exchange factor. Whereas, yeast mtHsp70 has been extensively studied in the context of protein import in the mitochondria, and the bacterial 70-kDa heat shock protein was recently shown to act as an ATP-fuelled unfolding enzyme capable of detoxifying stably misfolded polypeptides into harmless natively refolded proteins, little is known about the molecular functions of the human mortalin in pr...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5103933</comments>
            <pubDate>Tue, 02 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5103933</guid>        </item>
        <item>
            <title>Eleven days of moderate exercise and heat exposure induces acclimation without significant HSP70 and apoptosis responses of lymphocytes in college-aged males.</title>
            <link>http://www.medworm.com/index.php?rid=5103934&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21796498%26dopt%3DAbstract</link>
            <description>Authors: Hom LL, Lee EC, Apicella JM, Wallace SD, Emmanuel H, Klau JF, Poh PY, Marzano S, Armstrong LE, Casa DJ, Maresh CM
    The purpose of this study was to assess whether a lymphocyte heat shock response and altered heat tolerance to ex vivo heat shock is evident during acclimation. We aimed to use flow cytometry to assess the CD3(+)CD4(+) T lymphocyte cell subset. We further aimed to induce acclimation using moderately stressful daily exercise-heat exposures to achieve acclimation. Eleven healthy males underwent 11 days of heat acclimation. Subjects walked for 90 min (50 ± 8% VO(2max)) on a treadmill (3.5 mph, 5% grade), in an environmental chamber (33°C, 30-50% relative humidity). Rectal temperature (°C), heart rate (in beats per minute), rating of perceived exertion , ther...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5103934</comments>
            <pubDate>Wed, 27 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5103934</guid>        </item>
        <item>
            <title>High-dose green tea polyphenols induce nephrotoxicity in dextran sulfate sodium-induced colitis mice by down-regulation of antioxidant enzymes and heat-shock protein expressions.</title>
            <link>http://www.medworm.com/index.php?rid=5058032&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21766215%26dopt%3DAbstract</link>
            <description>Authors: Inoue H, Akiyama S, Maeda-Yamamoto M, Nesumi A, Tanaka T, Murakami A
    Previously, we reported that oral feeding of 1% green tea polyphenols (GTPs) aggravated the dextran sulfate sodium (DSS)-induced colitis in mice. In the present study, we assessed the toxicity of 1% GTPs in several organs from normal and DSS-exposed mice. Sixty-two male ICR mice were initially divided into four groups. Non-treated group (group 1, n = 15) was given standard diet and water, GTPs (group 2, n = 15) received 1% GTPs in diet and water, DSS (group 3, n = 15) received diet and 5% DSS in water, and GTPs + DSS group (group 4, n = 17) received 1% GTPs in diet and 5% DSS in water. We found that group 4 significantly increased (P &amp;lt; 0.05) kidney weight, the levels of serum creatinine...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058032</comments>
            <pubDate>Fri, 15 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058032</guid>        </item>
        <item>
            <title>Metformin induced expression of Hsp60 in human THP-1 monocyte cells.</title>
            <link>http://www.medworm.com/index.php?rid=5058031&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21769504%26dopt%3DAbstract</link>
            <description>In this study, we demonstrate significant up-regulation of Hsp60 at both mRNA and protein levels when these cells were exposed to metformin at therapeutic dosage levels. Interestingly, there was also an increase in expression of CD14 mRNA in these cells. This suggested a possible modulation of the differentiation rates of the THP-1 cells during exposure to metformin. As monocyte differentiation marks a critical step in atherosclerosis, these observations suggest that long-term exposure to metformin could have important implications for the diabetic patient.
    PMID: 21769504 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058031</comments>
            <pubDate>Fri, 15 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058031</guid>        </item>
        <item>
            <title>Endoplasmic reticulum stress or mutation of an EF-hand Ca(2+)-binding domain directs the FKBP65 rotamase to an ERAD-based proteolysis.</title>
            <link>http://www.medworm.com/index.php?rid=5058033&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21761186%26dopt%3DAbstract</link>
            <description>Authors: Murphy LA, Ramirez EA, Trinh VT, Herman AM, Anderson VC, Brewster JL
    FKBP65 is an endoplasmic reticulum (ER)-localized chaperone and rotamase, with cargo proteins that include tropoelastin and collagen. In humans, mutations in FKBP65 have recently been shown to cause a form of osteogenesis imperfecta (OI), a brittle bone disease resulting from deficient secretion of mature type I collagen. In this work, we describe the rapid proteolysis of FKBP65 in response to ER stress signals that activate the release of ER Ca(2+) stores. A large-scale screen for stress-induced cellular changes revealed FKBP65 proteins to decrease within 6-12 h of stress activation. Inhibiting IP(3)R-mediated ER Ca(2+) release blocked this response. No other ER-localized chaperone and folding mediators ass...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058033</comments>
            <pubDate>Thu, 14 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058033</guid>        </item>
        <item>
            <title>Erratum to: Multiphoton ANS fluorescence microscopy as an in vivo sensor for protein misfolding stress.</title>
            <link>http://www.medworm.com/index.php?rid=5058034&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21755273%26dopt%3DAbstract</link>
            <description>Authors: Hadley KC, Borrelli MJ, Lepock JR, McLaurin J, Croul SE, Guha A, Chakrabartty A
    
    PMID: 21755273 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058034</comments>
            <pubDate>Wed, 13 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058034</guid>        </item>
        <item>
            <title>Detection of Hsp60 in saliva and serum from type 2 diabetic and non-diabetic control subjects.</title>
            <link>http://www.medworm.com/index.php?rid=5058036&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21748374%26dopt%3DAbstract</link>
            <description>In this study, we report the presence of elevated levels of Hsp60 in both saliva and serum of type 2 diabetic patients compared to non-diabetic controls. Hsp60 was detectable in the saliva of 10% of control and 93% of type 2 diabetic patients. Levels detected were in the range of 3-7 ng/ml in control and 3-75 ng/ml in type 2 diabetic patients. Serum Hsp60 levels in the range of 3-88 ng/ml were detected in 33% of control subjects, and levels in the range of 28-1,043 ng/ml were detected in 100% of type 2 diabetic patients. This is the first reporting of the presence of mitochondrial stress protein in salivary secretions. The serum Hsp60 levels were 16-fold higher compared to those in saliva, and there was a good positive correlation between salivary and serum Hsp60 levels (r = 0.55)....</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058036</comments>
            <pubDate>Tue, 12 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058036</guid>        </item>
        <item>
            <title>Erratum to: Rescuing of deficient killing and phagocytic activities of macrophages derived from non-obese diabetic mice by treatment with geldanamycin or heat shock: potential clinical implications.</title>
            <link>http://www.medworm.com/index.php?rid=5058035&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21748375%26dopt%3DAbstract</link>
            <description>Authors: Vega VL, Charles W, Crotty Alexander LE
    
    PMID: 21748375 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5058035</comments>
            <pubDate>Mon, 11 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5058035</guid>        </item>
        <item>
            <title>Erratum to: Increased heat shock protein 70 levels in induced sputum and plasma correlate with severity of asthma patients.</title>
            <link>http://www.medworm.com/index.php?rid=5009148&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21732132%26dopt%3DAbstract</link>
            <description>Authors: Hou C, Zhao H, Li W, Liang Z, Zhang D, Liu L, Tong W, Cai SX, Zou F
    
    PMID: 21732132 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009148</comments>
            <pubDate>Tue, 05 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009148</guid>        </item>
        <item>
            <title>Stress response gene activation protects sea urchin embryos exposed to X-rays.</title>
            <link>http://www.medworm.com/index.php?rid=5009149&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720812%26dopt%3DAbstract</link>
            <description>In conclusion, our findings confirm the sea urchin embryo as a sensible bioindicator of cell damage and we propose this model for studies on the protective pathways activated in response to X-rays. The novel result of the involvement of BAG3 and p63 in the response to X-rays, never tested so far in any other embryonic system, opens the way for their use as biomarkers of X-ray hazards.
    PMID: 21720812 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009149</comments>
            <pubDate>Thu, 30 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009149</guid>        </item>
        <item>
            <title>Studies on the protective effects of betaine against oxidative damage during experimentally induced restraint stress in Wistar albino rats.</title>
            <link>http://www.medworm.com/index.php?rid=5009151&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21717086%26dopt%3DAbstract</link>
            <description>Authors: Ganesan B, Anandan R, Lakshmanan PT
    Stress can be defined as physical and psychological modifications that disrupt the homeostasis and the balance of organisms. Stress is known as one of the most important reasons of several diseases. In the present study, the anti-stress effect of betaine was evaluated with reference to its antioxidant property. Wistar albino rats were divided into four groups such as control, betaine, restraint stress (6 h/day for 30 days), and betaine + restraint stress. The oxidative damage was assessed by measuring the protein and corticosterone in plasma, lipid peroxidation, non-enzymic (reduced glutathione), and enzymic antioxidants (glutathione peroxidase, glutathione-S-transferase, catalase, and superoxide dismutase) in the lymphoid organs of th...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009151</comments>
            <pubDate>Wed, 29 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009151</guid>        </item>
        <item>
            <title>A cell model to study different degrees of Hsp60 deficiency in HEK293 cells.</title>
            <link>http://www.medworm.com/index.php?rid=5009150&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21717087%26dopt%3DAbstract</link>
            <description>Authors: Bie AS, Palmfeldt J, Hansen J, Christensen R, Gregersen N, Corydon TJ, Bross P
    Mitochondrial dysfunction is associated with neurodegenerative diseases and mutations in the HSPD1 gene, encoding the mitochondrial Hsp60 chaperone, are the causative factors of two neurodegenerative diseases, hereditary spastic paraplegia and MitChap60 disease. In cooperation with Hsp10, Hsp60 forms a barrel-shaped complex, which encloses unfolded polypeptides and provides an environment facilitating folding. We have generated an Hsp60 variant with a mutation (Asp423Ala) in the ATPase domain and established a stable human embryonic kidney (HEK293) cell line allowing tetracycline-controlled expression of this mutant variant. We monitored expression of the Hsp60-Asp423Ala variant protein following in...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009150</comments>
            <pubDate>Wed, 29 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009150</guid>        </item>
        <item>
            <title>Chaperonin containing T-complex polypeptide (CCT) subunit expression in oral mucosal wounds and fibroblasts.</title>
            <link>http://www.medworm.com/index.php?rid=5009152&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21710295%26dopt%3DAbstract</link>
            <description>Authors: Satish L, Lo N, Gallo PH, Johnson S, Haberman S, Kathju S
    Mucosal wound healing in adults has been reported to feature diminished scar formation compared to healing skin wounds. We sought to determine if the expression pattern of chaperonin containing T-complex polypeptide (CCT) subunits in mucosal wounds and fibroblasts is different from that observed in skin wounds and fibroblasts. We found that CCT-beta is the only subunit message to be reduced in wounded mucosa versus unwounded control, and this reduction was confirmed at the protein level. In contrast, mRNA levels of CCT-zeta, -delta, -eta, and -epsilon were significantly increased in mucosal wounds. The increase in CCT-eta was also confirmed at the protein level. Expression levels of CCT-alpha, -beta, -delta; -epsilon, a...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009152</comments>
            <pubDate>Mon, 27 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009152</guid>        </item>
        <item>
            <title>Heat-shock response and antioxidant defense during air exposure in Patagonian shallow-water limpets from different climatic habitats.</title>
            <link>http://www.medworm.com/index.php?rid=4961685&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21671159%26dopt%3DAbstract</link>
            <description>Authors: Pöhlmann K, Koenigstein S, Alter K, Abele D, Held C
    Climate warming involves not only a rise of air temperature means, but also more frequent heat waves in many regions on earth, and is predicted to intensify physiological stress especially in extremely changeable habitats like the intertidal. We investigated the heat-shock response (HSR) and enzymatic antioxidant defense levels of Patagonian shallow-water limpets, adapted to distinct tidal exposure conditions in the sub- and intertidal. Limpets were sampled in the temperate Northern Patagonia and the subpolar Magellan region. Expression levels of two Hsp70 genes and activities of the antioxidants superoxide dismutase (SOD) and catalase (CAT) were measured in submerged and 2- and 12-h air-exposed specimens. Air-exposed Patago...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961685</comments>
            <pubDate>Mon, 13 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961685</guid>        </item>
        <item>
            <title>Predicting the functionally distinct residues in the heme, cation, and substrate-binding sites of peroxidase from stress-tolerant mangrove specie, Avicennia marina.</title>
            <link>http://www.medworm.com/index.php?rid=4961686&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21660646%26dopt%3DAbstract</link>
            <description>Authors: Jabeen U, Abbasi A, Salim A
    Recent work was conducted to predict the structure of functionally distinct regions of Avicennia marina peroxidase (AP) by using the structural coordinates of barley grains peroxidase as the template. This enzyme is utilized by all living organisms in many biosynthetic or degradable processes and in defense against oxidative stress. The homology model showed some distinct structural changes in the heme, calcium, and substrate-binding regions. Val53 was found to be an important coordinating residue between distal calcium ion and the distal heme site while Ser176 is coordinated to the proximal histidine through Ala174 and Leu172. Different ionic and hydrogen-bonded interactions were also observed in AP. Analyses of various substrate-enzyme interaction...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4961686</comments>
            <pubDate>Thu, 09 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4961686</guid>        </item>
        <item>
            <title>Increased heat shock protein 70 levels in induced sputum and plasma correlate with severity of asthma patients.</title>
            <link>http://www.medworm.com/index.php?rid=4912701&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21643870%26dopt%3DAbstract</link>
            <description>In conclusion, this study indicates that induced sputum and plasma HSP70 could serve as a useful marker for assessing the degree of airway obstruction in patients with asthma. However, further investigation is needed to establish the role of circulating and sputum HSP70 in the pathogenesis of asthma.
    PMID: 21643870 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4912701</comments>
            <pubDate>Fri, 03 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4912701</guid>        </item>
        <item>
            <title>Rescuing of deficient killing and phagocytic activities of macrophages derived from non-obese diabetic mice by treatment with geldanamycin or heat shock: potential clinical implications.</title>
            <link>http://www.medworm.com/index.php?rid=4912708&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21626279%26dopt%3DAbstract</link>
            <description>Authors: Vega VL, Charles W, Alexander LE
    Diabetes mellitus type 1 (DMT1) is an autoimmune disease characterized by the destruction of insulin-producing cells in the pancreas. Diabetic patients are more susceptible to recurrent and uncontrolled infections, with worse prognoses than in healthy individuals. Macrophages (Mϕs) derived from DMT1 individuals have compromised mounting of inflammatory and immune responses. The mechanisms responsible for these alterations remain unknown. It has been shown that the presence of extra- and intracellular heat shock proteins (hsp) positively modulates immune cell function. Using naive Mϕs derived from non-obese diabetic (NOD) mice, a well-established mouse model for DMT1, we demonstrate that heat shock (HS) as well as treatment with geldanamycin (...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4912708</comments>
            <pubDate>Sat, 28 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4912708</guid>        </item>
        <item>
            <title>Transcription of the Hsp30, Hsp70, and Hsp90 heat shock protein genes is modulated by the PalA protein in response to acid pH-sensing in the fungus Aspergillus nidulans.</title>
            <link>http://www.medworm.com/index.php?rid=4813152&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21553327%26dopt%3DAbstract</link>
            <description>In this study, we show that the Aspergillus nidulans hsp30 (ANID_03555.1), hsp70 (ANID_05129.1), and hsp90 (ANID_08269.1) genes are preferentially expressed in an acidic milieu, whose expression is dependent on the palA (+) background under optimal temperature for fungal growth. Heat shock induction of these three hsp genes showed different patterns in response to extracellular pH changes in the palA(+) background. However, their accumulation upon heating for 2 h was almost unaffected by ambient pH changes in the palA (-) background. The PalA protein is a member of a conserved signaling cascade that is involved in the pH-mediated regulation of gene expression. Moreover, we identified several genes whose expression at pH 5.0 is also dependent on the palA (+) background. These results reve...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4813152</comments>
            <pubDate>Sat, 07 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4813152</guid>        </item>
        <item>
            <title>The protective role of 5-hydroxymethyl-2-furfural (5-HMF) against acute hypobaric hypoxia.</title>
            <link>http://www.medworm.com/index.php?rid=4813153&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21494793%26dopt%3DAbstract</link>
            <description>Authors: Li MM, Wu LY, Zhao T, Wu KW, Xiong L, Zhu LL, Fan M
    Our previous study showed that pretreatment with 5-hydroxymethyl-2-furfural (5-HMF) led to protection against hypoxic injury via a p-ERK-mediated pathway in vitro. Whether the protection of 5-HMF against hypoxia is effective in vivo is unknown. The present study is aimed to verify the role of 5-HMF in acute hypobaric hypoxia using Kunming mice as an in vivo model and further investigate the underlying mechanisms. Mice pretreated with or without 5-HMF for 1 h were exposed to acute hypobaric hypoxic condition for 6 h and then the survival time, the survival rate, the permeability of blood-brain barrier (BBB), the histological analysis in hippocampus and cortex, and the phosphorylation level of mitogen-activated protein kinase...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4813153</comments>
            <pubDate>Thu, 14 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4813153</guid>        </item>
        <item>
            <title>Multiphoton ANS fluorescence microscopy as an in vivo sensor for protein misfolding stress.</title>
            <link>http://www.medworm.com/index.php?rid=4705811&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484286%26dopt%3DAbstract</link>
            <description>Authors: Hadley KC, Borrelli MJ, Lepock JR, McLaurin J, Croul SE, Guha A, Chakrabartty A
    The inability of cells to maintain protein folding homeostasis is implicated in the development of neurodegenerative diseases, malignant transformation, and aging. We find that multiphoton fluorescence imaging of 1-anilinonaphthalene-8-sulfonate (ANS) can be used to assess cellular responses to protein misfolding stresses. ANS is relatively nontoxic and enters live cells and cells or tissues fixed in formalin. In an animal model of Alzheimer's disease, ANS fluorescence imaging of brain tissue sections reveals the binding of ANS to fibrillar deposits of amyloid peptide (Aβ) in amyloid plaques and in cerebrovascular amyloid. ANS imaging also highlights non-amyloid deposits of glial fibrillary acidic...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4705811</comments>
            <pubDate>Mon, 11 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4705811</guid>        </item>
        <item>
            <title>Cholesterol induces pancreatic β cell apoptosis through oxidative stress pathway.</title>
            <link>http://www.medworm.com/index.php?rid=4705812&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21472505%26dopt%3DAbstract</link>
            <description>Authors: Lu X, Liu J, Hou F, Liu Z, Cao X, Seo H, Gao B
    Type 2 diabetes is often associated with high blood cholesterol. Here, we investigated the effect of cholesterol loading on MIN6 cells derived from pancreatic β cells. Exposure of MIN6 cells to cholesterol-induced apoptosis in time- and dose-dependent manner. Treatment with methyl-β-cyclodextrin that removes cholesterol from plasma membrane prevented the cells from cholesterol-induced apoptosis. Western blot analysis revealed that the levels of phosphorylated-p38 mitogen-activated protein kinase (P-p38 MAPK) and c-Jun N-terminal kinases (P-JNK) were significantly increased after the cholesterol loading, suggesting that the stress-activated protein kinase signaling was stimulated. A specific p38 inhibitor rescued MIN6 cells from ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4705812</comments>
            <pubDate>Wed, 06 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4705812</guid>        </item>
        <item>
            <title>The molecular characterization and expression of heat shock protein 90 (Hsp90) and 26 (Hsp26) cDNAs in sea cucumber (Apostichopus japonicus).</title>
            <link>http://www.medworm.com/index.php?rid=4705810&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484287%26dopt%3DAbstract</link>
            <description>Authors: Zhao H, Yang H, Zhao H, Chen M, Wang T
    The heat shock proteins (HSPs) are a family of proteins whose expression is enhanced in response to environmental stressors. The Apostichopus japonicus hsp90 and hsp26 genes were cloned using expressed sequence tag and rapid amplification of cDNA ends techniques. The full-length cDNA of Aphsp90 and Aphsp26 contains 3,458 and 1,688 nucleotides encoding 720 and 236 amino acids, respectively. Multiple alignments indicated that the deduced amino acid sequences of ApHsp90 and ApHsp26 shared a high level of identity with Hsp90 and small SHPs (sHSPs) sequences of zebrafish, ant, acorn worms, etc., and shared identical structural features with Hsp90 and sHSPs. The expression profiles of these two genes under heat treatment were investigated by re...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4705810</comments>
            <pubDate>Wed, 06 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4705810</guid>        </item>
        <item>
            <title>Heat shock proteins in stabilization of spontaneously restored sinus rhythm in permanent atrial fibrillation patients after mitral valve surgery.</title>
            <link>http://www.medworm.com/index.php?rid=4705813&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21455828%26dopt%3DAbstract</link>
            <description>Authors: Cao H, Xue L, Xu X, Wu Y, Zhu J, Chen L, Chen D, Chen Y
    A spontaneously restored sinus rhythm in permanent atrial fibrillation patients has been often observed after mitral valve (MV) surgery, but persisting duration in sinus rhythm varies from patient to patient. Heat shock proteins (Hsps) may be involved in pathogenesis of atrial fibrillation. We hypothesized that stabilization of restored sinus rhythm is associated with expression of Hsps in the atria. To test this hypothesis, clinical data, biopsies of right atrial appendage, and blood samples were collected from 135 atrial fibrillation patients who spontaneously restored sinus rhythm after conventional isolated MV replacement. Comparison was made between patients who had recurrence of atrial fibrillation within 7 days (A...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4705813</comments>
            <pubDate>Thu, 31 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4705813</guid>        </item>
        <item>
            <title>Theiler's murine encephalomyelitis virus infection induces a redistribution of heat shock proteins 70 and 90 in BHK-21 cells, and is inhibited by novobiocin and geldanamycin.</title>
            <link>http://www.medworm.com/index.php?rid=4705814&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21445704%26dopt%3DAbstract</link>
            <description>This study investigated the localisation of Hsps 70 and 90 in TMEV-infected BHK-21 cells by indirect immunofluorescence and confocal microscopy. The effect of Hsp90 inhibitors novobiocin (Nov) and geldanamycin (GA) on the development of cytopathic effect (CPE) induced by infection was also examined. Hsp90 staining was uniformly distributed in the cytoplasm of uninfected cells but was found concentrated in the perinuclear region during late infection where it overlapped with the signal for non-structural protein 2C within the viral replication complex. Hsp70 redistributed into the vicinity of the viral replication complex during late infection, but its distribution did not overlap with that of 2C. Inhibition of Hsp90 by GA and Nov had a negative effect on virus growth over a 48-h period as ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4705814</comments>
            <pubDate>Mon, 28 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4705814</guid>        </item>
        <item>
            <title>Elevated serum levels of heat shock protein 70 can be detected after radiofrequency ablation.</title>
            <link>http://www.medworm.com/index.php?rid=4649091&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21442384%26dopt%3DAbstract</link>
            <description>In this study, we evaluated the release of heat shock protein 70 into the serum of cancer-bearing patients directly after radiofrequency ablation. Sera of 22 patients undergoing radiofrequency ablation for the treatment of primary and secondary malignancies of the liver, kidney, and lung, as well as control sera of 20 patients undergoing diagnostic liver biopsy were analyzed using a manufactured heat shock protein 70 ELISA. A significant increase in serum levels of heat shock protein 70 was detectable in the patient cohort 1 day after radiofrequency ablation. More than a twofold increase was observed in nine out of 22 patients, which tended to correlate with favorable clinical outcome. No patient of the control group revealed a comparable increase. Radiofrequency ablation can lead to a re...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4649091</comments>
            <pubDate>Sat, 26 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4649091</guid>        </item>
        <item>
            <title>Cholesterol-derived bile acids enhance the chaperone activity of α-crystallins.</title>
            <link>http://www.medworm.com/index.php?rid=4582622&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21380614%26dopt%3DAbstract</link>
            <description>Authors: Song S, Liang JJ, Mulhern ML, Madson CJ, Shinohara T
    Human lens membranes contain the highest cholesterol concentration of any known biological membranes, but it significantly decreases with age. Oxygenation of cholesterol generates numerous forms of oxysterols (bile acids). We previously showed that two forms of the bile acid components-ursodeoxycholic acid (UDCA) and tauroursodeoxycholic acid (TUDCA)-suppressed lens epithelial cell death and alleviated cataract formation in galactosemic rat lenses. We investigated whether these compounds also suppress the thermal aggregation of human lens crystallins. Total water-soluble (WS) proteins were prepared from human lenses, and recombinant human crystallins (αA-, αB-, βB2-, and γC-crystallin) were generated by a prokaryotic exp...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4582622</comments>
            <pubDate>Sun, 06 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4582622</guid>        </item>
        <item>
            <title>Comparison of adjuvant activity of N- and C-terminal domain of gp96 in a Her2-positive breast cancer model.</title>
            <link>http://www.medworm.com/index.php?rid=4582623&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21359667%26dopt%3DAbstract</link>
            <description>Authors: Pakravan N, Hassan ZM
    It has been frequently reported that gp96 acts as a strong biologic adjuvant. Some studies have even investigated adjuvant activity of the gp96 C- or N-terminal domain. The controversy surrounding adjuvant activity of gp96 terminal domains prompted us to compare adjuvant activity of gp96 C- or N-terminal domain toward Her2/neu, as DNA vaccine in a Her2/neu-positive breast cancer model. To do so, mice were immunized with DNA vaccine consisting of transmembrane and extracellular domain (TM + ECD) of rat Her2/neu alone or fused to N- or C-terminal domain of gp96. Treatment with Her2/neu fused to N-terminal domain of gp96 resulted in tumor progression, compared to the groups vaccinated with pCT/Her2 or pHer2. Immunological examination revealed that treatment ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4582623</comments>
            <pubDate>Sat, 26 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4582623</guid>        </item>
        <item>
            <title>Hsp-27 induction requires POU4F2/Brn-3b TF in doxorubicin-treated breast cancer cells, whereas phosphorylation alters its cellular localisation following drug treatment.</title>
            <link>http://www.medworm.com/index.php?rid=4474516&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21279488%26dopt%3DAbstract</link>
            <description>Authors: Fujita R, Ounzain S, Wang AC, Heads RJ, Budhram-Mahadeo VS
    POU4F2/Brn-3b transcription factor (referred to as Brn-3b) is elevated in &amp;gt;60% of breast cancers and profoundly alters growth and behaviour of cancer cells by regulating distinct subsets of target genes. Previous studies showed that Brn-3b was required to maximally transactivate small heat shock protein, HSPB1/Hsp-27 (referred to as Hsp-27), and consequently, Brn-3b expression correlated well with Hsp27 levels in human breast biopsies. In these studies, we showed that Brn-3b is increased in MCF7 breast cancer cells that survive following treatment with chemotherapeutic drug doxorubicin (Dox) with concomitant increases in Hsp-27 expression. Targeting of Brn-3b using short interfering RNA reduced Hsp-27 in Dox-treated...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4474516</comments>
            <pubDate>Sat, 29 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4474516</guid>        </item>
        <item>
            <title>Cellular thermotolerance is associated with heat shock protein 70.1 genetic polymorphisms in Holstein lactating cows.</title>
            <link>http://www.medworm.com/index.php?rid=4474518&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21274669%26dopt%3DAbstract</link>
            <description>In conclusion, exposure to HS differently affected cell viability and gene and protein expression of Hsp70.1 in the selected genotypes. These results indicate that the presence of SNPs (C/- and G/T) in the 5'-UTR region of inducible Hsp70.1 ameliorates HS response and tolerance to heat of bovine PBMC. These mutation sites may be useful as molecular genetic markers to assist selection for heat tolerance.
    PMID: 21274669 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4474518</comments>
            <pubDate>Fri, 28 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4474518</guid>        </item>
        <item>
            <title>Heat-shock protein 90 alpha (HSP90α) modulates signaling pathways towards tolerance of oxidative stress and enhanced survival of hepatocytes of Mugil cephalus.</title>
            <link>http://www.medworm.com/index.php?rid=4474517&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21274670%26dopt%3DAbstract</link>
            <description>Authors: Padmini E, Usha Rani M
    Oxidative stress causes damage at the cellular level and activates a number of signaling pathways. Earlier, we have demonstrated that pollutant-related oxidative stress upregulates heat-shock protein 90 alpha (HSP90α) against stress insult in hepatocytes of Mugil cephalus living in a polluted estuary. However, the impact of pollution-induced HSP90α upregulation on stress tolerance is not clear. Here we propose that the effect of stress resistance depends on the ability of HSP90α to modulate the signaling pathways involving proteins such as apoptosis signal-regulating kinase 1, c-Jun NH(2)-terminal protein kinase 1/2, signal transducers and activators of transcription, extracellular signal-regulated kinase 1/2, protein kinase B, nuclear factor-kappa bi...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4474517</comments>
            <pubDate>Fri, 28 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4474517</guid>        </item>
        <item>
            <title>Single-point mutation in a conserved TPR domain of Hip disrupts enhancement of glucocorticoid receptor signaling.</title>
            <link>http://www.medworm.com/index.php?rid=4411774&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21240662%26dopt%3DAbstract</link>
            <description>In this study, a cDNA for human Hip was used in mutational analysis to map Hip function to critical structural elements. A single amino acid substitution (L211S) resulted in a loss of Hip function. This mutation also appears to disrupt the interaction of Hip with Hsp70 in vitro. Failure to recover Hip-L211S constructs in co-immunoprecipitation assays with an Hsp70 monoclonal antibody suggests that the mutation is unlikely to result in a misfolded substrate.
    PMID: 21240662 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411774</comments>
            <pubDate>Sun, 16 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411774</guid>        </item>
        <item>
            <title>Proteome profiling of heat shock of human primary breast epithelial cells, a dataset report.</title>
            <link>http://www.medworm.com/index.php?rid=4343836&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21221872%26dopt%3DAbstract</link>
            <description>Authors: Jia M, Souchelnytskyi S
    Exposure to elevated temperatures has a strong effect on cell functions, and is used in clinical practice. Hyperthermia may affect multiple regulatory mechanisms in cells. To understand better the response to hyperthermia of immortalized primary human breast epithelial cells, we performed a proteomics study of these cells cultured at 34°C or 39°C. Twenty-four proteins were shown to be differentially expressed due to hyperthermia. Analysis of these proteins showed the potential involvement of various biological processes in response to hyperthermia, e.g., cell adhesion, cell communication, and cell cycle. Transforming growth factor-β2 (TGF-β2) and heat shock protein 27 (HSP27) were found to be upregulated at 39°C. TGF-β2 was found to affect express...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4343836</comments>
            <pubDate>Tue, 11 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4343836</guid>        </item>
        <item>
            <title>Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock.</title>
            <link>http://www.medworm.com/index.php?rid=4343837&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21191678%26dopt%3DAbstract</link>
            <description>Authors: Botha M, Chiang AN, Needham PG, Stephens LL, Hoppe HC, Külzer S, Przyborski JM, Lingelbach K, Wipf P, Brodsky JL, Shonhai A, Blatch GL
    Heat shock protein 70 (Hsp70) and heat shock protein 40 (Hsp40) function as molecular chaperones during the folding and trafficking of proteins within most cell types. However, the Hsp70-Hsp40 chaperone partnerships within the malaria parasite, Plasmodium falciparum, have not been elucidated. Only one of the 43 P. falciparum Hsp40s is predicted to be a cytosolic, canonical Hsp40 (termed PfHsp40) capable of interacting with the major cytosolic P. falciparum-encoded Hsp70, PfHsp70. Consistent with this hypothesis, we found that PfHsp40 is upregulated under heat shock conditions in a similar pattern to PfHsp70. In addition, PfHsp70 and PfHsp40 re...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4343837</comments>
            <pubDate>Thu, 30 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4343837</guid>        </item>
        <item>
            <title>Heat shock proteins in porcine ovary: synthesis, accumulation and regulation by stress and hormones.</title>
            <link>http://www.medworm.com/index.php?rid=4343840&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21188661%26dopt%3DAbstract</link>
            <description>We examined (1) whether HSP70.2, HSP72 and HSP105/110 can be produced and accumulated in porcine ovarian tissue, (2) whether these HSPs could be indicators of stress, i.e. whether two kinds of stress (high temperatures and malnutrition/serum deprivation) can affect them, and (3) whether some hormonal regulators of ovarian functions (insulin-like growth factor (IGF)-I, leptin and follicle-stimulating hormone (FSH)) can affect these HSPs and response of ovaries to HSP-related stress. We analysed the expression of HSP70.2, HSP72 and HSP105/110 mRNA (by using real-time reverse transcriptase polymerase chain reaction) in porcine ovarian granulosa cells, as well as the accumulation of HSP70 protein (by using sodium dodecyl sulphate polyacrylamide gel electrophoresis-Western) in either whole ovar...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4343840</comments>
            <pubDate>Tue, 28 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4343840</guid>        </item>
        <item>
            <title>Thermotolerance and hsp70 heat shock response in the cold-stenothermal chironomid Pseudodiamesa branickii (NE Italy).</title>
            <link>http://www.medworm.com/index.php?rid=4343839&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21188662%26dopt%3DAbstract</link>
            <description>Authors: Bernabò P, Rebecchi L, Jousson O, Martínez-Guitarte JL, Lencioni V
    To better understand the physiological capability of cold-stenothermal organisms to survive high-temperature stress, we analyzed the thermotolerance limits and the expression level of hsp70 genes under temperature stress in the alpine midge Pseudodiamesa branickii (Diptera Chironomidae). A lethal temperature (LT(100)) of 36°C and a lethal temperature 50% (LT(50)) of 32.2°C were found for the cold-stenothermal larvae after short-term shocks (1 h). Additional experiments revealed that the duration of the exposure negatively influenced survival, whereas a prior exposure to a less severe high temperature generated an increase in survival. To investigate the molecular basis of this high thermotolerance, the exp...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4343839</comments>
            <pubDate>Tue, 28 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4343839</guid>        </item>
        <item>
            <title>Effect of cigarette smoke and dexamethasone on Hsp72 system of alveolar epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=4343838&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21188663%26dopt%3DAbstract</link>
            <description>Authors: Gál K, Cseh A, Szalay B, Rusai K, Vannay A, Lukácsovits J, Heemann U, Szabó AJ, Losonczy G, Tamási L, Müller V
    Smoking is the leading risk factor of chronic obstructive pulmonary disease (COPD) and lung cancer. Corticosteroids are abundantly used in these patients; however, the interaction of smoking and steroid treatment is not fully understood. Heat shock proteins (Hsps) play a central role in the maintenance of cell integrity, apoptosis and cellular steroid action. To better understand cigarette smoke-steroid interaction, we examined the effect of cigarette smoke extract (CSE) and/or dexamethasone (DEX) on changes of intracellular heat shock protein-72 (Hsp72) in lung cells. Alveolar epithelial cells (A549) were exposed to increasing doses (0; 0.1; 1; and 10 μM/μl) ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4343838</comments>
            <pubDate>Tue, 28 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4343838</guid>        </item>
        <item>
            <title>Distinguishing integral and receptor-bound heat shock protein 70 (Hsp70) on the cell surface by Hsp70-specific antibodies.</title>
            <link>http://www.medworm.com/index.php?rid=4343841&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21165727%26dopt%3DAbstract</link>
            <description>Authors: Multhoff G, Hightower LE
    Cell Stress &amp; Chaperones journal has become a major outlet for papers and review articles about anti-heat shock protein (HSP) antibodies. In the last decade, it became evident that apart from their intracellular localization, members of the heat shock protein 90 (Hsp90; HSPC) and Hsp70 (HSPA) family are also found on the cell surface. In this review, we will focus on Hsp70 (HSPA1A), the major stress-inducible member of the human Hsp70 family. Depending on the cell type, the membrane association of Hsp70 comes in two forms. In tumor cells, Hsp70 appears to be integrated within the plasma membrane, whereas in non-malignantly transformed (herein termed normal) cells, Hsp70 is associated with cell surface receptors. This observation raises the question...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4343841</comments>
            <pubDate>Fri, 17 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4343841</guid>        </item>
        <item>
            <title>Versatile TPR domains accommodate different modes of target protein recognition and function.</title>
            <link>http://www.medworm.com/index.php?rid=4343842&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21153002%26dopt%3DAbstract</link>
            <description>Authors: Allan RK, Ratajczak T
    The tetratricopeptide repeat (TPR) motif is one of many repeat motifs that form structural domains in proteins that can act as interaction scaffolds in the formation of multi-protein complexes involved in numerous cellular processes such as transcription, the cell cycle, protein translocation, protein degradation and host defence against invading pathogens. The crystal structures of many TPR domain-containing proteins have been determined, showing TPR motifs as two anti-parallel α-helices packed in tandem arrays to form a structure with an amphipathic groove which can bind a target peptide. This is however not the only mode of target recognition by TPR domains, with short amino acid insertions and alternative TPR motif conformations also shown to contrib...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4343842</comments>
            <pubDate>Thu, 09 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4343842</guid>        </item>
        <item>
            <title>The effect of hyperbaric oxygen preconditioning on heat shock protein 72 expression following in vitro stress in human monocytes.</title>
            <link>http://www.medworm.com/index.php?rid=4251960&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21132545%26dopt%3DAbstract</link>
            <description>Authors: Vince RV, Midgley AW, Laden G, Madden LA
    Hyperbaric oxygen (HBO) is thought to confer protection to cells via a cellular response to free radicals. This process may involve increased expression of heat shock proteins, in particular the highly inducible heat shock protein 72 (Hsp72). Healthy male volunteers (n = 16) were subjected to HBO for 1 h at 2.8 ATA. Inducible Hsp72 expression was measured by flow cytometry pre-, post- and 4 h-post HBO. Peripheral blood mononuclear cells (PBMC) were isolated from whole blood via density centrifugation pre-, post- and 4 h post-HBO. PBMC were then subjected to an in vitro heat shock at 40°C or hypoxia at 37°C (5% O(2)) with a control at 37°C. Cells were then analysed for Hsp72 expression by flow cytometry. Monocytes showed no si...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4251960</comments>
            <pubDate>Sun, 05 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4251960</guid>        </item>
        <item>
            <title>Salivary Hsp72 does not track exercise stress and caffeine-stimulated plasma Hsp72 responses in humans.</title>
            <link>http://www.medworm.com/index.php?rid=4251959&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21132546%26dopt%3DAbstract</link>
            <description>Authors: Fortes MB, Whitham M
    Heat shock protein 72 (Hsp72) has been detected within saliva, and its presence may contribute to oral defence. It is currently unknown how physiological stress affects salivary Hsp72 or if salivary Hsp72 concentrations reflect plasma Hsp72 concentrations. We studied the effect of exercise upon salivary Hsp72 expression, and using caffeine administration, investigated the role of sympathetic stimulation upon salivary Hsp72 expression. Six healthy males performed two treadmill running exercise bouts in hot conditions (30°C) separated by 1 week in a randomized cross-over design, one with caffeine supplementation (CAF) the other with placebo (PLA). Plasma and saliva samples were collected prior to, during and post-exercise and assayed for Hsp72 concentratio...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4251959</comments>
            <pubDate>Sun, 05 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4251959</guid>        </item>
        <item>
            <title>Effects of glucose-regulated protein94 (Grp94) on Ig secretion from human blood mononuclear cells.</title>
            <link>http://www.medworm.com/index.php?rid=4221449&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21120645%26dopt%3DAbstract</link>
            <description>Authors: Tramentozzi E, Zamarchi R, Pagetta A, Brunati AM, Rossi E, Tibaldi E, Finotti P
    Grp94 is the main endoplasmic reticulum-resident heat shock protein (HSP) that besides chaperoning native proteins, displays important modulatory effects on both the innate and adaptive immune response. Since the knowledge of a direct influence of Grp94 on the humoral response is lacking, in this work we tested the effect of Grp94 on Ig secretion from peripheral blood mononuclear cells (PBMCs) of five normal volunteers. The concentration of Ig secreted in the medium after incubation of 15 days was found increased in a dose-dependent manner in the presence of Grp94, used at the final concentrations of 10 and 100 ng/ml. However, by measuring the Ig secretion at different incubation times, it was ap...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4221449</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4221449</guid>        </item>
        <item>
            <title>Serum antibody titers against heat shock protein 27 are associated with the severity of coronary artery disease.</title>
            <link>http://www.medworm.com/index.php?rid=4202698&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21107776%26dopt%3DAbstract</link>
            <description>Authors: Pourghadamyari H, Moohebati M, Parizadeh SM, Falsoleiman H, Dehghani M, Fazlinezhad A, Akhlaghi S, Tavallaie S, Sahebkar A, Paydar R, Ghayour-Mobarhan M, Ferns GA
    Antibody titers to several heat shock proteins (anti-Hsps) have been reported to be associated with the severity and progression of cardiovascular disease. However, there are little data regarding anti-Hsp27 titers in patients with coronary artery disease (CAD). A total of 400 patients with suspected CAD were recruited. Based on the results of coronary angiography, these patients were classified into CAD(+) (n = 300) and CAD(-) (n = 100) groups defined as patients with ≥50% and &amp;lt;50% stenosis of any major coronary artery, respectively. Eighty-three healthy subjects were also recruited as the control g...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4202698</comments>
            <pubDate>Thu, 25 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4202698</guid>        </item>
        <item>
            <title>Functional switching of a novel prokaryotic 2-Cys peroxiredoxin (PpPrx) under oxidative stress.</title>
            <link>http://www.medworm.com/index.php?rid=4202699&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21104173%26dopt%3DAbstract</link>
            <description>Authors: An BC, Lee SS, Lee EM, Lee JT, Wi SG, Jung HS, Park W, Lee SY, Chung BY
    Many proteins have been isolated from eukaryotes as redox-sensitive proteins, but whether these proteins are present in prokaryotes is not clear. Redox-sensitive proteins contain disulfide bonds, and their enzymatic activity is modulated by redox in vivo. In the present study, we used thiol affinity purification and mass spectrometry to isolate and identify 19 disulfide-bond-containing proteins in Pseudomonas putida exposed to potential oxidative damages. Among these proteins, we found that a typical 2-Cys Prx-like protein (designated PpPrx) displays diversity in structure and apparent molecular weight (MW) and can act as both a peroxidase and a molecular chaperone. We also identified a regulatory factor i...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4202699</comments>
            <pubDate>Sun, 21 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4202699</guid>        </item>
        <item>
            <title>Lipopolysaccharide pretreatment protects against ischemia/reperfusion injury via increase of HSP70 and inhibition of NF-κB.</title>
            <link>http://www.medworm.com/index.php?rid=4187163&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21080136%26dopt%3DAbstract</link>
            <description>In this study, we pretreated rats with LPS (1.0 mg/kg) 24 h before they were subjected to I/R injury, and then examined the roles of heat shock protein-70 (HSP70) and nucleus factor-κB (NF-κB) in LPS-induced cardioprotection. We observed that pretreatment with low-dose LPS resulted in significantly increased levels of HSP70 in the myocardium, which could dramatically inhibit NF-κB translocation and reduce degradation of inhibitory κB. Inhibition of NF-κB, in turn, attenuated release of inflammatory cytokines (tumor necrosis factor-α, interleukin (IL)-1β, and IL-6) and reduced apoptosis of myocardium and infarct area following I/R injury. Moreover, HSP70 could ameliorate oxidative stress following I/R injury. To further investigate whether increase of HSP70 might be responsible for...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4187163</comments>
            <pubDate>Tue, 16 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4187163</guid>        </item>
        <item>
            <title>Response of mice to continuous 5-day passive hyperthermia resembles human heat acclimation.</title>
            <link>http://www.medworm.com/index.php?rid=4187162&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21080137%26dopt%3DAbstract</link>
            <description>This study suggests that continuous 5-day exposure of CD-1 mice to mild hyperthermia induces a state that resembles the physiologic and cellular responses of human HA. This model may be useful for analyzing the molecular mechanisms of HA and its consequences on host responsiveness to subsequent stresses.
    PMID: 21080137 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4187162</comments>
            <pubDate>Tue, 16 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4187162</guid>        </item>
        <item>
            <title>The protective role of 5-HMF against hypoxic injury.</title>
            <link>http://www.medworm.com/index.php?rid=4169186&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21057989%26dopt%3DAbstract</link>
            <description>Authors: Li MM, Wu LY, Zhao T, Xiong L, Huang X, Liu ZH, Fan XL, Xiao CR, Gao Y, Ma YB, Chen JJ, Zhu LL, Fan M
    In an attempt to find new types of anti-hypoxic agents from herbs, we identified 5-hydroxymethyl-2-furfural (5-HMF) as a natural agent that fulfills the criterion. 5-HMF, the final product of carbohydrate metabolism, has favorable biological effects such as anti-oxidant activity and inhibiting sickling of red blood cells. The role of 5-HMF in hypoxia, however, is not yet. Our pilot results showed that pretreatment with 5-HMF markedly increased both the survival time and the survival rate of mice under hypoxic stress. The present study was aimed to further investigate the protective role of 5-HMF and the underlying mechanisms in hypoxic injury using ECV304 cells as an in vitro ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4169186</comments>
            <pubDate>Sat, 06 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4169186</guid>        </item>
        <item>
            <title>Serum level of soluble Hsp70 is associated with vascular calcification.</title>
            <link>http://www.medworm.com/index.php?rid=4139956&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21046302%26dopt%3DAbstract</link>
            <description>Authors: Krepuska M, Szeberin Z, Sótonyi P, Sarkadi H, Fehérvári M, Apor A, Rimely E, Prohászka Z, Acsády G
    It has been previously reported that serum levels of 70-kDa heat shock protein (Hsp70) are elevated in peripheral artery disease. The aim of the present study was to examine whether increased serum Hsp70 levels are related to the extent of arterial calcification and standard laboratory parameters of patients with peripheral artery disease, as well as to markers of inflammation (C-reactive protein), atherosclerosis (homocysteine), and calcification (fetuin-a). One hundred eighty chronic atherosclerotic patients with significant carotid stenosis and/or lower extremity vascular disease were enrolled in this cross-sectional study. Systemic atherosclerosis and calcification was a...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4139956</comments>
            <pubDate>Wed, 03 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4139956</guid>        </item>
        <item>
            <title>HSFs and regulation of Hsp70.1 (Hspa1b) in oocytes and preimplantation embryos: new insights brought by transgenic and knockout mouse models.</title>
            <link>http://www.medworm.com/index.php?rid=4139955&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21053113%26dopt%3DAbstract</link>
            <description>Authors: Le Masson F, Elisabeth C
    Gene encoding heat shock protein (Hsps) are induced following a thermal stress thanks to the activation of heat shock transcription factor (HSF) which interacts with heat shock elements (HSE) located within the sequence of Hsp promoters. This cellular and protective response (heat shock response (HSR)) is well known and evolutionarily conserved. Nevertheless, HSR does not function in all the cells produced during the life of a multicellular organism, e.g., early mouse embryos. Taking advantage of mouse transgenic and knockout models, we investigated the roles of trans (HSF 1 and 2) and cis (HSE) regulatory elements in the control of Hsp70.1 (Hspa1b) through several developmental steps from oocytes to blastocysts. Our studies confirm that, even in absen...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4139955</comments>
            <pubDate>Sat, 30 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4139955</guid>        </item>
        <item>
            <title>Extracellular heat shock proteins, cellular export vesicles, and the Stress Observation System: A form of communication during injury, infection, and cell damage : It is never known how far a controversial finding will go! Dedicated to Ferruccio Ritossa.</title>
            <link>http://www.medworm.com/index.php?rid=4088891&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20963644%26dopt%3DAbstract</link>
            <description>Authors: De Maio A
    Heat shock proteins (hsp) have been found to play a fundamental role in the recovery from multiple stress conditions and to offer protection from subsequent insults. The function of hsp during stress goes beyond their intracellular localization and chaperone role as they have been detected outside cells activating signaling pathways. Extracellular hsp are likely to act as indicators of the stress conditions, priming other cells, particularly of the immune system, to avoid the propagation of the insult. Some extracellular hsp, for instance Hsp70, are associated with export vesicles, displaying a robust activation of macrophages. We have coined the term Stress Observation System (SOS) for the mechanism for sensing extracellular hsp, which we propose is a form of cellul...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088891</comments>
            <pubDate>Wed, 20 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088891</guid>        </item>
        <item>
            <title>Identification of peptide mimotopes of gp96 using single-chain antibody library.</title>
            <link>http://www.medworm.com/index.php?rid=4088892&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20953748%26dopt%3DAbstract</link>
            <description>Authors: Shanmugam A, Suriano R, Goswami N, Chaudhuri D, Ashok BT, Rajoria S, George AL, Mittelman A, Tiwari RK
    Heat shock proteins such as gp96 are immunogenic and are widely used as vaccines in immunotherapy of cancers. The present study focuses on the use of peptide mimotopes as immunotherapeutic vaccines for prostate cancer. To this end, we developed a 15-mer gp96 peptide mimotope specifically reactive to MAT-LyLu gp96-peptide complex using combinatorial single-chain antibody and peptide phage display library. The immunogenicity of the synthesized gp96 mimotope was analyzed initially in normal BALB/c mice in combination with various adjuvants such as complete Freund's adjuvant (CFA), aluminum salts (ALUM), granulocyte-macrophage colony-stimulating factor (GM-CSF), and liposome, of ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088892</comments>
            <pubDate>Fri, 15 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088892</guid>        </item>
        <item>
            <title>Antitumor activity of efrapeptins, alone or in combination with 2-deoxyglucose, in breast cancer in vitro and in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=4065653&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20927616%26dopt%3DAbstract</link>
            <description>Authors: Papathanassiu AE, Macdonald NJ, Emlet DR, Vu HA
    Efrapeptins (EF), a family of fungal peptides, inhibit proteasomal enzymatic activities and the in vitro and in vivo growth of HT-29 cells. They are also known inhibitors of F(1)F(0)-ATPase, a mitochondrial enzyme that functions as an Hsp90 co-chaperone. We have previously shown that treatment of cancer cells with EF results in disruption of the Hsp90:F(1)F(0)-ATPase complex and inhibition of Hsp90 chaperone activity. The present study examines the effect of EF on breast cancer growth in vitro and in vivo. As a monotherapy, EF inhibited cell proliferation in vitro with an IC(50) value ranging from 6 nM to 3.4 μM. Inhibition of Hsp90 chaperone function appeared to be the dominant mechanism of action and the factor determining c...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4065653</comments>
            <pubDate>Wed, 06 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4065653</guid>        </item>
        <item>
            <title>Impact of seropositivity to Chlamydia pneumoniae and anti-hHSP60 on cardiovascular events in hemodialysis patients.</title>
            <link>http://www.medworm.com/index.php?rid=4045657&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20922511%26dopt%3DAbstract</link>
            <description>In conclusion, our data suggest that anti-hHSP60 autoimmune response is not related to CP infection and CP-related CVD risk in HD patients.
    PMID: 20922511 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4045657</comments>
            <pubDate>Mon, 04 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4045657</guid>        </item>
        <item>
            <title>Increased stability of Bcl-2 in HSP70-mediated protection against apoptosis induced by oxidative stress.</title>
            <link>http://www.medworm.com/index.php?rid=4045658&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20890773%26dopt%3DAbstract</link>
            <description>Authors: Jiang B, Liang P, Deng G, Tu Z, Liu M, Xiao X
    We have previously shown that heat shock protein 70 (HSP70) markedly inhibits H(2)O(2)-induced apoptosis in mouse C2C12 myogenic cells by reducing the release of Smac. However, the molecular mechanism by which HSP70 interferes with Smac release during oxidative stress-induced apoptosis is not understood. In the current study, we showed that HSP70 increased the stability of Bcl-2 during oxidative stress. An antisense phosphorothioate oligonucleotide against Bcl-2 caused selective inhibition of Bcl-2 protein expression induced by HSP70 and significantly attenuated HSP70-mediated cell protection against H(2)O(2)-induced release of Smac and apoptosis. Taken together, our results indicate that there are important relationships among HSP...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4045658</comments>
            <pubDate>Sat, 02 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4045658</guid>        </item>
        <item>
            <title>Stress at the Korean Mountains: meeting report of the 8th International Workshop on the Molecular Biology of Stress Responses.</title>
            <link>http://www.medworm.com/index.php?rid=4045661&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20886326%26dopt%3DAbstract</link>
            <description>Authors: De Maio A, Tanguay RM, Kampinga H, Lee E, Kim CD, Hightower L
    South Korea is a country exemplified by a combination of upscale new technology and ancient mysticism. The busy streets of Seoul hustle and bustle like any large, active metropolis, yet the city's inhabitants radiate an intrinsic sense of peace, creating a timeless atmosphere. The combination of emerging technology and profound respect for the Korean culture and heritage makes this country a unique environment in which to organize a successful scientific meeting. Cell Stress Society International, in its quest to cross the cultural frontiers of science and propagate research on the stress response, partnered with the newly created Korean Cell Stress Society to hold the 8th International Workshop on the Molecular Bio...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4045661</comments>
            <pubDate>Fri, 01 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4045661</guid>        </item>
        <item>
            <title>Identification of in vivo HSP90-interacting proteins reveals modularity of HSP90 complexes is dependent on the environment in psychrophilic bacteria.</title>
            <link>http://www.medworm.com/index.php?rid=4045660&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20890740%26dopt%3DAbstract</link>
            <description>Authors: García-Descalzo L, Alcazar A, Baquero F, Cid C
    Heat shock protein 90 (HSP90) is a conserved molecular chaperone that functions as part of complexes in which different client proteins target it to diverse sets of substrates. In this paper, HSP90 complexes were investigated in γ-proteobacteria from mild (Shewanella oneidensis) and cold environments (Shewanella frigidimarina and Psychrobacter frigidicola), to determine changes in HSP90 interactions with client proteins in response to the adaptation to cold environments. HSP90 participation in cold adaptation was determined using the specific inhibitor 17-allylamino-geldanamycin. Then, HSP90 was immunoprecipitated from bacterial cultures, and the proteins in HSP90 complexes were analyzed by two-dimensional gel electrophoresis an...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4045660</comments>
            <pubDate>Fri, 01 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4045660</guid>        </item>
        <item>
            <title>Interactions between the actin filament capping and severing protein gelsolin and the molecular chaperone CCT: evidence for nonclassical substrate interactions.</title>
            <link>http://www.medworm.com/index.php?rid=4045659&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20890741%26dopt%3DAbstract</link>
            <description>Authors: Brackley KI, Grantham J
    CCT is a member of the chaperonin family of molecular chaperones and consists of eight distinct subunit species which occupy fixed positions within the chaperonin rings. The activity of CCT is closely linked to the integrity of the cytoskeleton as newly synthesized actin and tubulin monomers are dependent upon CCT to reach their native conformations. Furthermore, an additional role for CCT involving interactions with assembling/assembled microfilaments and microtubules is emerging. CCT is also known to interact with other proteins, only some of which will be genuine folding substrates. Here, we identify the actin filament remodeling protein gelsolin as a CCT-binding partner, and although it does not behave as a classical folding substrate, gelsolin bind...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4045659</comments>
            <pubDate>Fri, 01 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4045659</guid>        </item>
        <item>
            <title>The structural stability and chaperone activity of artemin, a ferritin homologue from diapause-destined Artemia embryos, depend on different cysteine residues.</title>
            <link>http://www.medworm.com/index.php?rid=4045662&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20878295%26dopt%3DAbstract</link>
            <description>In this study, cysteines 22, 61, 166, and 172 of artemin were substituted with alanines, respectively yielding ArtC22A, ArtC61A, ArtC166A, and ArtC172A. Wild-type and modified artemins were synthesized in transformed bacteria and purified. As measured by heat-induced denaturation of citrate synthase in vitro, each substitution reduced chaperone activity, with ArtC172A the least active. Protein modeling indicated that C172 is close to a region of surface hydrophobicity, also present in ferritin, suggesting that this site contributes to chaperone activity. Only slight differences in oligomer molecular mass were apparent between artemin variants, but ArtC22A and ArtC61A displayed significantly reduced thermostability, perhaps due to the disruption of an inter-subunit disulphide bridge. In con...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4045662</comments>
            <pubDate>Mon, 27 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4045662</guid>        </item>
        <item>
            <title>Serum heat shock protein 70 and oxidized LDL in patients with type 2 diabetes: does sex matter?</title>
            <link>http://www.medworm.com/index.php?rid=4010366&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20872261%26dopt%3DAbstract</link>
            <description>Authors: Nakhjavani M, Morteza A, Meysamie A, Esteghamati A, Khalilzadeh O, Esfahanian F, Khajeali L, Feiz F
    Several studies suggest that the response to various stressors differs between the sexes. We aimed to study serum HSP70 and levels of oxidized-LDL (ox-LDL) as markers of oxidative stress in men and women with type 2 diabetes. We quantified serum HSP70 and levels of ox-LDL in three cohorts; patients with newly diagnosed diabetes, patients with long-standing diabetes and normal controls. The cohort of patients with newly diagnosed diabetes was followed up for 3Â months under glucose-lowering therapy with metformin. Our findings showed that serum HSP70 level was increased in women with long-standing diabetes in comparison with men. HSP70 did not decrease after glucose lowering th...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4010366</comments>
            <pubDate>Sat, 25 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4010366</guid>        </item>
        <item>
            <title>Heat shock protein 70 is acute phase reactant: response elicited by tumor treatment with photodynamic therapy.</title>
            <link>http://www.medworm.com/index.php?rid=4010367&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20865355%26dopt%3DAbstract</link>
            <description>Authors: Merchant S, Korbelik M
    Oxidative stress in photodynamic therapy (PDT)-treated tumor cells is known to instigate a strong upregulation of the expression of heat shock proteins. However, the treatment of mouse Lewis lung carcinoma (LLC) cells with Photofrinâ¢ PDT resulted in the upregulation of heat shock protein 70 (Hsp70) gene not only in these cells but also in co-incubated untreated Hepa 1-6 cells. To investigate whether this phenomenon extends in vivo, LLC tumors growing in C57BL/6 mice were treated with Photofrinâ¢ PDT. The tumors and the livers from the mice were collected at 4, 8, or 24Â h after therapy for quantitative reverse transcriptase polymerase chain reaction-based analysis of Hsp70 gene expression. Increased Hsp70 gene expression was detected in both t...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4010367</comments>
            <pubDate>Thu, 23 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4010367</guid>        </item>
        <item>
            <title>Neutrophil gelatinase-associated lipocalin (NGAL) and matrix metalloproteinases as novel stress markers in children and young adults on chronic dialysis.</title>
            <link>http://www.medworm.com/index.php?rid=3988434&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20853162%26dopt%3DAbstract</link>
            <description>Authors: MusiaÅ K, ZwoliÅska D
    Phenomena related to chronic kidney disease, such as atherosclerosis, aggravate with the introduction of dialysis. Matrix metalloproteinases (MMP) and factors modifying their activity, such as their tissue inhibitors (TIMP) or neutrophil gelatinase-associated lipocalin (NGAL), take part in the matrix turnover and the endothelial damage characteristic for atherogenesis. However, there are no data on the associations between these parameters and other known pro-atherogenic factors, or on the impact of various dialysis modalities on them. The aim of our study was to assess the serum concentrations of NGAL, MMP-7, MMP-9, and TIMP-1, as well as their correlations with human heat shock proteins (Hsp90Î±, anti-Hsp60), endothelial dysfunction (sE-selectin...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3988434</comments>
            <pubDate>Sat, 18 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3988434</guid>        </item>
        <item>
            <title>Gene expression profiles of cytosolic heat shock proteins Hsp70 and Hsp90 from symbiotic dinoflagellates in response to thermal stress: possible implications for coral bleaching.</title>
            <link>http://www.medworm.com/index.php?rid=3956116&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20821176%26dopt%3DAbstract</link>
            <description>In this study, we identified members of two major heat shock proteins (HSPs) families, Hsp70 and Hsp90, in Symbiodinium sp. (clade C) with full-length sequences that showed the highest similarity and evolutionary relationship with other known HSPs from dinoflagellate protists. Regulation of HSPs gene expression was examined in samples of the scleractinian coral Acropora millepora subjected to elevated temperatures progressively over 18 h (fast) and 120 h (gradual thermal stress). Moderate to severe heat stress at 26 degrees C and 29 degrees C (+3 degrees C and +6 degrees C above average sea temperature) resulted in an increase in algal Hsp70 gene expression from 39% to 57%, while extreme heat stress (+9 degrees C) reduced Hsp70 transcript abundance by 60% (after 18 h) and 70% (after 120 h)...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3956116</comments>
            <pubDate>Mon, 06 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3956116</guid>        </item>
        <item>
            <title>Matrix metalloproteinases (MMP-2,9) and their tissue inhibitors (TIMP-1,2) as novel markers of stress response and atherogenesis in children with chronic kidney disease (CKD) on conservative treatment.</title>
            <link>http://www.medworm.com/index.php?rid=3956115&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20821177%26dopt%3DAbstract</link>
            <description>Authors: MusiaÅ K, ZwoliÅska D
    The system of matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) may play a key role in atherogenesis of chronic kidney disease (CKD) patients by its impact on matrix accumulation. Connections with inflammation, stress, or endothelial dysfunction are also probable. However, the data on correlations between these parameters in CKD patients are scarce in adults and absent in children. The aim of our study was to evaluate serum concentrations of MMP-2, MMP-9, TIMP-1, and TIMP-2, as well as their correlations with markers of stress response (Hsp90-alpha, anti-Hsp60), endothelial dysfunction (sE-selectin), and inflammation (high-sensitivity C-reactive protein) in CKD children treated conservatively. Thirty-seven patients were divided in...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3956115</comments>
            <pubDate>Sun, 05 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3956115</guid>        </item>
        <item>
            <title>Expression of heat shock protein-coding genes associated with anhydrobiosis in an African chironomid Polypedilum vanderplanki.</title>
            <link>http://www.medworm.com/index.php?rid=3934838&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20809134%26dopt%3DAbstract</link>
            <description>Authors: Gusev O, Cornette R, Kikawada T, Okuda T
    In order to survive in extreme environments, organisms need to develop special adaptations both on physiological and molecular levels. The sleeping chironomid Polypedilum vanderplanki, inhabiting temporary water pools in semi-arid regions of Africa, is the only insect to have evolutionarily acquired the ability to withstand prolonged complete desiccation at larval stage, entering a state called anhydrobiosis. Even after years in a dry state, larvae are able to revive within a short period of time, completely restoring metabolism. Because of the possible involvement of stress proteins in the preservation of biomolecules during the anhydrobiosis of the sleeping chironomid, we have analyzed the expression of genes encoding six heat shock p...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3934838</comments>
            <pubDate>Mon, 30 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3934838</guid>        </item>
        <item>
            <title>Heat shock proteins as biomarkers for the rapid detection of brain and spinal cord ischemia: a review and comparison to other methods of detection in thoracic aneurysm repair.</title>
            <link>http://www.medworm.com/index.php?rid=3934839&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20803353%26dopt%3DAbstract</link>
            <description>We describe the current state of knowledge of the relationship and interactions between extra- and intracellular HSPs and describe mechanisms and significance of extracellular expression of HSPs. We focus on the role of the heat shock proteins as biomarkers of central nervous system (CNS) ischemia and other severe stressors and discuss recent and novel technologies for rapid measurement of proteins in vivo and ex vivo. The HSPs are compared to other proposed small molecule biomarkers for detection of CNS injury and to other methods of detecting brain and spinal cord ischemia in real time. While other biomarkers may be of use in prognosis and in design of appropriate therapies, none appears to be as rapid as the HSPs; therefore, no other measurement appears to be of use in the immediate det...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3934839</comments>
            <pubDate>Sun, 29 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3934839</guid>        </item>
        <item>
            <title>The Nrf2-Keap1 cellular defense pathway and heat shock protein 70 (Hsp70) response. Role in protection against oxidative stress in early neonatal unilateral ureteral obstruction (UUO).</title>
            <link>http://www.medworm.com/index.php?rid=3900913&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20734248%26dopt%3DAbstract</link>
            <description>Authors: Rinaldi Tosi ME, Bocanegra V, Manucha W, Gil Lorenzo A, VallÃ©s PG
    Perturbation of renal tubular antioxidants and overproduction of reactive oxygen species may amplify the proinflammatory state of renal obstruction, culminating in oxidative stress and tubular loss. Here, we analyzed the heat shock protein 70 (Hsp70) response and the function and signal transduction of NF-E2-related protein 2 (Nrf2) transcription factor on oxidative stress modulation in obstruction. Rats were subjected to unilateral ureteral obstruction or sham operation and kidneys harvested at 5, 7, 10, and 14 days after obstruction. Hsp70 expression and Nrf2 activity and its downstream target gene products were assessed. After 10 and 14 days of obstruction, enhanced lipid peroxidation through higher thioba...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3900913</comments>
            <pubDate>Mon, 23 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3900913</guid>        </item>
        <item>
            <title>High levels of acute phase proteins and soluble 70 kDa heat shock proteins are independent and additive risk factors for mortality in colorectal cancer.</title>
            <link>http://www.medworm.com/index.php?rid=3900915&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20730518%26dopt%3DAbstract</link>
            <description>Authors: Kocsis J, MÃ©szÃ¡ros T, Madaras B, TÃ³th EK, Kamondi S, GÃ¡l P, Varga L, ProhÃ¡szka Z, FÃ¼st G
    Recently, we reported that high soluble Hsp70 (sHsp70) level was a significant predictor of mortality during an almost 3-year-long follow-up period in patients with colorectal cancer. This association was the strongest in the group of &amp;lt;70-year-old female patients as well as in those who were in a less advanced stage of the disease at baseline. According to these observations, measurement of the serum level of sHsp70 is a useful, stage-independent prognostic marker in colorectal cancer, especially in patients without distant metastasis. Since many literature data indicated that measurement of C-reactive protein (CRP) and other acute phase proteins (APPs) may also be sui...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3900915</comments>
            <pubDate>Sat, 21 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3900915</guid>        </item>
        <item>
            <title>Adjuvant activity of GP96 C-terminal domain towards Her2/neu DNA vaccine is fusion direction-dependent.</title>
            <link>http://www.medworm.com/index.php?rid=3900914&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20730610%26dopt%3DAbstract</link>
            <description>Authors: Pakravan N, Hashemi SM, Hassan ZM
    The Her2 is one of tumor-associated antigens (TAA), regarded as an ideal target of immunotherapy. DNA encoding full-length or truncated rat Her2/neu have shown protective and therapeutics potentials against Her2/neu-expressing mammary tumors. However, the efficacy of active vaccination is limited since Her2 is a self-tolerated antigen. Hence, new strategies are required to enhance both the quality and quantity of the immune response against Her2-expressing tumors. Many studies have used Her2/neu gene with cytokine or other molecules involved in regulation of immune response to enhance the potency of Her2/neu DNA vaccines. Some studies fused adjuvant gene to C-terminal domain of Her2/neu gene, while others fused the adjuvant gene N-terminally t...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3900914</comments>
            <pubDate>Sat, 21 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3900914</guid>        </item>
        <item>
            <title>A cell-based screen for inhibitors of protein folding and degradation.</title>
            <link>http://www.medworm.com/index.php?rid=3885754&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20717760%26dopt%3DAbstract</link>
            <description>We describe a simple screen for inhibitors of protein synthesis, folding, and proteasomal degradation pathways in this paper. The molecular chaperone-dependent client v-Src was fused to firefly luciferase and expressed in HCT-116 colorectal tumor cells. Both luciferase and protein tyrosine kinase activity were preserved in cells expressing this fusion construct. Exposing these cells to the Hsp90 inhibitor geldanamycin caused a rapid reduction of luciferase and kinase activities and depletion of detergent-soluble v-Src::luciferase fusion protein. Hsp70 knockdown reduced v-Src::luciferase activity and, when combined with geldanamycin, caused a buildup of v-Src::luciferase and ubiquitinated proteins in a detergent-insoluble fraction. Proteasome inhibitors also decreased luciferase activity an...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3885754</comments>
            <pubDate>Wed, 18 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3885754</guid>        </item>
        <item>
            <title>Expression of hsp90 mediates cytoprotective effects in the gastrodermis of planarians.</title>
            <link>http://www.medworm.com/index.php?rid=3865628&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20706815%26dopt%3DAbstract</link>
            <description>Authors: Conte M, Isolani ME, Deri P, Mannini L, Batistoni R
    Heat shock proteins (HSPs) play a crucial role in the protection of cells. In the present study, we have identified an hsp90-related gene (Djhsp90) encoding a cytosolic form of HSP90 that is primarily expressed in gastrodermis of the planarian Dugesia japonica. Djhsp90 becomes significantly induced after traumatic amputation or other stress stimuli, such as exposure to X-ray or ultraviolet radiations, heat shock, or prolonged starvation. When Djhsp90 is silenced by ribonucleic acid interference (RNAi), planarians dramatically decrease in size, becoming unable to eat, and die in a few weeks. Our results indicate that this gene plays an essential cytoprotective role in the gastrodermis of planarians and suggest that this chaper...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3865628</comments>
            <pubDate>Thu, 12 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3865628</guid>        </item>
        <item>
            <title>Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells.</title>
            <link>http://www.medworm.com/index.php?rid=3855638&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20694844%26dopt%3DAbstract</link>
            <description>Authors: Finka A, Mattoo RU, Goloubinoff P
    Molecular chaperones are central to cellular protein homeostasis. In mammals, protein misfolding diseases and aging cause inflammation and progressive tissue loss, in correlation with the accumulation of toxic protein aggregates and the defective expression of chaperone genes. Bacteria and non-diseased, non-aged eukaryotic cells effectively respond to heat shock by inducing the accumulation of heat-shock proteins (HSPs), many of which molecular chaperones involved in protein homeostasis, in reducing stress damages and promoting cellular recovery and thermotolerance. We performed a meta-analysis of published microarray data and compared expression profiles of HSP genes from mammalian and plant cells in response to heat or isothermal treatments ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3855638</comments>
            <pubDate>Sun, 08 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3855638</guid>        </item>
        <item>
            <title>Acute exercise activates myocardial nuclear factor kappa B.</title>
            <link>http://www.medworm.com/index.php?rid=3855639&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20694538%26dopt%3DAbstract</link>
            <description>Authors: Balan M, Locke M
    The myocardial stress response to exercise is dependent on exercise intensity and thus understanding the molecular responses between various exercise intensity levels might aid in exercise prescription. Nuclear factor kappa B (NF-kappaB) is a ubiquitous transcription factor that mediates a variety of cellular processes including inflammation, immune responses, apoptosis and cell growth/development. NF-kappaB can be comprised of homo- and/or heterodimers formed from five distinct proteins: p50 (NF-kappaB1), p52 (NF-kappaB2), RelA (p65), c-Rel, and RelB. NF-kappaB is located in the cytoplasm and kept inactive by inhibitory proteins but following the exposure to a myriad of stimuli, an activated NF-kappaB dimer translocates to the nucleus and exerts transcription...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3855639</comments>
            <pubDate>Thu, 05 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3855639</guid>        </item>
        <item>
            <title>Decarbonylated cyclophilin A Cpr1 protein protects Saccharomyces cerevisiae KNU5377Y when exposed to stress induced by menadione.</title>
            <link>http://www.medworm.com/index.php?rid=3825082&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20680535%26dopt%3DAbstract</link>
            <description>Authors: Kim IS, Jin I, Yoon HS
    Cyclophilins are conserved cis-trans peptidyl-prolyl isomerase that are implicated in protein folding and function as molecular chaperones. The accumulation of Cpr1 protein to menadione in Saccharomyces cerevisiae KNU5377Y suggests a possibility that this protein may participate in the mechanism of stress tolerance. Stress response of S. cerevisiae KNU5377Y cpr1Delta mutant strain was investigated in the presence of menadione (MD). The growth ability of the strain was confirmed in an oxidant-supplemented medium, and a relationship was established between diminishing levels of cell rescue enzymes and MD sensitivity. The results demonstrate the significant effect of CPR1 disruption in the cellular growth rate, cell viability and morphology, and redox state...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3825082</comments>
            <pubDate>Sun, 01 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3825082</guid>        </item>
        <item>
            <title>Heat shock protein 70 (Hsp70)-stimulated deoxycytidine deaminases from a human lymphoma cell but not the activation-induced cytidine deaminase (AID) from Ramos 6.4 human Burkitt's lymphoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=3825081&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20680536%26dopt%3DAbstract</link>
            <description>Authors: Bases R
    Deoxycytidine deaminase enzyme activity was reduced in lysates of human leukemic THP1 cells 24 h after transfection with siRNA designed to inhibit cell synthesis of heat shock protein 70 (Hsp70)1a and Hsp701b. The cytidine deaminase enzyme activity from the cell lysates was purified from an affinity column which contained bound single-stranded oligodeoxycytidylic acid. Deficient enzyme activity in certain elution fractions from the siRNA-transfected cells was restored by including recombinant HSP 70 in the assays. Enzyme activity in some other fractions was increased after siRNA transfection. Activation-induced cytidine deaminase (AID) is a central factor in the immune response. A more specific assay for AID was used to study the influence of Hsp70 on AID activity. Unl...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3825081</comments>
            <pubDate>Sat, 31 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3825081</guid>        </item>
        <item>
            <title>alphaB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide.</title>
            <link>http://www.medworm.com/index.php?rid=3767360&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20632140%26dopt%3DAbstract</link>
            <description>Authors: Dehle FC, Ecroyd H, Musgrave IF, Carver JA
    Amyloid fibril formation is associated with diseases such as Alzheimer's, Parkinson's, and prion diseases. Inhibition of amyloid fibril formation by molecular chaperone proteins, such as the small heat-shock protein alphaB-crystallin, may play a protective role in preventing the toxicity associated with this form of protein misfolding. Reduced and carboxymethylated kappa-casein (RCMkappa-CN), a protein derived from milk, readily and reproducibly forms fibrils at physiological temperature and pH. We investigated the toxicity of fibril formation by RCMkappa-CN using neuronal model PC12 cells and determined whether the inhibition of fibril formation altered its cell toxicity. To resolve ambiguities in the literature, we also investigated...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3767360</comments>
            <pubDate>Wed, 14 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3767360</guid>        </item>
        <item>
            <title>Increased expression of co-chaperone HOP with HSP90 and HSC70 and complex formation in human colonic carcinoma.</title>
            <link>http://www.medworm.com/index.php?rid=3742757&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20617406%26dopt%3DAbstract</link>
            <description>Authors: Kubota H, Yamamoto S, Itoh E, Abe Y, Nakamura A, Izumi Y, Okada H, Iida M, Nanjo H, Itoh H, Yamamoto Y
    Co-chaperone HOP (also called stress-inducible protein 1) is a co-chaperone that interacts with the cytosolic 70-kDa heat shock protein (HSP70) and 90-kDa heat shock protein (HSP90) families using different tetratricopeptide repeat domains. HOP plays crucial roles in the productive folding of substrate proteins by controlling the chaperone activities of HSP70 and HSP90. Here, we examined the levels of HOP, HSC70 (cognate of HSP70, also called HSP73), and HSP90 in the tumor tissues from colon cancer patients, in comparison with the non-tumor tissues from the same patients. Expression level of HOP was significantly increased in the tumor tissues (68% of patients, n = 19). Level...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3742757</comments>
            <pubDate>Thu, 08 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3742757</guid>        </item>
        <item>
            <title>Anti-heat shock protein 70 autoantibody epitope changes and BD091 promotes atherosclerosis in rats.</title>
            <link>http://www.medworm.com/index.php?rid=3734418&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20607472%26dopt%3DAbstract</link>
            <description>In conclusion, BD091 reaction with HSP70 expressed on arterial endothelial cells inducing endothelium damage triggers the inflammatory response in the vessel wall that accelerates atherosclerosis in rats. BD091 shares the same binding epitope with HSP70 autoantibodies. These data indicated that a specific epitope of anti-HSP70 autoantibody participated in the pathogenesis of atherosclerosis.
    PMID: 20607472 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3734418</comments>
            <pubDate>Tue, 06 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3734418</guid>        </item>
        <item>
            <title>Transcriptional increase and misexpression of 14-3-3 epsilon in sea urchin embryos exposed to UV-B.</title>
            <link>http://www.medworm.com/index.php?rid=3734419&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20607471%26dopt%3DAbstract</link>
            <description>Authors: Russo R, Zito F, Costa C, Bonaventura R, Matranga V
    Members of the 14-3-3 protein family are involved in many important cellular events, including stress response, survival and apoptosis. Genes of the 14-3-3 family are conserved from plants to humans, and some members are responsive to UV radiation. Here, we report the isolation of the complete cDNA encoding the 14-3-3 epsilon isoform from Paracentrotus lividus sea urchin embryos, referred to as Pl14-3-3epsilon, and the phylogenetic relationship with other homologues described in different phyla. Pl14-3-3epsilon mRNA levels were measured by QPCR during development and found to increase from the mesenchyme blastula to the prism stage. In response to UV-B (312 nm) exposure, early stage embryos collected 2 h later showed a 2.3-fo...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3734419</comments>
            <pubDate>Sat, 03 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3734419</guid>        </item>
        <item>
            <title>Heat treatment increases the incidence of alopecia areata in the C3H/HeJ mouse model.</title>
            <link>http://www.medworm.com/index.php?rid=3726600&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20582641%26dopt%3DAbstract</link>
            <description>In this study, we investigated the effects of heat treatment, a physiological stress, on AA development in C3H/HeJ mice. Whereas this strain of mice are predisposed to AA at low incidence by 18 months of age, we observed a significant increase in the incidence of hair loss in heat-treated 8-month-old C3H/HeJ mice compared with sham-treated mice. Histological analysis detected mononuclear cell infiltration in anagen hair follicles, a characteristic of AA, in heat-treated mouse skin. As expected, increased expression of induced HSPA1A/B (formerly called HSP70i) was detected in skin samples from heat-treated mice. Importantly, increased HSPA1A/B expression was also detected in skin samples from C3H/HeJ mice that developed AA spontaneously. Our results suggest that induction of HSPA1A/B may pr...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3726600</comments>
            <pubDate>Sat, 26 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3726600</guid>        </item>
        <item>
            <title>Down-regulation of HSP60 expression by RNAi increases lipopolysaccharide- and cerulein-induced damages on isolated rat pancreatic tissues.</title>
            <link>http://www.medworm.com/index.php?rid=3702145&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20574674%26dopt%3DAbstract</link>
            <description>The objective of this study was to investigate the function of heat shock protein 60 (HSP60) on pancreatic tissues by applying HSP60 small interfering RNA (siRNA) to reduce HSP60 expression. Rat pancreas was isolated and pancreatic tissue snips were prepared, cultured, and stimulated with low and high concentrations of cerulein (10(-11) and 10(-5) mol/L) or lipopolysaccharide (LPS, 10 and 20 mug/mL). Before the stimulation and 1 and 4 h after the stimulation, the viability and the level of trypsinogen activation peptide (TAP) in the tissue fragments were determined and the levels of tumor necrosis factor-alpha (TNF-alpha) and interleukin 6 (IL-6) in the culture supernatants were measured. Real-time PCR and Western blotting were used to evaluate the HSP60 mRNA and protein expression. After ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3702145</comments>
            <pubDate>Wed, 23 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3702145</guid>        </item>
        <item>
            <title>Co-administration of GP96 and Her2/neu DNA vaccine in a Her2 breast cancer model.</title>
            <link>http://www.medworm.com/index.php?rid=3663114&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20544406%26dopt%3DAbstract</link>
            <description>In this study, animals with Her2-expressing tumors were vaccinated by co-administration of GP96+ Her2/neu DNA vaccines. Analyses of the immune response, 2 weeks after the last immunization revealed decreased CD4+ CD25+ Foxp3+ naturally occurring regulatory T cells (Tregs) at the tumor site and increased IFN-gamma/IL-4 level. Nevertheless, the graph of tumor size demonstrated a bi-phasic pattern in which partial control of tumor progression initially occurred, but finally its effectiveness was inversely affected by tumor size.
    PMID: 20544406 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3663114</comments>
            <pubDate>Fri, 11 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3663114</guid>        </item>
        <item>
            <title>A microarray analysis of the effects of moderate hypothermia and rewarming on gene expression by human hepatocytes (HepG2).</title>
            <link>http://www.medworm.com/index.php?rid=3645412&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20526826%26dopt%3DAbstract</link>
            <description>We examined the gene expression changes produced by moderate hypothermia and tested the hypothesis that rewarming after hypothermia approximates a heat-shock response. Six sets of human HepG2 hepatocytes were subjected to moderate hypothermia (31 degrees C for 16 h), a conventional in vitro heat shock (43 degrees C for 30 min) or control conditions (37 degrees C), then harvested immediately or allowed to recover for 3 h at 37 degrees C. Expression analysis was performed with Affymetrix U133A gene chips, using analysis of variance-based techniques. Moderate hypothermia led to distinct time-dependent expression changes, as did heat shock. Hypothermia initially caused statistically significant, greater than or equal to twofold changes in expression (relative to controls) of 409 sequences (143...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3645412</comments>
            <pubDate>Sat, 05 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3645412</guid>        </item>
        <item>
            <title>Xenohormesis: health benefits from an eon of plant stress response evolution.</title>
            <link>http://www.medworm.com/index.php?rid=3633951&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20524162%26dopt%3DAbstract</link>
            <description>Authors: Hooper PL, Hooper PL, Tytell M, VÃ­gh L
    Xenohormesis is a biological principle that explains how environmentally stressed plants produce bioactive compounds that can confer stress resistance and survival benefits to animals that consume them. Animals can piggyback off products of plants' sophisticated stress response which has evolved as a result of their stationary lifestyle. Factors eliciting the plant stress response can judiciously be employed to maximize yield of health-promoting plant compounds. The xenohormetic plant compounds can, when ingested, improve longevity and fitness by activating the animal's cellular stress response and can be applied in drug discovery, drug production, and nutritional enhancement of diet.
    PMID: 20524162 [PubMed - as supplied by publish...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3633951</comments>
            <pubDate>Thu, 03 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3633951</guid>        </item>
        <item>
            <title>Stress, genomes, and evolution.</title>
            <link>http://www.medworm.com/index.php?rid=3627144&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20521130%26dopt%3DAbstract</link>
            <description>Authors: Mittelman D, Wilson JH
    Evolutionary change, whether in populations of organisms or malignant tumor cells, is contingent on the availability of inherited variation for natural selection to act upon. It is becoming clear that the Hsp90 chaperone, which normally functions to buffer client proteins against the effects of genetic variation, plays a central role in this process. Severe environmental stress can overwhelm the chaperone's buffering capacity, causing previously cryptic genetic variation to be expressed. Recent studies now indicate that in addition to exposing existing variation, Hsp90 can induce novel epigenetic and genetic changes. We discuss key findings that suggest a rich set of pathways by which Hsp90 can mediate the influences of the environment on the genome.
   ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3627144</comments>
            <pubDate>Thu, 03 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3627144</guid>        </item>
        <item>
            <title>Increased serum HSP70 levels are associated with the duration of diabetes.</title>
            <link>http://www.medworm.com/index.php?rid=3600218&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20496051%26dopt%3DAbstract</link>
            <description>Authors: Nakhjavani M, Morteza A, Khajeali L, Esteghamati A, Khalilzadeh O, Asgarani F, Outeiro TF
    The evolutionary conserved family of heat shock proteins (HSP) is responsible for protecting cells against different types of stress, including oxidative stress. Although the levels of HSPs can be readily measured in blood serum, the levels of HSP70 in patients with different durations of diabetes have not been studied before. We quantified serum HSP70 levels in a healthy control group (n = 36) and two groups of type 2 diabetic patients, defined as newly diagnosed diabetes (n = 36) and patients with diabetes duration of more than 5 years (n = 37). The clinical characteristics and biochemical parameters were evaluated in the studied population. We found that serum HSP70 levels were signifi...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3600218</comments>
            <pubDate>Sat, 22 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3600218</guid>        </item>
        <item>
            <title>Extracellular heat shock protein 70 (HSPA1A) and classical vascular risk factors in a general population.</title>
            <link>http://www.medworm.com/index.php?rid=3590810&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20490736%26dopt%3DAbstract</link>
            <description>Authors: Dulin E, GarcÃ­a-Barreno P, Guisasola MC
    Atherosclerosis is a chronic inflammatory and autoimmune disease. Candidate molecules/autoantigens include heat shock proteins (HSPs); Hsp70 (HSPA1A) is one of the best studied HSPs. Various studies have shown a correlation between extracellular Hsp70 (eHsp70) and anti-Hsp70/anti-Hsp60 antibody concentration and development of atherosclerosis. A random sample of 456 people aged 40-60 (218 males, 234 females) was studied to investigate the prevalence of traditional vascular risk factors and eHsp70 and anti-Hsp70/anti-Hsp60 antibodies levels, according to the risk of vascular disease. Task Force Chart was applied for classification. Subjects were divided into three groups: G0 (with no vascular risk factor or a risk lower than 5%), n = 2...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3590810</comments>
            <pubDate>Wed, 19 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3590810</guid>        </item>
        <item>
            <title>Celastrol regulates multiple nuclear transcription factors belonging to HSP90's clients in a dose- and cell type-dependent way.</title>
            <link>http://www.medworm.com/index.php?rid=3582435&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20480272%26dopt%3DAbstract</link>
            <description>In this study, we observe the effects of celastrol on 18 TFs (belonging to HSP90 clients) in three human cell lines: MCF-7 (breast cancer), HepG2 (hepatoma), and THP-1 (monocytic leukemia). The results show that at least half of the detectable TFs were affected by celastrol, though the effect patterns varied with cell type and dosage. Bi-directional regulations of some TFs were identified, a phenomenon not yet seen with other HSP90 inhibitors. Celastrol's capability to affect multiple TFs was consistent with its altering HSP90/TFs interactions and disrupting HSP90/Hop interaction, in addition to the reported damaging HSP90/Cdc37 interaction. This work confirms, for the first time, that celastrol has broad effects on TFs belonging to HSP90's clients, casts new light on understanding these r...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3582435</comments>
            <pubDate>Mon, 17 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3582435</guid>        </item>
        <item>
            <title>Neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic alcohol administration.</title>
            <link>http://www.medworm.com/index.php?rid=3564635&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20461564%26dopt%3DAbstract</link>
            <description>In this study, we investigated the neuroprotective effect of small heat shock protein, Hsp27, after acute and chronic ethanol administrations using transgenic mice overexpressing the human Hsp27 protein. Transgenic mice and wild-type littermates were injected with 2 g/kg ethanol intraperitoneally, and then motor coordination and muscle strength were analyzed using different behavioral tests, such as footprint analysis, balance beam, and inverted screen tests. Ethanol-injected transgenic mice showed similar footprints to control saline-injected mice, did not fall of the beam, and were able to climb to the top of the inverted screen, while wild-type mice showed ataxia and incoordination after ethanol injection. The effect of Hsp27 on chronic ethanol consumption was also investigated. Drinkin...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3564635</comments>
            <pubDate>Tue, 11 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3564635</guid>        </item>
        <item>
            <title>An unfolded protein response is the initial cellular response to the expression of mutant matrilin-3 in a mouse model of multiple epiphyseal dysplasia.</title>
            <link>http://www.medworm.com/index.php?rid=3522924&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20428984%26dopt%3DAbstract</link>
            <description>Authors: Nundlall S, Rajpar MH, Bell PA, Clowes C, Zeeff LA, Gardner B, Thornton DJ, Boot-Handford RP, Briggs MD
    Multiple epiphyseal dysplasia (MED) can result from mutations in matrilin-3, a structural protein of the cartilage extracellular matrix. We have previously shown that in a mouse model of MED the tibia growth plates were normal at birth but developed a progressive dysplasia characterised by the intracellular retention of mutant matrilin-3 and abnormal chondrocyte morphology. By 3 weeks of age, mutant mice displayed a significant decrease in chondrocyte proliferation and dysregulated apoptosis. The aim of this current study was to identify the initial post-natal stages of the disease. We confirmed that the disease phenotype is seen in rib and xiphoid cartilage and, like tibia ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3522924</comments>
            <pubDate>Thu, 29 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3522924</guid>        </item>
        <item>
            <title>Identification of two small heat shock proteins with different response profile to cadmium and pathogen stresses in Venerupis philippinarum.</title>
            <link>http://www.medworm.com/index.php?rid=3491355&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20405260%26dopt%3DAbstract</link>
            <description>Authors: Li C, Wang L, Ning X, Chen A, Zhang L, Qin S, Wu H, Zhao J
    Small heat shock proteins (sHSPs) encompass a widespread and diverse class of proteins with molecular chaperone activity. In the present study, two sHSP isoforms (VpsHSP-1 and VpsHSP-2) were cloned from Venerupis philippinarum haemocytes by Rapid Amplification of cDNA Ends (RACE) approaches. The expression profiles of these two genes under Vibrio anguillarum challenge and cadmium exposure were investigated by quantitative real-time reverse transcriptase polymerase chain reaction. The bacterial challenge could significantly up-regulate the mRNA expression of both VpsHSP-1 and VpsHSP-2, with the increase of VpsHSP-2 expression occurred earlier than that of VpsHSP-1. During the cadmium exposure experiment, the expression ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3491355</comments>
            <pubDate>Mon, 19 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3491355</guid>        </item>
        <item>
            <title>KLF4 promotes hydrogen-peroxide-induced apoptosis of chronic myeloid leukemia cells involving the bcl-2/bax pathway.</title>
            <link>http://www.medworm.com/index.php?rid=3483644&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20401760%26dopt%3DAbstract</link>
            <description>Authors: Li Z, Zhao J, Li Q, Yang W, Song Q, Li W, Liu J
    K562 cells and peripheral blood mononuclear cells were treated with hydrogen peroxide (H(2)O(2)) to determine the expression of Kr&amp;#xFC;ppel-like factor (KLF) 4. A full-length complementary DNA or an anti-sense oligonucleotide of KLF4 was transfected into cells, and expressions of B-cell lymphoma/leukemia-2 (bcl-2) and bcl-2-associated X (bax) proteins were analyzed. The results showed that H(2)O(2) treatment of cells resulted in an increase in KLF4 levels; KLF4 induced apoptosis and slowed cell growth, potentially resulting from up-regulation of bax and down-regulation of bcl-2. Transcriptional activities on bcl-2 and bax were promoted following KLF4 overexpression potentially through KLF4 binding sites on corresponding promoter...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3483644</comments>
            <pubDate>Sun, 18 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3483644</guid>        </item>
        <item>
            <title>Differential stress responses among newly received calves: variations in reductant capacity and Hsp gene expression.</title>
            <link>http://www.medworm.com/index.php?rid=3483645&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20401744%26dopt%3DAbstract</link>
            <description>Authors: Eitam H, Vaya J, Brosh A, Orlov A, Khatib S, Izhaki I, Shabtay A
    Bovine respiratory disease complex (BRD), a major economic concern to the beef cattle industry all over the world, is triggered by physical, biological and psychological stresses. It is becoming noticeable that the key to reducing BRD appears to be centered at reducing the response to stress. The aims of the present study were to detect individual variations in the stress response of newly received young calves through their leukocyte heat shock protein (Hsp) response, selected neutrophil-related gene expression and oxidative stress, and relate them to pulmonary adhesions at slaughter, an indicative sign of clinical and subclinical episodes of BRD at an early age. Differential expression patterns of Hsp60 and Hsp...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3483645</comments>
            <pubDate>Sat, 17 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3483645</guid>        </item>
        <item>
            <title>The response of interleukin-6 and soluble interleukin-6 receptor isoforms following intermittent high intensity and continuous moderate intensity cycling.</title>
            <link>http://www.medworm.com/index.php?rid=3480812&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20396982%26dopt%3DAbstract</link>
            <description>This study also investigated the expression of the differentially spliced sIL-6R (DS-sIL-6R) in response to exercise. Eleven healthy males completed two exercise trials matched for external work done (582 +/- 82 kJ). During MOD, participants cycled at 61.8 (2.6)% VO(2peak) for 58.7 (1.9) min, while HIIT consisted of ten 4-min intervals cycling at 87.5 (3.4)% [Formula: see text] separated by 2-min rest. Blood samples were collected pre-exercise, post-exercise, and 1.5, 6, and 23 h post-exercise. Plasma IL-6, sIL-6R, IL-6/sIL-6R complex, and DS-sIL-6R levels were measured by enzyme-linked immunosorbent assay. HIIT caused a significantly greater increase in IL-6 than MOD (P = 0.018). Both MOD and HIIT resulted in an increase in sIL-6R and IL-6/sIL-6R complex (P &amp;lt; 0.001), however, this was ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3480812</comments>
            <pubDate>Thu, 15 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3480812</guid>        </item>
        <item>
            <title>Hsp60 and Hsp10 increase in colon mucosa of Crohn's disease and ulcerative colitis.</title>
            <link>http://www.medworm.com/index.php?rid=3476225&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20390473%26dopt%3DAbstract</link>
            <description>Authors: Rodolico V, Tomasello G, Zerilli M, Martorana A, Pitruzzella A, Marino Gammazza A, David S, Zummo G, Damiani P, Accomando S, Conway de Macario E, Macario AJ, Cappello F
    The purpose of this work was to determine in colon mucosa of Crohn's disease (CD) and ulcerative colitis (UC) in relapse: a) the levels of the chaperonins Hsp60 and Hsp10; b) the quantity of inflammatory cells; and c) if the levels of chaperonins parallel those of inflammation cells. Twenty cases of CD and UC and twenty normal controls (NC) were studied using immunohistochemistry, Western blotting and immunofluorescence. Immunohistochemically, Hsp60 and Hsp10 were increased in both inflammatory bowel diseases (IBD) compared to NC. These results were confirmed by Western blotting. Hsp60 and Hsp10 occurred in the...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3476225</comments>
            <pubDate>Wed, 14 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3476225</guid>        </item>
        <item>
            <title>Cloning and expression of rabbit CCT subunits eta and beta in healing cutaneous wounds.</title>
            <link>http://www.medworm.com/index.php?rid=3476223&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20393890%26dopt%3DAbstract</link>
            <description>Authors: Satish L, Johnson S, Abdulally A, Post JC, Ehrlich GD, Kathju S
    We have previously identified the CCT subunit eta as specifically reduced in healing fetal skin wounds by differential display, and observed that this reduction is not seen with any other CCT subunit. We now report the cloning and characterization of the cDNAs for rabbit CCT-eta and its closest evolutionary homolog, CCT-beta. Quantitative examination of CCT-eta and -beta message expression in healing fetal and adult wounds at 12 h post-injury confirms that CCT-eta mRNA is decreased in fetal wound tissues, but actually elevated in adult wound tissues. CCT-beta mRNA, in contrast, remains unchanged in both fetal and adult wound tissues. CCT-eta mRNA remains persistently elevated in healing adult wounds for 28 days fo...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3476223</comments>
            <pubDate>Wed, 14 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3476223</guid>        </item>
        <item>
            <title>Inactivation of the hereditary spastic paraplegia-associated Hspd1 gene encoding the Hsp60 chaperone results in early embryonic lethality in mice.</title>
            <link>http://www.medworm.com/index.php?rid=3476224&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20393889%26dopt%3DAbstract</link>
            <description>In this study, we describe the generation and characterization of a mutant mouse line bearing an inactivating gene-trap insertion in the Hspd1 gene encoding Hsp60. We found that heterozygous mice were born at the expected ratio compared to wild-type mice and displayed no obvious phenotype deficits. Using quantitative reverse transcription PCR, we found significantly decreased levels of the Hspd1 transcript in all of the tissues examined, demonstrating that the inactivation of the Hspd1 gene is efficient. By Western blot analysis, we found that the amount of Hsp60 protein, compared to either cytosolic tubulin or mitochondrial voltage-dependent anion-selective channel protein 1/porin, was decreased as well. The expression of the nearby Hspe1 gene, which encodes the Hsp10 co-chaperonin, was c...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3476224</comments>
            <pubDate>Sun, 11 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3476224</guid>        </item>
        <item>
            <title>Expression of uncoupling protein 3 in mitochondria protects against stress-induced myocardial injury: a proteomic study.</title>
            <link>http://www.medworm.com/index.php?rid=3468382&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20383618%26dopt%3DAbstract</link>
            <description>Authors: Wang X, Gong J, Liu X, Zhan R, Kong R, Zhao Y, Wan D, Leng X, Chen M, Qian L
    It has been confirmed that stress plays an important role in the induction and development of cardiovascular diseases, but its mechanism and molecular basis remain unknown. In the present study, a myocardial injury model induced by restraint stress was established in rat. To screen for the related proteins involved in stress-induced myocardial injury, proteomic techniques based on 2-DE and mass spectrometry were used. In our results, ten proteins were found to be altered. The expression of eight of these proteins was increased after restraint stress, including cardiac myosin heavy chain, dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial aldehyde dehy...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3468382</comments>
            <pubDate>Fri, 09 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3468382</guid>        </item>
        <item>
            <title>Caffeic acid protects rat heart mitochondria against isoproterenol-induced oxidative damage.</title>
            <link>http://www.medworm.com/index.php?rid=3457215&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20376586%26dopt%3DAbstract</link>
            <description>This study may have a significant impact on myocardial-infarcted patients.
    PMID: 20376586 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3457215</comments>
            <pubDate>Thu, 08 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3457215</guid>        </item>
        <item>
            <title>Hsp90 modulates CAG repeat instability in human cells.</title>
            <link>http://www.medworm.com/index.php?rid=3450218&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20373063%26dopt%3DAbstract</link>
            <description>We report that impairment of Hsp90 in human cells induces contractions of CAG repeat tracks by tenfold. Inhibition of the recombinase Rad51, a downstream target of Hsp90, induces a comparable increase in repeat instability, suggesting that Hsp90-enabled homologous recombination normally functions to stabilize CAG repeat tracts. By contrast, Hsp90 inhibition does not increase the rate of gene-inactivating point mutations. The capacity of Hsp90 to modulate repeat-tract lengths suggests that the chaperone, in addition to exposing cryptic variation, might facilitate the expression of new phenotypes through induction of novel genetic variation.
    PMID: 20373063 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3450218</comments>
            <pubDate>Wed, 07 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3450218</guid>        </item>
        <item>
            <title>Identification of potential HLA class I and class II epitope precursors associated with heat shock protein 70 (HSPA).</title>
            <link>http://www.medworm.com/index.php?rid=3435297&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20358320%26dopt%3DAbstract</link>
            <description>In this study, we investigated the possible involvement of HSPA in HLA class I or class II antigen presentation and analysed the antigenic potential of the associated peptides. HSPA was purified from CCRF-CEM and K562 cell lines, and using mass spectrometry techniques, we identified 44 different peptides which were co-purified with HSPA. The affinity of the identified peptides to two HSPA isoforms, HSPA1A and HSPA8, was confirmed using a peptide array. Four of the HSPA-associated peptides were matched with 13 previously reported HLA epitopes. Of these 13 peptides, nine were HLA class I and four were HLA class II epitopes. These results demonstrate the association of HSPA with HLA class I and class II epitopes, therefore providing further evidence for the involvement of HSPA in the antigen ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3435297</comments>
            <pubDate>Wed, 31 Mar 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3435297</guid>        </item>
        <item>
            <title>Identification of microRNAs associated with hyperthermia-induced cellular stress response.</title>
            <link>http://www.medworm.com/index.php?rid=3429635&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20352393%26dopt%3DAbstract</link>
            <description>In this study, we identify a group of thermally regulated miRNAs (TRMs) that are associated with the CSR. Using miRNA microarrays, we show that dermal fibroblasts differentially express 123 miRNAs when exposed to hyperthermia. Interestingly, only 27 of these miRNAs are annotated in the current Sanger registry. We validated the expression of the annotated miRNAs using qPCR techniques, and we found that the qPCR and microarray data was in well agreement. Computational target-prediction studies revealed that putative targets for the TRMs are heat shock proteins and Argonaute-2-the core functional unit of RNA silencing. These results indicate that cells express a specific group of miRNAs when exposed to hyperthermia, and these miRNAs may function in the regulation of the CSR. Future studies wi...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3429635</comments>
            <pubDate>Mon, 29 Mar 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3429635</guid>        </item>
        <item>
            <title>The Hsp72 response in peri-parturient dairy cows: relationships with metabolic and immunological parameters.</title>
            <link>http://www.medworm.com/index.php?rid=3421125&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20349286%26dopt%3DAbstract</link>
            <description>Authors: Catalani E, Amadori M, Vitali A, Bernabucci U, Nardone A, Lacetera N
    The study was aimed at assessing whether the peri-parturient period is associated with changes of intracellular and plasma inducible heat shock proteins (Hsp) 72 kDa molecular weight in dairy cows, and to establish possible relationships between Hsp72, metabolic, and immunological parameters subjected to changes around calving. The study was carried out on 35 healthy peri-parturient Holstein cows. Three, two, and one week before the expected calving, and 1, 2, 3, 4, and 5 weeks after calving, body conditions score (BCS) was measured and blood samples were collected to separate plasma and peripheral blood mononuclear cells (PBMC). Concentrations of Hsp72 in PBMC and plasma increased sharply after calving. In t...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3421125</comments>
            <pubDate>Sun, 28 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3421125</guid>        </item>
        <item>
            <title>Characterization of plant p23-like proteins for their co-chaperone activities.</title>
            <link>http://www.medworm.com/index.php?rid=3421124&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20349287%26dopt%3DAbstract</link>
            <description>Authors: Zhang Z, Sullivan W, Felts SJ, Prasad BD, Toft DO, Krishna P
    The small acidic protein p23 is best described as a co-chaperone of Hsp90, an essential molecular chaperone in eukaryotes. p23 binds to the ATP-bound form of Hsp90 and stabilizes the Hsp90-client protein complex by slowing down ATP turnover. The stabilizing activity of p23 was first characterized in studies of steroid receptor-Hsp90 complexes. Earlier studies of the Hsp90 chaperone complex in plants suggested that a p23-like stabilizing activity was absent in plant cell lysates. Here, we show that p23-like proteins are present in plants and are capable of binding Hsp90, but unlike human p23 and yeast ortholog Sba1, the plant p23-like proteins do not stabilize the steroid receptor-Hsp90 complexes formed in wheat germ ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3421124</comments>
            <pubDate>Sun, 28 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3421124</guid>        </item>
        <item>
            <title>A single dose of carbon monoxide intraperitoneal administration protects rat intestine from injury induced by lipopolysaccharide.</title>
            <link>http://www.medworm.com/index.php?rid=3412785&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20339960%26dopt%3DAbstract</link>
            <description>Authors: Liu SH, Ma K, Xu XR, Xu B
    Treatment with inhaled carbon monoxide (CO) has been shown to ameliorate intestinal injury induced by lipopolysaccharide (LPS) or ischemia-reperfusion in experimental animals. We hypothesized that CO intraperitoneal administration (i.p) might provide similar protection against inhaled gas. In the present study, 1 h after intravenously receiving 5 mg/kg LPS, rats were exposed to either room air or 2 ml/kg of 250 ppm CO i.p for 1, 3, and 6 h. Intestinal tissues were collected to determine the levels of platelet activator factor (PAF), intercellular adhesion molecule-1 (ICAM-1), interlukin-10 (IL-10), maleic dialdehyde (MDA), cell apoptotic rate and the phosphorylated p38 mitogen activated protein kinase (MAPK), as well as myeloperoxidase (MPO) and super...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3412785</comments>
            <pubDate>Sat, 27 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3412785</guid>        </item>
        <item>
            <title>Plasma levels of Hsp70 and anti-Hsp70 antibody predict risk of acute coronary syndrome.</title>
            <link>http://www.medworm.com/index.php?rid=3386346&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20300983%26dopt%3DAbstract</link>
            <description>This study assessed whether there is a significant association between extracellular human Hsp70, anti-Hsp70 antibody and acute coronary syndrome (ACS) and stable angina (SA), and examined dynamic changes in Hsp70 and anti-Hsp70 antibody levels induced by acute myocardial infarction (AMI). Plasma Hsp70 and anti-Hsp70 antibody levels in 291 patients with ACS (179 AMI, 112 unstable angina), 126 patients with SA and 417 age and sex-matched healthy subjects, and in 40 patients after admission for AMI, and on day 2, 3, and 7 after the onset of AMI were determined using enzyme-linked immunosorbent assays. Hsp70 levels were significantly higher in ACS and SA and anti-Hsp70 antibody levels were only markedly lower in ACS than controls. After adjustment for traditional CHD risk factors, increasing ...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3386346</comments>
            <pubDate>Fri, 19 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Age-related protective effect of deprenyl on changes in the levels of diagnostic marker enzymes and antioxidant defense enzymes activities in cerebellar tissue in Wistar rats.</title>
            <link>http://www.medworm.com/index.php?rid=3362836&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20224915%26dopt%3DAbstract</link>
            <description>Authors: Subramanian MV, James TJ
    Antioxidants are free radical scavengers and protect living organisms against oxidative damage to tissues. Experimental evidence implicates oxygen-derived free radicals as important causative agents of aging and the present study was designed to evaluate the age-related effects of deprenyl on the antioxidant defense in the cerebellum of male Wistar rats. Experimental rats of three age groups (6, 12, and 18 months old) were administered with liquid deprenyl (2 mg/kg body weight/day for a period of 15 days i.p) and levels of diagnostic marker enzymes (alanine aminotransferase, aspartate aminotransferase, lactate dehydrogenase and creatine phosphokinase) in plasma, lipid peroxides, reduced glutathione and activities of glutathione-dependent antioxidant en...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3362836</comments>
            <pubDate>Sat, 13 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Long- but not short-term heat acclimation produces an apoptosis-resistant cardiac phenotype: a lesson from heat stress and ischemic/reperfusion insults.</title>
            <link>http://www.medworm.com/index.php?rid=3362837&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20221856%26dopt%3DAbstract</link>
            <description>In conclusion, the elevated Bcl-X(L)/Bad ratio and decreased cyt c leakage to the cytosol are insufficient to protect the heart and interactions with additional cytoprotective pathways involved in acclimation (elevated HSP70, ROS, and sarcolemmal adaptations to abolish extrinsic apoptosis pathways) are required to induce the apoptosis-resistant AC phenotype.
    PMID: 20221856 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3362837</comments>
            <pubDate>Fri, 12 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>N-terminally fusion of Her2/neu to HSP70 decreases efficiency of Her2/neu DNA vaccine.</title>
            <link>http://www.medworm.com/index.php?rid=3362835&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20224916%26dopt%3DAbstract</link>
            <description>In this study, we examined if N-terminally fusion of Her2/neu to HSP70 could also improve efficiency of Her2/neu DNA vaccine. Therefore, mice with an established Her2/neu expressing tumor were immunized with DNA vaccine consisting of extracellular and trans-membrane domain (EC+TM) of rat Her2/neu alone or N-terminally fused to HSP70 and immune response was evaluated. Administration of rat Her2/neu led to partial control of tumor progression. Surprisingly, fusion of HSP70 to N-terminal of rat Her2/neu led to tumor progression. Our result proposes that fusion direction of biologic adjuvant is an important consideration when Her2/neu is used.
    PMID: 20224916 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3362835</comments>
            <pubDate>Fri, 12 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Febrile range temperature represses TNF-alpha gene expression in LPS-stimulated macrophages by selectively blocking recruitment of Sp1 to the TNF-alpha promoter.</title>
            <link>http://www.medworm.com/index.php?rid=3362838&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20221720%26dopt%3DAbstract</link>
            <description>In conclusion, our studies further emphasize the complex and redundant control of TNF-alpha transcription and identify additional potential mechanisms through which FRT exposure may reduce TNF-alpha expression by selectively modifying gene-specific recruitment of transcription factors to the proximal TNF-alpha promoter.
    PMID: 20221720 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones)</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3362838</comments>
            <pubDate>Wed, 10 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM).</title>
            <link>http://www.medworm.com/index.php?rid=3316403&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20186508%26dopt%3DAbstract</link>
            <description>Authors: Gilady SY, Bui M, Lynes EM, Benson MD, Watts R, Vance JE, Simmen T
    Protein secretion from the endoplasmic reticulum (ER) requires the enzymatic activity of chaperones and oxidoreductases that fold polypeptides and form disulfide bonds within newly synthesized proteins. The best-characterized ER redox relay depends on the transfer of oxidizing equivalents from molecular oxygen through ER oxidoreductin 1 (Ero1) and protein disulfide isomerase to nascent polypeptides. The formation of disulfide bonds is, however, not the sole function of ER oxidoreductases, which are also important regulators of ER calcium homeostasis. Given the role of human Ero1alpha in the regulation of the calcium release by inositol 1,4,5-trisphosphate receptors during the onset of apoptosis, we hypothesized...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3316403</comments>
            <pubDate>Fri, 26 Feb 2010 00:00:00 +0100</pubDate>
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            <title>Larval excretory-secretory products from the parasite Schistosoma mansoni modulate HSP70 protein expression in defence cells of its snail host, Biomphalaria glabrata.</title>
            <link>http://www.medworm.com/index.php?rid=3312293&amp;cid=s_37762_171_f&amp;fid=37762&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20182834%26dopt%3DAbstract</link>
            <description>This study focused on the effects of larval excretory-secretory products (ESPs) from the parasite Schistosoma mansoni on HSP70 protein expression levels in haemocytes (defence cells) from its snail intermediate host Biomphalaria glabrata. S. mansoni larval stage ESPs are known to interfere with haemocyte physiology and behaviour. Haemocytes from two different B. glabrata strains, one which is susceptible to S. mansoni infection and one which is resistant, both showed reduced HSP70 protein levels following 1 h challenge with S. mansoni ESPs when compared to unchallenged controls; however, the reduction observed in the resistant strain was less marked. The decline in intracellular HSP70 protein persisted for at least 5 h in resistant snail haemocytes only. Furthermore, in schistosome-suscept...</description>
            <author>Cell Stress and Chaperones</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3312293</comments>
            <pubDate>Thu, 25 Feb 2010 00:00:00 +0100</pubDate>
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