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. Sat, 20 Mar 2010 16:35:09 +0100 http://www.medworm.com/index.php?rid=3362836&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20224915%26dopt%3DAbstract 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... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3362836 Sat, 13 Mar 2010 00:00:00 +0100 3362836 http://www.medworm.com/index.php?rid=3362837&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20221856%26dopt%3DAbstract 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) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3362837 Fri, 12 Mar 2010 00:00:00 +0100 3362837 http://www.medworm.com/index.php?rid=3362835&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20224916%26dopt%3DAbstract 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) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3362835 Fri, 12 Mar 2010 00:00:00 +0100 3362835 http://www.medworm.com/index.php?rid=3362838&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20221720%26dopt%3DAbstract 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) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3362838 Wed, 10 Mar 2010 00:00:00 +0100 3362838 http://www.medworm.com/index.php?rid=3316403&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20186508%26dopt%3DAbstract 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... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3316403 Fri, 26 Feb 2010 00:00:00 +0100 3316403 http://www.medworm.com/index.php?rid=3312293&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20182834%26dopt%3DAbstract 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... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3312293 Thu, 25 Feb 2010 00:00:00 +0100 3312293 http://www.medworm.com/index.php?rid=3312292&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20182835%26dopt%3DAbstract Authors: Linhares IM, Witkin SS Chlamydia trachomatis is an obligate intracellular bacterium that infects chiefly urogenital and ocular epithelial cells. In some infected women the microorganism migrates to the upper reproductive tract resulting in a chronic, but asymptomatic, infection. The immune response to this infection, production of interferon-gamma and pro-inflammatory cytokines, results in interruption of chlamydial intracellular replication. However, the Chlamydia remains viable and enters into a persistent state. In this form, most chlamydial genes are inactive. An exception is the gene coding for the 60 kDa heat shock protein (hsp60), which is synthesized in increased amounts and is released into the extracellular milieu. The chronic release of chlamydial hsp60 induces a lo... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3312292 Thu, 25 Feb 2010 00:00:00 +0100 3312292 http://www.medworm.com/index.php?rid=3303353&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20174993%26dopt%3DAbstract Authors: Dehbi M, Baturcam E, Eldali A, Ahmed M, Kwaasi A, Chishti MA, Bouchama A Exposure of rats to environmental heat enhances the expression of heat shock protein-72 (Hsp-72) in most of their organs proportionally to heat stress severity. Pre-induction or over-expression of Hsp-72 prevents organ damage and lethality, suggesting that heat shock proteins (Hsps) may have a pathogenic role in this condition. We investigated the expression profile of Hsps in baboons subjected to environmental heat stress until the core temperature attained 42.5 degrees C (moderate heatstroke) or occurrence of hypotension associated with core temperature >/=43.5 degrees C (severe heatstroke). Western blot analysis demonstrated a differential induction of Hsp-72 among organs of heat-stressed animals wi... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3303353 Tue, 23 Feb 2010 00:00:00 +0100 3303353 http://www.medworm.com/index.php?rid=3291523&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20169475%26dopt%3DAbstract Authors: Burdette AJ, Churchill PF, Caldwell GA, Caldwell KA TorsinA is a member of the AAA+ ATPase family of proteins and, notably, is the only known ATPase localized to the ER lumen. It has been suggested to act as a molecular chaperone, while a mutant form associated with early-onset torsion dystonia, a dominantly inherited movement disorder, appears to result in a net loss of function in vivo. Thus far, no studies have examined the chaperone activity of torsinA in vitro. Here we expressed and purified both wild-type (WT) and mutant torsinA fusion proteins in bacteria and examined their ability to function as molecular chaperones by monitoring suppression of luciferase and citrate synthase (CS) aggregation. We also assessed their ability to hold proteins in an intermediate state for... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3291523 Fri, 19 Feb 2010 00:00:00 +0100 3291523 http://www.medworm.com/index.php?rid=3280277&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20157854%26dopt%3DAbstract Authors: Sun X, Fontaine JM, Hoppe AD, Carra S, Deguzman C, Martin JL, Simon S, Vicart P, Welsh MJ, Landry J, Benndorf R A number of missense mutations in the two related small heat shock proteins HspB8 (Hsp22) and HspB1 (Hsp27) have been associated with the inherited motor neuron diseases (MND) distal hereditary motor neuropathy and Charcot-Marie-Tooth disease. HspB8 and HspB1 interact with each other, suggesting that these two etiologic factors may act through a common biochemical mechanism. However, their role in neuron biology and in MND is not understood. In a yeast two-hybrid screen, we identified the DEAD box protein Ddx20 (gemin3, DP103) as interacting partner of HspB8. Using co-immunoprecipitation, chemical cross-linking, and in vivo quantitative fluorescence resonance energy ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3280277 Wed, 17 Feb 2010 00:00:00 +0100 3280277 http://www.medworm.com/index.php?rid=3263335&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20146106%26dopt%3DAbstract Authors: Li YY, Li XJ, Lv S, Li K, Li YN, Gao ZR, Feng JY, Chen CJ, Schaefer C Acute pancreatitis (AP) is an inflammatory process in which cytokines and chemokines are involved. After onset, extrapancreatic stimuli can induce the expression of cytokines in pancreatic acinar cells, thereby amplifying this inflammatory loop. To further determine the role and mechanism of irritating agents in the pathogenesis of AP, rat pancreatic tissues were stimulated with ascitic fluid (APa) and serum (APs) from rats with AP or with lipopolysaccharide (LPS). In addition, the alteration of heat shock protein 60 (HSP60) expression was evaluated. Rat pancreas was removed and meticulously snipped to fragments. The snips were cultured for up to 48 h. During this period, the tissue viability as well as amyl... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3263335 Wed, 10 Feb 2010 00:00:00 +0100 3263335 http://www.medworm.com/index.php?rid=3239318&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20127215%26dopt%3DAbstract Authors: Tukaj S, Kotlarz A, Jozwik A, Smolenska Z, Bryl E, Witkowski JM, Lipinska B Recent research on the heat shock proteins (Hsps) in chronic inflammatory diseases indicates that Hsps may have disease-suppressive activities. Our aim was to characterize immune response directed to bacterial (DnaJ) and human Hsp40s in patients with rheumatoid arthritis (RA). We found elevated levels of anti-DnaJ, anti-Hdj2, and anti-Hdj3 (but not ant-Hdj1) serum antibodies in the RA patients (P </= 0.001) compared to healthy controls. In peripheral blood mononuclear cells (PBMCs) culture, all tested Hsp40 proteins significantly inhibited the divisions of CD4+ and CD8+ T cells of the RA patients but not those of the controls. Both DnaJ and Hdj2 stimulated secretion of the main anti-inflammatory cyt... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3239318 Tue, 02 Feb 2010 00:00:00 +0100 3239318 http://www.medworm.com/index.php?rid=3189507&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20084477%26dopt%3DAbstract In this study, coimmunoprecipitation was employed to determine if association of HSP70 family members occurs, including Hsp70B' which is present in the human genome but not in mouse and rat. Heteromeric complexes of Hsp70B', Hsp70, and Hsc70 were detected in differentiated human SH-SY5Y neuronal cells. Hsp70B' also formed complexes with Hsp40 suggesting a common co-chaperone for HSP70 family members. PMID: 20084477 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3189507 Tue, 19 Jan 2010 00:00:00 +0100 3189507 http://www.medworm.com/index.php?rid=3189506&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20084478%26dopt%3DAbstract Authors: Gerbin CS, Landgraf R Heat shock protein 90 (HSP90) targets a broad spectrum of client proteins with divergent modes of interaction and consequences. The homologous epidermal growth factor receptor (EGFR) and ERBB2 receptors as well as kinase-deficient mutants thereof differ in their requirement for HSP90 in the nascent versus mature state of the receptor. Specific features of the kinase domain have been implicated for the selective association of HSP90 with mature ERBB2. We evaluated the role of HSP90 for the homologous ERBB3 receptor. ERBB3 is naturally kinase deficient, a central mediator in cell survival and stress response and the primary dimerization partner for ERBB2 in signaling. Cellular studies indicate that, similar to EGFR, the geldanamycin (GA) sensitivity of ERBB... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3189506 Tue, 19 Jan 2010 00:00:00 +0100 3189506 http://www.medworm.com/index.php?rid=3135963&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20043217%26dopt%3DAbstract In this study, we introduce a new component of the stress response: the increase of receptor-mediated uptake of macromolecules from the external environment. We observed that endocytosis of transferrin, which is involved in the delivery of iron to the cell, was increased after stress induced by heat shock or after incubation with inhibitors of Hsp90 function. In both cases, the increase in endocytosis was reverted by inhibition of transcription, suggesting that gene expression is required. Transfection of cells with Hsp70 gene or inhibition of its expression by siRNA confirmed the role of this HSP in the increase of endocytosis. The mechanism for the enhancement of transferrin uptake was related to an accelerated internalization of the ligand-receptor complex as well as an increase in rece... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3135963 Thu, 31 Dec 2009 00:00:00 +0100 3135963 http://www.medworm.com/index.php?rid=3061764&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19960284%26dopt%3DAbstract Authors: Cheng H, Wang L, Wang CC alpha-Synuclein (alphaSyn) is the main component of Lewy bodies formed in midbrain dopaminergic neurons which is a pathological characteristic of Parkinson's disease. It has been recently showed to induce endoplasmic reticulum (ER) stress and impair ER functions. However, the mechanism of how ER responds to alphaSyn toxicity is poorly understood. In the present study, we found that protein disulfide isomerase (PDI), a stress protein abundant in ER, effectively inhibits alphaSyn fibril formation in vitro. In PDI molecule with a structure of abb'xa'c, domain a' was found to be essential and sufficient for PDI to inhibit alphaSyn fibril formation. PDI was further found to be more avid for binding with intermediate species formed during alphaSyn fibril for... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3061764 Fri, 04 Dec 2009 00:00:00 +0100 3061764 http://www.medworm.com/index.php?rid=3049345&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19953350%26dopt%3DAbstract This study describes the localization of CHIP expression in normal rodent brain and the early CHIP response in primary cultures of cortical neurons following ischemic stress models: heat stress (HS) and oxygen-glucose deprivation (OGD). CHIP was highly expressed throughout the brain, predominantly in neurons. The staining pattern was primarily cytoplasmic, although small amounts were seen in the nucleus. More intense nuclear staining was observed in primary cultured neurons which increased with stress. Nuclear accumulation of CHIP occurred within 5-10 min of HS and decreased to baseline levels or lower by 30-60 min. Decrease in nuclear CHIP at 30-60 min of HS was associated with a sharp increase in delayed cell death. While no changes in cytoplasmic CHIP were observed immediately following... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3049345 Wed, 02 Dec 2009 00:00:00 +0100 3049345 http://www.medworm.com/index.php?rid=3049344&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19953351%26dopt%3DAbstract Authors: Ommen G, Chrobak M, Clos J Molecular chaperone proteins play a pivotal role in the protozoan parasite Leishmania donovani, controlling cell fate and ensuring intracellular survival. In higher eukaryotes, the so-called co-chaperone proteins are required for client protein recognition and proper function of chaperones, among them the small glutamine-rich tetratricopeptide repeat proteins (SGT) which interact with both HSP70 and HSP90 chaperones. An atypical SGT homolog is found in the L. donovani genome, encoding a protein lacking the C-terminal glutamine-rich region, normally typical for SGT family members. The gene is expressed constitutively during the life cycle and is essential for survival and/or growth of the parasites. LdSGT forms large, stable complexes that also includ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3049344 Wed, 02 Dec 2009 00:00:00 +0100 3049344 http://www.medworm.com/index.php?rid=3049343&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19953352%26dopt%3DAbstract We examined the HSP response in the foot, hepatopancreas, and kidney tissues of snails exposed to normothermic desiccation. Our findings show variations in the HSP response in both timing and magnitude between the two species. The levels of endogenous Hsp72 in S. cariosa were higher in all the examined tissues, and the induction of Hsp72, Hsp74, and Hsp90 developed earlier than in S. zonata. In contrary, the induction of sHSPs (Hsp25 and Hsp30) was more pronounced in S. zonata compared to S. cariosa. Our results suggest that land snails use HSPs as part of their survival strategy during desiccation and as important components of the aestivation mechanism in the transition from activity to dormancy. Our study underscores the distinct strategy of HSP expression in response to desiccation, na... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3049343 Wed, 02 Dec 2009 00:00:00 +0100 3049343 http://www.medworm.com/index.php?rid=3049346&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19949909%26dopt%3DAbstract Authors: Godman CA, Chheda KP, Hightower LE, Perdrizet G, Shin DG, Giardina C A genome-wide microarray analysis of gene expression was carried out on human microvascular endothelial cells (HMEC-1) exposed to hyperbaric oxygen treatment (HBOT) under conditions that approximated clinical settings. Highly up-regulated genes included immediate early transcription factors (FOS, FOSB, and JUNB) and metallothioneins. Six molecular chaperones were also up-regulated immediately following HBOT, and all of these have been implicated in protein damage control. Pathway analysis programs identified the Nrf-2-mediated oxidative stress response as one of the primary responders to HBOT. Several of the microarray changes in the Nrf2 pathway and a molecular chaperone were validated using quantitative PCR... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3049346 Tue, 01 Dec 2009 00:00:00 +0100 3049346 http://www.medworm.com/index.php?rid=3037170&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19943197%26dopt%3DAbstract Authors: Reuner A, Hengherr S, Mali B, Förster F, Arndt D, Reinhardt R, Dandekar T, Frohme M, Brümmer F, Schill RO Semi-terrestrial tardigrades exhibit a remarkable tolerance to desiccation by entering a state called anhydrobiosis. In this state, they show a strong resistance against several kinds of physical extremes. Because of the probable importance of stress proteins during the phases of dehydration and rehydration, the relative abundance of transcripts coding for two alpha-crystallin heat-shock proteins (Mt-sHsp17.2 and Mt-sHsp19.5), as well for the heat-shock proteins Mt-sHsp10, Mt-Hsp60, Mt-Hsp70 and Mt-Hsp90, were analysed in active and anhydrobiotic tardigrades of the species Milnesium tardigradum. They were also analysed in the transitional stage (I) of dehydration... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3037170 Fri, 27 Nov 2009 00:00:00 +0100 3037170 http://www.medworm.com/index.php?rid=3009364&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19924566%26dopt%3DAbstract Authors: Djurhuus R, Nossum V, Lundsett N, Hovin W, Svardal AM, Havnes MB, Fismen L, Hjelde A, Brubakk AO Heat stress prior to diving has been shown to confer protection against endothelial damage due to decompression sickness. Several lines of evidence indicate a relation between such protection and the heat shock protein (HSP)70 and HSP90 and the major cellular red-ox determinant, glutathione (GSH). The present study has used human endothelial cells as a model system to investigate how heat stress and simulated diving affect these central cellular defense molecules. The results demonstrated for the first time that a simulated dive at 2.6 MPa (26 bar) had a potentiating effect on the heat-induced expression of HSP70, increasing the HSP70 concentration on average 54 times above control... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3009364 Thu, 19 Nov 2009 00:00:00 +0100 3009364 http://www.medworm.com/index.php?rid=3009365&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19921466%26dopt%3DAbstract Authors: Kappé G, Boelens WC, de Jong WW The presence of an alpha-crystallin domain documents the evolutionary relatedness of the ubiquitous family of small heat shock proteins. Sequence and three-dimensional structure provide no evidence for the presence of such a domain in HSPC034, recently proposed as the 11th member of the human HSPB family. Also, phylogenetic analyses detect no relationship between HSPC034 and the human HSPB1-10 sequences. Arguments are provided as to why inclusion in the HSPB family of proteins like HSPC034, which resemble small heat shock proteins in being heat-inducible and having chaperone-like properties and a low monomeric mass, but are evolutionarily unrelated, is misleading and confusing. PMID: 19921466 [PubMed - as supplied by publisher] (Source:... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=3009365 Wed, 18 Nov 2009 00:00:00 +0100 3009365 http://www.medworm.com/index.php?rid=2985605&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19904630%26dopt%3DAbstract In this report we intended to test the effect of lipocalin-2 on the expression of heme oxygenase ((1, 2)) and superoxide dismutase ((1, 2)) which are two strong antioxidants. NGAL was cloned to pcDNA3.1 plasmid by using genetic engineering method. The recombinant vector was transfected to CHO and HEK293T to establish stable cell expressing NGAL and the expression of HO-1, 2 and SOD(1, 2) were compared with appropriate controls by RT-PCR and western blot. On the other hand, expression of NGAL was suppressed by siRNA transfection in order to study the effect of lipocalin-2 on mentioned genes/proteins. The results showed that the expression of HO-1 and SOD(1, 2) enzymes were higher in cells expressing recombinant lipocalin-2 compared with the control cells. Although the expression of HO-1 was... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2985605 Wed, 11 Nov 2009 00:00:00 +0100 2985605 http://www.medworm.com/index.php?rid=2985606&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19902381%26dopt%3DAbstract In this study, we examined the effect of HP (10% O(2), 48 h) on necrosis induced by AA (0% O(2), 24 h) in PC12 cells. We found that HP delayed the regulatory volume decrease and reduced cell swelling after 24 h of exposure to AA. Since aldose reductase (AR) is involved in cell volume regulation, we detected AR mRNA expression with reverse transcription-polymerase chain reaction (RT-PCR) techniques. The AR mRNA level was dramatically elevated by HP. Furthermore, an HP-induced decrease in cell injury was reversed by berberine chloride (BB), the inhibitor of AR. In addition, sorbitol synthesized from glucose catalyzed by AR is directly related to cell volume regulation. Subsequently, we tested sorbitol content in the cytoplasm. HP clearly elevated sorbitol content, while BB inhibited the elev... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2985606 Tue, 10 Nov 2009 00:00:00 +0100 2985606 http://www.medworm.com/index.php?rid=2978240&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19898960%26dopt%3DAbstract Authors: Ma Y, Shimizu Y, Mann MJ, Jin Y, Hendershot LM In response to terminal differentiation signals that enable B cells to produce vast quantities of antibodies, a dramatic expansion of the secretory pathway and a corresponding increase in the molecular chaperones and folding enzymes that aid and monitor immunoglobulin synthesis occurs. Recent studies reveal that the unfolded protein response (UPR), which is normally activated by endoplasmic reticulum (ER) stress, plays a critical role in this process. Although B cells activate all three branches of the UPR in response to pharmacological inducers of the pathway, plasma cell differentiation elicits only a partial UPR in which components of the PKR-like ER kinase (PERK) branch are not expressed. This prompted us to further characteri... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2978240 Sun, 08 Nov 2009 00:00:00 +0100 2978240 http://www.medworm.com/index.php?rid=2955141&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19882236%26dopt%3DAbstract In conclusion, Hsp27 and its antibody concentrations appear to relate to the presence of cardiovascular complications in patients with GI. PMID: 19882236 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2955141 Sat, 31 Oct 2009 00:00:00 +0100 2955141 http://www.medworm.com/index.php?rid=2927935&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19856132%26dopt%3DAbstract Authors: Mymrikov EV, Bukach OV, Seit-Nebi AS, Gusev NB Human alphaB-crystallin and small heat shock proteins HspB6 and HspB8 were mutated so that all endogenous Cys residues were replaced by Ser and the single Cys residue was inserted in a position homologous to that of Cys137 of human HspB1, i.e. in a position presumably located in the central part of beta7 strand of the alpha-crystallin domain. The secondary, tertiary, and quaternary structures of thus obtained Cys-mutants as well as their chaperone-like activity were similar to those of their wild-type counterparts. Mild oxidation of Cys-mutants leads to formation of disulfide bond crosslinking neighboring monomers thus indicating participation of the beta7 strand in intersubunit interaction. Oxidation weakly affects the secondary ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2927935 Sat, 24 Oct 2009 00:00:00 +0100 2927935 http://www.medworm.com/index.php?rid=2912922&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19838832%26dopt%3DAbstract Authors: Marcos-Carcavilla A, Moreno C, Serrano M, Laurent P, Cribiu EP, Andréoletti O, Ruesche J, Weisbecker JL, Calvo JH, Moazami-Goudarzi K Susceptibility to scrapie is mainly controlled by point mutations at the PRNP locus. However, additional quantitative trait loci (QTL) have been identified across the genome including a region in OAR18. The gene which encodes the inducible form of the cytoplasmic Hsp90 chaperone (HSP90AA1) maps within this region and seems to be associated with the resistance/susceptibility to scrapie in sheep. Here, we have analyzed several polymorphisms which were previously described in the ovine HSP90AA1 5' flanking region and in intron 10 in two naturally scrapie infected Romanov sheep populations. First, we have studied 58 ARQ/VRQ animals pertaining t... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2912922 Sat, 17 Oct 2009 23:00:00 +0100 2912922 http://www.medworm.com/index.php?rid=2912921&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19838833%26dopt%3DAbstract In this study, we report that proteasome inhibitors, lactacystin and carbobenzoxy-L: -leucyl-L: -leucyl-L: -leucinal (MG132), induced the accumulation of ubiquitinated proteins as well as a dose- and time-dependent increase in the relative levels of heat shock protein (HSP)30 and HSP70 and their respective mRNAs in Xenopus laevis A6 kidney epithelial cells. In A6 cells recovering from MG132 exposure, HSP30 and HSP70 levels were still elevated after 24 h but decreased substantially after 48 h. The activation of heat shock factor 1 (HSF1) may be involved in MG132-induced hsp gene expression in A6 cells since KNK437, a HSF1 inhibitor, repressed the accumulation of HSP30 and HSP70. Exposing A6 cells to simultaneous MG132 and mild heat shock enhanced the accumulation of HSP30 and HSP70 to a muc... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2912921 Sat, 17 Oct 2009 23:00:00 +0100 2912921 http://www.medworm.com/index.php?rid=2902256&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19830596%26dopt%3DAbstract The objective of this study is to investigate the expression and distribution of heat shock protein 70 (Hsp70) in the intestine of intrauterine growth retardation (IUGR) piglets. Samples from the duodenum, prejejunum, distal jejunum, ileum, and colon of IUGR and normal-body-weight (NBW) piglets were collected at birth. The results indicated that the body and intestine weight of IUGR piglets were significantly lower than NBW piglets. The villus height and villus/crypt ratio in jejunum and ileum of IUGR piglets were significantly reduced compared to NBW piglets. These results indicated that IUGR causes abnormal gastrointestinal morphologies and gastrointestinal dysfunction. The mRNA of hsp70 was increased in prejejunum (P < 0.05), distal jejunum (P < 0.05), and colon in IUGR piglets. H... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2902256 Wed, 14 Oct 2009 23:00:00 +0100 2902256 http://www.medworm.com/index.php?rid=2888566&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19821156%26dopt%3DAbstract Authors: Molvarec A, Tamási L, Losonczy G, Madách K, Prohászka Z, Rigó J Heat shock proteins (Hsps) are ubiquitous and phylogenetically conserved molecules. They are usually considered to be intracellular proteins with molecular chaperone and cytoprotective functions. However, Hsp70 (HSPA1A) is present in the peripheral circulation of healthy nonpregnant and pregnant individuals. In normal pregnancy, circulating Hsp70 levels are decreased, and show a positive correlation with gestational age and an inverse correlation with maternal age. The capacity of extracellular Hsp70 to elicit innate and adaptive proinflammatory (Th1-type) immune responses might be harmful in pregnancy and may lead to the maternal immune rejection of the fetus. Decreased circulating Hsp70 level... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2888566 Sun, 11 Oct 2009 23:00:00 +0100 2888566 http://www.medworm.com/index.php?rid=2872624&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19809895%26dopt%3DAbstract Authors: Lamore SD, Cabello CM, Wondrak GT The differentiated epidermis of human skin serves as an essential barrier against environmental insults from physical, chemical, and biological sources. Zinc pyrithione (ZnPT) is an FDA-approved microbicidal agent used worldwide in clinical antiseptic products, over-the-counter topical antimicrobials, and cosmetic consumer products including antidandruff shampoos. Here we demonstrate for the first time that cultured primary human skin keratinocytes and melanocytes display an exquisite vulnerability to nanomolar concentrations of ZnPT resulting in pronounced induction of heat shock response gene expression and impaired genomic integrity. In keratinocytes treated with nanomolar concentrations of ZnPT, expression array analysis revealed massive u... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2872624 Tue, 06 Oct 2009 23:00:00 +0100 2872624 http://www.medworm.com/index.php?rid=2872625&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19806471%26dopt%3DAbstract Authors: Frydenberg J, Barker JS, Loeschcke V The small heat shock gene (shsp) cluster of Drosophila buzzatii was sequenced and the gene order and DNA sequence were compared with those of the shsps in Drosophila melanogaster. The D. buzzatii shsp cluster contains an inversion and a duplication of hsp26. A phylogenetic tree was constructed based on hsp26 genes from several Drosophila species of the Sophophora and Drosophila subgenera. The tree shows first a separation of the Sophophora and the Drosophila subgenera and then the Drosophila subgenus is divided into the Hawaiian Drosophila and the repleta/virilis groups. Only the latter contain a duplicated hsp26. Comparing the gene organisation of the shsp cluster shows that all the Drosophila subgenus species contain the inversion. Putati... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2872625 Mon, 05 Oct 2009 23:00:00 +0100 2872625 http://www.medworm.com/index.php?rid=2832577&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19777374%26dopt%3DAbstract In conclusion, this study proves an elevation of circulating Hsp70 levels during asthmatic pregnancy compared to healthy pregnant women. However, further studies are warranted to determine the role of circulating Hsp70 in the pathogenesis of maternal and perinatal complications of asthma in pregnancy. PMID: 19777374 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2832577 Wed, 23 Sep 2009 23:00:00 +0100 2832577 http://www.medworm.com/index.php?rid=2832576&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19777375%26dopt%3DAbstract Authors: Seit-Nebi AS, Gusev NB The recently published review by Dreiza et al. (Cell Stress and Chaperones DOI 10.1007/s12192-0090127-8 ) dealing with the functional role of HSPB6 in muscle regulation is critically analyzed. Published data indicate that the chaperone-like activity of HSPB6 is comparable with that of HSPB5 and that phosphorylation of HSPB6 does not affect its oligomeric structure. Different hypotheses concerning the molecular mechanisms of HSPB6 action on smooth muscle contraction and on the reorganization of the cytoskeleton are compared, and it is concluded that although HSPB6 is not a genuine actin-binding protein, it can affect the actin cytoskeleton indirectly. Phosphorylated HSPB6 interacts with 14-3-3 and thereby displaces other binding partners of 14-3-3; among ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2832576 Wed, 23 Sep 2009 23:00:00 +0100 2832576 http://www.medworm.com/index.php?rid=2832575&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19777376%26dopt%3DAbstract Authors: Colson-Proch C, Morales A, Hervant F, Konecny L, Moulin C, Douady CJ Whereas the consequences of global warming at population or community levels are well documented, studies at the cellular level are still scarce. The study of the physiological or metabolic effects of such small increases in temperature (between +2 degrees C and +6 degrees C) is difficult because they are below the amplitude of the daily or seasonal thermal variations occurring in most environments. In contrast, subterranean biotopes are highly thermally buffered (+/-1 degrees C within a year), and underground water organisms could thus be particularly well suited to characterise cellular responses of global warming. To this purpose, we studied genes encoding chaperone proteins of the HSP70 family in amphipod... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2832575 Wed, 23 Sep 2009 23:00:00 +0100 2832575 http://www.medworm.com/index.php?rid=2824933&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19768582%26dopt%3DAbstract Authors: Xing H, Hong Y, Sarge KD Cullin-RING ubiquitin ligases promote the polyubiquitination and degradation of many important cellular proteins, which previous studies indicated can be targeted for degradation via interaction with BTB domain-containing subunits of this E3 ligase complex. PEST domains are known to promote the degradation of proteins that contain them. However, the molecular mechanism by which PEST sequences promote degradation of these proteins is not understood. Here we show that the PEST sequences of a short-lived protein called HSF2 interact with Cullin3, a subunit of a Cullin-RING E3 ubiquitin ligase, and that this interaction mediates the Cul3-dependent ubiquitination and degradation of HSF2. These results indicate how, at the molecular level, PEST sequences can... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2824933 Fri, 18 Sep 2009 23:00:00 +0100 2824933 http://www.medworm.com/index.php?rid=2805179&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19757191%26dopt%3DAbstract Authors: Zhang B, Wang H, Jiang B, Liang P, Liu M, Deng G, Xiao X Nucleolin plays important roles in chromatin structure, rDNA transcription, rRNA maturation, nucleocytoplasmic transport, and ribosome assembly. Although it has been shown to be anti-apoptotic, the underlying mechanisms remain unclear. In the current study, we first examined endogenous nucleolin expression in response to oxidative stress-induced apoptosis in human umbilical vascular endothelial cells (HUVECs). Flow cytometry and caspase activity assays showed that H(2)O(2) treatment caused apoptosis of the cells; reverse-transcription polymerase chain reaction and Western blotting revealed the downregulation of nucleolin expression and increased protein cleavage during this process. Overexpression of nucleolin protein by... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2805179 Sat, 12 Sep 2009 23:00:00 +0100 2805179 http://www.medworm.com/index.php?rid=2768541&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19731087%26dopt%3DAbstract Authors: Henderson B, Calderwood SK, Coates AR, Cohen I, van Eden W, Lehner T, Pockley AG In recent years, it has been hypothesised that a new signalling system may exist in vertebrates in which secreted molecular chaperones form a dynamic continuum between the cellular stress response and corresponding homeostatic physiological mechanisms. This hypothesis seems to be supported by the finding that many molecular chaperones are released from cells and act as extracellular signals for a range of cells. However, this nascent field of biological research seems to suffer from an excessive criticism that the biological activities of molecular chaperones are due to undefined components of the microbial expression hosts used to generate recombinant versions of these proteins. In this article, ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2768541 Thu, 03 Sep 2009 23:00:00 +0100 2768541 http://www.medworm.com/index.php?rid=2721015&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19693705%26dopt%3DAbstract In conclusion, CO treatment seems to provide a good pre-conditioning for the prevention of LPS-induced endothelial injury. PMID: 19693705 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2721015 Wed, 19 Aug 2009 23:00:00 +0100 2721015 http://www.medworm.com/index.php?rid=2692278&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19669938%26dopt%3DAbstract Authors: Liu Y, Liu M, Liu J, Zhang H, Tu Z, Xiao X Krüppel-like factor 4 (KLF4) is a zinc finger-containing transcription factor with diverse regulatory functions in cell growth, proliferation, and differentiation. But little is known about the regulation of KLF4 on the expression of HSP90 (HSP84 and HSP86). In the current study, overexpression of KLF4 was firstly identified to promote the basal expression of HSP90 (HSP84 and HSP86) but not the inducible expression in the C2C12 cells and RAW264.7 cells. Conversely, KLF4 inhibition by antisense oligonucleotides markedly decreased the constitutive expression of HSP90 (HSP84 and HSP86). Here, we also presented data that overexpression of KLF4 resulted in enhanced promoter activities of HSP84. Consistently, KLF4 bind to the KLF4 bind... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2692278 Mon, 10 Aug 2009 23:00:00 +0100 2692278 http://www.medworm.com/index.php?rid=2682627&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19657725%26dopt%3DAbstract Authors: Contreras-Sesvold CL, Sambuughin N, Blokhin A, Deuster PA Heat shock proteins act as molecular chaperones, assist in peptide maturation, and transport nascent peptides across membranes. One commonly studied single nucleotide polymorphism (SNP) for one of the proteins is HSPA1B (+A1538G). However, several studies of this polymorphism have failed to achieve Hardy-Weinberg equilibrium (HWE) for their sample. We compared various published procedures for analyzing the HSPA1B +A1538G SNP and report reasons for HWE discrepancies. Samples from 141 apparently healthy, physically active, volunteers (99 men and 42 women) were analyzed. The first protocol, initially described by Schröder et al., resulted in a genotypic distribution of 22 GG (15.6%), 119 AG (84.4%), and 0 AA; results ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2682627 Wed, 05 Aug 2009 23:00:00 +0100 2682627 http://www.medworm.com/index.php?rid=2640469&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19629754%26dopt%3DAbstract Authors: Fujikawa T, Munakata T, Kondo SI, Satoh N, Wada S The genome of Ciona intestinalis contains eight genes for HSP70 superfamily proteins, 36 genes for J-proteins, a gene for a J-like protein, and three genes for BAG family proteins. To understand the stress responses of genes in the HSP70 chaperone system comprehensively, the transcriptional profiles of these 48 genes under heat stress and endoplasmic reticulum (ER) stress were studied using real-time reverse transcriptase-polymerase chain reaction (RT-PCR) analysis. Heat stress treatment increased the messenger RNA (mRNA) levels of six HSP70 superfamily genes, eight J-protein family genes, and two BAG family genes. In the cytoplasmic group of the DnaK subfamily of the HSP70 family, Ci-HSPA1/6/7-like was the only heat-inducible ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2640469 Wed, 22 Jul 2009 23:00:00 +0100 2640469 http://www.medworm.com/index.php?rid=2630490&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19621276%26dopt%3DAbstract Authors: Vasconsuelo A, Milanesi L, Boland R Exposure to 17beta-estradiol prior to induction of apoptosis protects skeletal muscle cells against damage. The mechanism involved in this protective action of the hormone is poorly understood. In the present study, using the murine muscle cell line C2C12, evidence was obtained that inhibition of H(2)O(2)-induced apoptosis by the estrogen requires the participation of heat shock protein 27 (HSP27). Reverse transcriptase polymerase chain reaction, Western blot, and immunocytochemistry assays showed that 17beta-estradiol induces a time-dependent (5-60 min) increase in the expression of HSP27. In addition, in presence of quercetin, an inhibitor of HSPs, the antiapoptotic effect of the hormone was diminished. More specifically, blockage experime... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2630490 Mon, 20 Jul 2009 23:00:00 +0100 2630490 http://www.medworm.com/index.php?rid=2622334&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19618296%26dopt%3DAbstract In this study, we show that the N. crassa hsp70-1 (NCU09602.3) and hsp70-2 (NCU08693.3) genes are preferentially expressed in an acidic milieu after 15 h of cell growth in sufficient phosphate at 30 degrees C. No significant accumulation of these transcripts was detected at alkaline pH values. Both genes accumulated to a high level in mycelia that were incubated for 1 h at 45 degrees C, regardless of the phosphate concentration and extracellular pH changes. Transcription of the hsp70-1 and hsp70-2 genes was dependent on the pacC (+) background in mycelia cultured under optimal growth conditions or at 45 degrees C. The pacC gene encodes a Zn-finger transcription factor that is involved in the regulation of gene expression by pH. Heat shock induction of these two hsp genes in mycelia incubat... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2622334 Fri, 17 Jul 2009 23:00:00 +0100 2622334 http://www.medworm.com/index.php?rid=2580955&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19579057%26dopt%3DAbstract Authors: Jia Y, Wu SL, Isenberg JS, Dai S, Sipes JM, Field L, Zeng B, Bandle RW, Ridnour LA, Wink DA, Ramchandran R, Karger BL, Roberts DD Thiolutin is a dithiole synthesized by Streptomyces sp. that inhibits endothelial cell adhesion and tumor growth. We show here that thiolutin potently inhibits developmental angiogenesis in zebrafish and vascular outgrowth from tissue explants in 3D cultures. Thiolutin is a potent and selective inhibitor of endothelial cell adhesion accompanied by rapid induction of HSPB1 (Hsp27) phosphorylation. The inhibitory effects of thiolutin on endothelial cell adhesion are transient, potentially due to a compensatory increase in Hsp27 protein levels. Accordingly, heat shock induction of Hsp27 limits the anti-adhesive activity of thiolutin. Thiolutin treatmen... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2580955 Sat, 04 Jul 2009 23:00:00 +0100 2580955 http://www.medworm.com/index.php?rid=2580956&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19578980%26dopt%3DAbstract Authors: Kocsis J, Madaras B, Tóth EK, Füst G, Prohászka Z Many findings indicate that measuring the serum concentration of soluble 70-kD heat shock protein (soluble HSP70) may provide important information in cardiovascular, inflammatory, and pregnancy-related diseases; however, only scarce data are available in cancer. Therefore, using a commercial ELISA kit, we measured soluble HSP70 concentration in the sera of 179 patients with colorectal cancer. We investigated the relationship between soluble HSP70 concentration and mortality, during 33.0 (24.4-44.0) months long follow-up. High (>1.65 pg/ml, median concentration) soluble HSP70 level was a significant (hazard ratio: 1.88 (1.20-2.96, p = 0.005) predictor of mortality during the follow-up period. When we compared ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2580956 Fri, 03 Jul 2009 23:00:00 +0100 2580956 http://www.medworm.com/index.php?rid=2563011&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19568960%26dopt%3DAbstract Authors: Dreiza CM, Komalavilas P, Furnish EJ, Flynn CR, Sheller MR, Smoke CC, Lopes LB, Brophy CM The small heat shock protein, HSPB6, is a 17-kDa protein that belongs to the small heat shock protein family. HSPB6 was identified in the mid-1990s when it was recognized as a by-product of the purification of HSPB1 and HSPB5. HSPB6 is highly and constitutively expressed in smooth, cardiac, and skeletal muscle and plays a role in muscle function. This review will focus on the physiologic and biochemical properties of HSPB6 in smooth, cardiac, and skeletal muscle; the putative mechanisms of action; and therapeutic implications. PMID: 19568960 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2563011 Tue, 30 Jun 2009 23:00:00 +0100 2563011 http://www.medworm.com/index.php?rid=2563012&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19565356%26dopt%3DAbstract Authors: Corradetti A, Saccucci F, Emanuelli M, Vagnoni G, Cecati M, Sartini D, Giannubilo SR, Tranquilli AL Mitogen-activated protein kinase (MAPK) p38alpha was shown to be implicated in the organogenesis of the placenta, and such placental alteration is crucial for the development of hemolysis, elevated liver enzymes, and low platelets (HELLP) syndrome. We aimed to analyze for the first time human placental expression of MAPK p38alpha in pregnancies complicated by HELLP. The placental expression of MAPK p38alpha was investigated by semiquantitative polymerase chain reaction using cDNA extracted from placental tissue of 15 pregnancies with HELLP syndrome and 15 gestational age-matched controls. Seven patients with HELLP also had intrauterine fetal growth restriction (IUGR). In placent... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2563012 Mon, 29 Jun 2009 23:00:00 +0100 2563012 http://www.medworm.com/index.php?rid=2550486&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19557548%26dopt%3DAbstract Authors: Bellmann K, Charette SJ, Nadeau PJ, Poirier DJ, Loranger A, Landry J The cellular response to heat shock (HS) is a paradigm for many human diseases collectively known as "protein conformation diseases" in which the accumulation of misfolded proteins induces cell death. Here, we analyzed how cells having a different apoptotic threshold die subsequent to a treatment with HS. Cells with a low apoptotic threshold mainly induced apoptosis through activation of conventional stress kinase signaling pathways. By contrast, cells with a high apoptotic threshold also died by apoptosis but likely after the accumulation of heat-aggregated proteins as revealed by the formation of aggresomes in these cells, which were associated with the generation of atypical nuclear deformations. Inhibitio... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2550486 Thu, 25 Jun 2009 23:00:00 +0100 2550486 http://www.medworm.com/index.php?rid=2526298&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19551494%26dopt%3DAbstract Authors: Dokladny K, Lobb R, Wharton W, Ma TY, Moseley PL Heat shock protein (HSP)70 provides a spectrum of protection against any of a variety of stresses, preventing damage measured at the level of molecules, cells, as well as whole organism. We have previously reported that lipopolysaccharide (LPS)-induced lethality in rats is prevented by a previous exposure to a mild thermal stress and that a thermal stress sufficient to induce HSP70 expression in the liver is accompanied by an inhibition of endotoxin-mediated cytokines and modulation of febrile response. However, the effect of HSP70 upregulation on cytokine expression in animals is unknown. The aim of the present study was to demonstrate the effect of HSP70 overexpression with adenovirus administration on LPS-induced increase in ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526298 Tue, 23 Jun 2009 23:00:00 +0100 2526298 http://www.medworm.com/index.php?rid=2526307&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19496024%26dopt%3DAbstract In this study, the full-length complementary DNA (cDNA) of a novel inducible cytosolic Hsp70 family member (FcHsp70) was cloned from Fenneropenaeus chinensis. FcHsp70 full-length cDNA consists of 2,511 bp with a 1,890-bp open reading frame encoding 629 amino acids. Three Hsp70 protein family signatures, IDLGTTYS, IIDLGGGTFDVSIL, and IVLVGGSTRIPKVQK, were found in the predicted FcHsp70 amino acid sequence. Phylogenetic analysis showed that FcHsp70 was categorized together with the inducible HSP70s reported in other crustaceans. Compared to the previously identified cognate Hsp70 (FcHsc70) in F. chinensis, the expression of FcHsp70 showed quite different expression profiles when the shrimp were subjected to different stresses including heat shock and heavy metal treatments. Under heat shock ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526307 Wed, 03 Jun 2009 23:00:00 +0100 2526307 http://www.medworm.com/index.php?rid=2526304&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19496025%26dopt%3DAbstract In this study, several polymorphisms in the gene encoding the inducible form of the cytoplasmic Hsp90 (HSP90AA1) were addressed in 24 sheep breeds reared in different climatic regions of Europe, Africa, and Asia. Significant differences in the genotype frequencies for a C/G single nucleotide polymorphism (SNP) located at position -660 in the HSP90AA1 5'flanking region were found between the different breeds. Regression analyses reflected significant correlations (from 0.41 to 0.62) between the alternative genotypes of this polymorphism and several climatic and geographic variables characteristic of the regions where these breeds are reared. Real-time analysis revealed that animals bearing the CC(-660) genotype presented higher expression levels than those presenting the CG(-660) or GG(-660... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526304 Wed, 03 Jun 2009 23:00:00 +0100 2526304 http://www.medworm.com/index.php?rid=2526301&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19496026%26dopt%3DAbstract Authors: Sonna LA, Hawkins L, Lissauer ME, Maldeis P, Towns M, Johnson SB, Moore R, Singh IS, Cowan MJ, Hasday JD Environmental hyperthermia and exercise produce extensive changes in gene expression in human blood cells, but it is unknown whether this also happens during febrile-range hyperthermia. We tested the hypothesis that heat shock protein (HSP) and immunomodulatory stress gene expression correlate with fever in intensive care unit patients. Whole blood messenger RNA was obtained over consecutive days from 100 hospitalized patients suffering from sepsis or noninfectious systemic inflammatory response syndrome (SIRS) as defined by conventional criteria. The most abnormal body temperature in the preceding 24 h was recorded for each sample. Expression analysis was performed using t... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526301 Wed, 03 Jun 2009 23:00:00 +0100 2526301 http://www.medworm.com/index.php?rid=2526312&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19472074%26dopt%3DAbstract Authors: Yerbury JJ, Wilson MR Alzheimer's disease is characterised by the inappropriate death of brain cells and accumulation of the Abeta peptide in the brain. Thus, it is possible that there are fundamental differences between Alzheimer's disease patients and healthy individuals in their abilities to clear Abeta from brain fluid and to protect neurons from Abeta toxicity. In the present study, we examined (1) the cytotoxicity of Alzheimer's disease cerebrospinal fluid (CSF) compared to control CSF, (2) the ability of Alzheimer's disease and control CSF to protect cells from Abeta toxicity and to promote cell-mediated clearance of Abeta and lastly (3) the effects of extracellular chaperones, normally found in CSF, on these processes. We show that the Alzheimer's disease CSF samples t... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526312 Tue, 26 May 2009 23:00:00 +0100 2526312 http://www.medworm.com/index.php?rid=2526310&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19472075%26dopt%3DAbstract Authors: Wieten L, van der Zee R, Goedemans R, Sijtsma J, Serafini M, Lubsen NH, van Eden W, Broere F Stress proteins such as heat shock proteins (Hsps) are up-regulated in cells in response to various forms of stress, like thermal and oxidative stress and inflammation. Hsps prevent cellular damage and increase immunoregulation by the activation of anti-inflammatory T-cells. Decreased capacity for stress-induced Hsp expression is associated with immune disorders. Thus, therapeutic boosting Hsp expression might restore or enhance cellular stress resistance and immunoregulation. Especially food- or herb-derived phytonutrients may be attractive compounds to restore optimal Hsp expression in response to stress. In the present study, we explored three readout systems to monitor Hsp70 expres... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526310 Tue, 26 May 2009 23:00:00 +0100 2526310 http://www.medworm.com/index.php?rid=2526314&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19455405%26dopt%3DAbstract Authors: Pace V, Bellizzi D, Giordano F, Panno ML, De Benedictis G Apoptosis is a programmed cell death process, whose complexity led researchers to build mathematical models that could help to identify its crucial steps. In previous works, we theoretically analyzed and numerically simulated a model that describes a pathway from an external stimulus to caspase-3 activation. Here, the results of experiments performed on populations of synchronized cells treated with the inducer Apo2L/TRAIL are reported and are compared with model predictions. In particular, we have compared in vitro and in silico results relevant to the time evolutions of caspase-3 and caspase-8 activities, as well as of the dead cells fractions. In addition, the effect of the BAR gene silencing was evaluated. Caspase-3... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526314 Tue, 19 May 2009 23:00:00 +0100 2526314 http://www.medworm.com/index.php?rid=2526315&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19415527%26dopt%3DAbstract Authors: Mills DR, Haskell MD, Callanan HM, Flanagan DL, Brilliant KE, Yang D, Hixson DC We previously described a cell surface reactive monoclonal antibody, MAb OC.10, which recognizes an epitope shared by rat fetal liver ductal cells, hepatic progenitor cells, mature cholangiocytes, and hepatocellular carcinomas (HCC). Here, intrasplenic injection of MAb OC.10 into newborn rats was shown by immunofluorescence microscopy to strongly label intrahepatic bile ducts. Furthermore, the in situ labeling of intrahepatic cholangiocytes by injecting MAb OC.10 increased the number of intraportal and intralobular bile ducts with well-defined lumens when compared to IgM-injected control animals. The antigen for MAb OC.10 was identified by mass spectrometry as Hsc70, a constitutively expressed heat... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526315 Mon, 04 May 2009 23:00:00 +0100 2526315 http://www.medworm.com/index.php?rid=2526317&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19412742%26dopt%3DAbstract Authors: Wang X, Liu X, Kong R, Zhan R, Wang X, Leng X, Gong J, Duan M, Wang L, Wu L, Qian L NGFI-B/Nur77/TR3, originally identified as an immediate-early gene rapidly induced by serum and growth factors, is a member of the steroid hormone nuclear receptor superfamily with no identified endogenous ligand. NGFI-B induces apoptosis in a number of cell lineages exposed to proapoptotic stimuli by directly targeting the mitochondria, inducing cytochrome c release. The present study was designed to determine the role of NGFI-B in cardiomyocytes of restraint-stressed rats. The NGFI-B content was increased in mitochondria and reduced in plasma as apoptosis increased. Analysis showed that NGFI-B induces cardiomyocyte apoptosis in restraint-stressed rats by mediating mitochondrial energy metabol... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526317 Sat, 02 May 2009 23:00:00 +0100 2526317 http://www.medworm.com/index.php?rid=2526319&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19412660%26dopt%3DAbstract In this study, by using bovine aortic endothelial cells, we demonstrate that the inhibitory effect of endogenously generated NO by nitric oxide synthase (NOS) activation, by either NOS stimulators or association with heat shock protein 90 (Hsp90), is significant only at high prevailing pO(2) through nitrosation of mitochondrial ETC complexes, but it does not inhibit the respiration by competitive binding at CcO at very low pO(2). ETC complexes activity measurements confirmed that significant reduction in complex IV activity was noticed at higher pO(2), but it was unaffected at low pO(2) in these cells. This was further extended to heat-shocked cells, where NOS was activated by the induction/activation of (Hsp90) through heat shock at an elevated temperature of 42 degrees C. From these resu... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526319 Fri, 01 May 2009 23:00:00 +0100 2526319 http://www.medworm.com/index.php?rid=2526321&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19404777%26dopt%3DAbstract Authors: Clark MS, Peck LS The Antarctic limpet, Nacella concinna, exhibits the classical heat shock response, with up-regulation of duplicated forms of the inducible heat shock protein 70 (HSP70) gene in response to experimental manipulation of seawater temperatures. However, this response only occurs in the laboratory at temperatures well in excess of any experienced in the field. Subsequent environmental sampling of inter-tidal animals also showed up-regulation of these genes, but at temperature thresholds much lower than those required to elicit a response in the laboratory. It was hypothesised that this was a reflection of the complexity of the stresses encountered in the inter-tidal region. Here, we describe a further series of experiments comprising both laboratory manipulation ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526321 Wed, 29 Apr 2009 23:00:00 +0100 2526321 http://www.medworm.com/index.php?rid=2526323&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19396626%26dopt%3DAbstract Authors: Tsaytler PA, Krijgsveld J, Goerdayal SS, Rüdiger S, Egmond MR Hsp90 is an essential eukaryotic molecular chaperone that stabilizes a large set of client proteins, many of which are involved in various cellular signaling pathways. The current list of Hsp90 interactors comprises about 200 proteins and this number is growing steadily. In this paper, we report on the application of three complementary proteomic approaches directed towards identification of novel proteins that interact with Hsp90. These methods are coimmunoprecipitation, pull down with biotinylated geldanamycin, and immobilization of Hsp90beta on sepharose. In all, this study led to the identification of 42 proteins, including 18 proteins that had not been previously characterized as Hsp90 interactors. These n... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526323 Sat, 25 Apr 2009 23:00:00 +0100 2526323 http://www.medworm.com/index.php?rid=2526326&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19373565%26dopt%3DAbstract Authors: Sung YY, Dhaene T, Defoirdt T, Boon N, Macrae TH, Sorgeloos P, Bossier P Feeding of bacterially encapsulated heat shock proteins (Hsps) to invertebrates is a novel way to limit Vibrio infection. As an example, ingestion of Escherichia coli overproducing prokaryotic Hsps significantly improves survival of gnotobiotically cultured Artemia larvae upon challenge with pathogenic Vibrio campbellii. The relationship between Hsp accumulation and enhanced resistance to infection may involve DnaK, the prokaryotic equivalent to Hsp70, a major molecular chaperone in eukaryotic cells. In support of this proposal, heat-stressed bacterial strains LVS 2 (Bacillus sp.), LVS 3 (Aeromonas hydrophila), LVS 8 (Vibrio sp.), GR 8 (Cytophaga sp.), and GR 10 (Roseobacter sp.) were shown in this work t... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526326 Thu, 16 Apr 2009 23:00:00 +0100 2526326 http://www.medworm.com/index.php?rid=2526333&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19357992%26dopt%3DAbstract Authors: Pockley AG, Calderwood SK, Multhoff G Although heat shock (stress) proteins are typically regarded as being exclusively intracellular molecules, it is now apparent that they can be released from cells in the absence of cellular necrosis. We and others have reported the presence of Hsp60 (HSPD1) and Hsp70 (HSPA1A) in the circulation of normal individuals and our finding that increases in carotid intima-media thicknesses (a measure of atherosclerosis) in subjects with hypertension at a 4-year follow-up are less prevalent in those having high serum Hsp70 (HSPA1A) levels at baseline suggests that circulating Hsp70 (HSPA1A) has atheroprotective effects. Given that circulating Hsp70 (HSPA1A) levels can be in the range which has been shown to elicit a number of biological effects in ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2526333 Wed, 08 Apr 2009 23:00:00 +0100 2526333 http://www.medworm.com/index.php?rid=2301021&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19333787%26dopt%3DAbstract In this study, we reinvestigated the effect of CBX on the induction of HSPs in HeLa and human neuroblastoma (A-172) cells. CBX clearly induced not only Hsp70 but also Hsp90 (HSPC1), Hsp40 (DNAJB1), and Hsp27 (HSPB1) at concentrations of 10 to 800 muM for 16 h incubation. At higher concentrations (more than 400 muM), however, CBX appeared to be toxic. Treatment of cells with CBX resulted in enhanced phosphorylation and acquisition of DNA-binding ability of heat shock transcription factor 1 (HSF1). Furthermore, characteristic HSF1 granules were formed in the nucleus, suggesting that the induction of HSPs by CBX is mediated by the activation of HSF1. Furthermore, thermotolerance was induced by CBX treatment, as determined by clonogenic survival. Although the precise target of CBX is not known... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2301021 Tue, 31 Mar 2009 04:00:00 +0100 2301021 http://www.medworm.com/index.php?rid=2285407&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19301149%26dopt%3DAbstract Authors: Konstantinidis D, Paletas K, Koliakos G, Kaloyianni M Leptin, a 16-kDa cytokine produced mainly by the adipose tissue, is known to increase energy expenditure while at the same time lowering food intake by acting directly on the hypothalamus. ObRb, the leptin receptor mostly involved in intracellular signaling, is expressed in a wide range of tissues, thus allowing leptin to affect a much broader diversity of biological processes. High concentrations of leptin are encountered in patients with hyperleptinemia, a condition which very often accompanies obesity and which is a direct result of leptin resistance. In the present study, moderate and high concentrations of leptin (16 and 160 ng/ml) were mostly utilized in order to investigate the role of this cytokine in oxidative stre... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2285407 Fri, 20 Mar 2009 04:00:00 +0100 2285407 http://www.medworm.com/index.php?rid=2275197&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19294532%26dopt%3DAbstract Authors: Ganesan B, Anandan R Myocardial infarction is one of the most common manifestations of cardiovascular disease. In the present study, we investigated the protective effect of betaine, a potent lipotropic molecule, on changes in the levels of lysosomal enzymes and lipid peroxidation in isoprenaline-induced myocardial infarction in Wistar rats, an animal model of myocardial infarction in man. Male albino Wistar rats were pretreated with betaine (250 mg/kg body weight) daily for a period of 30 days. After the treatment period, isoprenaline (11 mg/100 g body weight) was intraperitoneally administered to rats at intervals of 24 h for 2 days. The activities of lysosomal enzymes (beta-glucuronidase, beta-galactosidase, beta-glucosidase, and acid phosphatase) were significantly (p <... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2275197 Wed, 18 Mar 2009 04:00:00 +0100 2275197 http://www.medworm.com/index.php?rid=2275198&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19291423%26dopt%3DAbstract Authors: Banerjee Mustafi S, Chakraborty PK, Dey RS, Raha S Chinese hamster lung fibroblasts V79 cells were treated with heat stress for 4 weeks with short duration (15 min) heat shock every alternate day in culture. It was observed that Hsp 70 and the antioxidant enzyme MnSOD became overexpressed during the chronic heat stress period. Both p38 MAPK and Akt became phosphorylated by chronic heat stress exposure. Simultaneous exposure to SB203580, a potent and specific p38MAPK inhibitor drastically inhibited the phosphorylation of p38MAPK and Akt. Furthermore, exposure to SB203580 also blocked the increase in Hsp70 and MnSOD levels and the elevated SOD activity brought about by chronic heat stress. Heat shock factor 1 (HSF1) transcriptional activity and nuclear translocation of HSF1 were... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2275198 Tue, 17 Mar 2009 04:00:00 +0100 2275198 http://www.medworm.com/index.php?rid=2261232&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19280368%26dopt%3DAbstract Authors: Johnson TK, Carrington LB, Hallas RJ, McKechnie SW Transcripts of the Drosophila hsr-omega gene are known to interact with RNA processing factors and ribosomes and are postulated to aid in co-ordinating nuclear and cytoplasmic activities particularly in stressed cells. However, the significance of these interactions for physiological processes and in turn for whole-organism fitness remains an open question. Because hsr-omega's cellular expression characteristics suggest it may influence protein synthesis, and because both genotypic and expression variation of hsr-omega have been associated with thermotolerance, we characterised 30 lines for variation in the rates of protein synthesis, measured in ovarian tissues, both before and after a mild heat shock, and for basal levels of... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2261232 Thu, 12 Mar 2009 04:00:00 +0100 2261232 http://www.medworm.com/index.php?rid=2261231&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19280369%26dopt%3DAbstract In conclusion, these results show that we have cloned a splice variant of mortalin with a novel catecholamine binding function and that this chaperone-like protein may be neuroprotective in dopamine-related central nervous system disorders. PMID: 19280369 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2261231 Thu, 12 Mar 2009 04:00:00 +0100 2261231 http://www.medworm.com/index.php?rid=2218455&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19238587%26dopt%3DAbstract Authors: Tucker NR, Ustyugov A, Bryantsev AL, Konkel ME, Shelden EA Constitutive expression of Hsp27 has been demonstrated in vertebrate embryos, especially in developing skeletal and cardiac muscle. Results of several previous studies have indicated that Hsp27 could play a role in the development of these tissues. For example, inhibition of Hsp27 expression has been reported to cause defective development of mammalian myoblasts in vitro and frog embryos in vivo. In contrast, transgenic mice lacking Hsp27 develop normally. Here, we examined the distribution of Hsp27 protein in developing and adult zebrafish and effects of suppressing Hsp27 expression using phosphorodiamidate morpholino oligonucleotides (PMO) on zebrafish development. Consistent with our previous analysis of hsp27 messe... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2218455 Tue, 24 Feb 2009 05:00:00 +0100 2218455 http://www.medworm.com/index.php?rid=2202460&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19224397%26dopt%3DAbstract In this study, we have investigated the relationship between chaperonin/co-chaperonin binding, ATP hydrolysis, and protein refolding in heterologous chaperonin systems from bacteria, chloroplast, and mitochondria. We characterized two types of chloroplast cpn60 oligomers, ch-cpn60 composed of alpha and beta subunits (alpha(7)beta(7) ch-cpn60) and one composed of all beta subunits (beta(14) ch-cpn60). In terms of ATPase activity, the rate of ATP hydrolysis increased with protein concentration up to 60 muM, reflecting a concentration at which the oligomers are stable. At high concentrations of cpn60, all cpn10 homologs inhibited ATPase activity of alpha(7)beta(7) ch-cpn60. In contrast, ATPase of beta(14) ch-cpn60 was inhibited only by mitochondrial cpn10, supporting previous reports showing ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2202460 Wed, 18 Feb 2009 05:00:00 +0100 2202460 http://www.medworm.com/index.php?rid=2202459&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19224398%26dopt%3DAbstract In this study, the role of Hsp27 in regulating actin filament dynamics is further investigated. Hsp27 protein levels were reduced using siRNA in SW480 cells, a human colon cancer cell line. An in vitro wound closure assay showed that cells with knocked down Hsp27 levels were unable to close wounds, indicating that this protein is involved in regulating cell motility. Immunoprecipitation pull down assays were done, to observe if and when Hsp27 and actin are in the same complex within the cell, before and after heat shock. At all time points tested, Hsp27 and actin were present in the same cell lysate fraction. Lastly, indirect immunostaining was done before and after heat shock to evaluate Hsp27 and actin interaction in cells. Hsp27 and actin showed colocalization before heat shock, little ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2202459 Wed, 18 Feb 2009 05:00:00 +0100 2202459 http://www.medworm.com/index.php?rid=2196221&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19221896%26dopt%3DAbstract Authors: Padmini E, Vijaya Geetha B Mitochondrial heat shock protein 70 (mtHSP70) is found to play a primary role in cellular defense against physiological stress like exposure to environmental contaminants and helpful in the maintenance of cellular homeostasis by promoting the cell survival. In the present investigation, the environmental-stress-induced increase in mtHSP70 levels along with the quantification of apoptosis signal regulating kinase 1 (ASK1) and thioredoxin (Trx) were measured in the liver mitochondria of grey mullets (Mugil cephalus) collected from the polluted Ennore estuary and the unpolluted Kovalam estuary for a period of 2 years. The results showed elevated lipid peroxide (LPO) and decreased total antioxidant capacity along with the decrease in mitochondrial viabil... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2196221 Tue, 17 Feb 2009 05:00:00 +0100 2196221 http://www.medworm.com/index.php?rid=2196220&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19221897%26dopt%3DAbstract Authors: Tulapurkar ME, Asiegbu BE, Singh IS, Hasday JD Expression of heat shock proteins (HSPs) is classically activated at temperatures above the physiologic range (>/=42 degrees C) via activation of the stress-activated transcription factor, heat shock factor-1 (HSF-1). Several studies suggest that less extreme hyperthermia, especially within the febrile range, as occurs during fever and exertional/environmental hyperthemia, can also activate HSF-1 and enhance HSP expression. We compared HSP72 protein and mRNA expression in human A549 lung epithelial cells continuously exposed to 38.5 degrees C, 39.5 degrees C, or 41 degrees C or exposed to a classic heat shock (42 degrees C for 2 h). We found that expression of HSP72 protein and mRNA increased linearly as incubation temperature ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2196220 Tue, 17 Feb 2009 05:00:00 +0100 2196220 http://www.medworm.com/index.php?rid=2192362&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19214782%26dopt%3DAbstract In conclusion, p38 MAPK-induced myocardial ischemic injury is not modulated by MK2. However, the absence of MK2 perturbs the cellular distribution of p38. The preserved nuclear distribution of active p38 MAPK in MK2(-/-) hearts and the conserved response to SB203580 suggests that activation of p38 MAPK may contribute to injury independently of MK2. PMID: 19214782 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2192362 Fri, 13 Feb 2009 05:00:00 +0100 2192362 http://www.medworm.com/index.php?rid=2192361&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19214783%26dopt%3DAbstract Authors: Chow AM, Ferrier-Pagès C, Khalouei S, Reynaud S, Brown IR The effect of increased light intensity and heat stress on heat shock protein Hsp60 was examined in two coral species using a branched coral and a laminar coral, selected for their different resistance to environmental perturbation. Transient Hsp60 induction was observed in the laminar coral following either light or thermal stress. Sustained induction was observed when these stresses were combined. The branched coral exhibited comparatively weak transient Hsp60 induction after heat stress and no detectable induction following light stress, consistent with its susceptibility to bleaching in native environments compared to the laminar coral. Our observations also demonstrate that increased light intensity and heat s... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2192361 Thu, 12 Feb 2009 05:00:00 +0100 2192361 http://www.medworm.com/index.php?rid=2184854&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19205928%26dopt%3DAbstract In conclusion, anti-Hsp60 and anti-Hsp70 antibodies as naturally occurring autoantibodies are present in the peripheral circulation of healthy pregnant women. Nevertheless, humoral immunity against heat shock proteins was not associated with preeclampsia. Further studies are warranted to explore the role of heat shock proteins and immune reactivity to them in the immunobiology of normal pregnancy and preeclampsia. PMID: 19205928 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2184854 Wed, 11 Feb 2009 05:00:00 +0100 2184854 http://www.medworm.com/index.php?rid=2108580&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19145477%26dopt%3DAbstract In this study, we utilized Hsp70-overexpressing mice to determine whether Hsp70 is protective in vivo. Both Hsp70-overexpressing mice and their wild-type littermates were treated with systemic kanamycin (700 mg/kg body weight) twice daily for 14 days. While kanamycin treatment resulted in significant hearing loss and hair cell death in wild-type mice, Hsp70-overexpressing mice were significantly protected against aminoglycoside-induced hearing loss and hair cell death. These data indicate that Hsp70 is protective against aminoglycoside-induced ototoxicity in vivo. PMID: 19145477 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2108580 Thu, 15 Jan 2009 05:00:00 +0100 2108580 http://www.medworm.com/index.php?rid=2098608&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19137416%26dopt%3DAbstract Authors: Chen X, Kang H, Zou F Oxidative stress can be a significant cause of cell death and apoptosis. We performed studies in HepG2 cells to explore whether prior exposure to oxidative stress ("oxidative preconditioning") and geldanamycin (GA) treatment can protect the cell from damage caused by subsequent oxidative insults. The cells were treated with 10 nM GA for 24 h before oxidative stress. Oxidative preconditioning was achieved by 2 h exposures to H(2)O(2) (50 muM) separated by a 10-h recovery period in normal culture medium. Oxidative stress was induced by exposure to 500 muM H(2)O(2) for 24 h. The effects of GA and oxidative preconditioning were investigated on the formation of Hsp90, vimentin, insoluble vimentin aggregates, and cleavage of vimentin in a cell culture model of ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2098608 Sat, 10 Jan 2009 05:00:00 +0100 2098608 http://www.medworm.com/index.php?rid=2090739&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19130302%26dopt%3DAbstract Authors: Ueda N, Boettcher A For a variety of species, changes in the expression of heat shock proteins (HSP) have been linked to key developmental changes, i.e., gametogenesis, embryogenesis, and metamorphosis. Many marine invertebrates are known to have a biphasic life cycle where pelagic larvae go through settlement and metamorphosis as they transition to the benthic life stage. A series of experiments were run to examine the expression of heat shock protein 70 (HSP 70) during larval and early spat (initial benthic phase) development in the Eastern oyster, Crassostrea virginica. In addition, the impact of thermal stress on HSP 70 expression during these early stages was studied. C. virginica larvae and spat expressed three HSP 70 isoforms, two constitutive, HSC 77 and HSC 72, and on... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2090739 Thu, 08 Jan 2009 05:00:00 +0100 2090739 http://www.medworm.com/index.php?rid=2087861&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19127412%26dopt%3DAbstract In this study, hydrogen peroxide (H(2)O(2))-induced apoptosis, upregulation of Foxa1, and the role of Foxa1 in the regulation of bcl2 gene expression were studied in A549 type II pneumocytes. H(2)O(2) upregulated Foxa1 mRNA and protein in a time- and dose-dependent manner. Overexpression of Foxa1 promoted apoptosis, whereas Foxa1 deficiency, induced by antisense oligonucleotides, decreased A549 cell apoptosis induced by H(2)O(2), as shown by flow cytometry. Moreover, Foxa1 overexpression decreased the expression of bcl2, while Foxa1 depletion increased the expression of bcl2. Electrophoretic mobility shift assay and chromatin immunoprecipitation revealed that Foxa1 bound to bcl2 promoter, and H(2)O(2) promoted its DNA binding activity. Luciferase reporter showed that Foxa1 also decreased t... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2087861 Wed, 07 Jan 2009 05:00:00 +0100 2087861 http://www.medworm.com/index.php?rid=2063044&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19105051%26dopt%3DAbstract Authors: Zhang K, Zhao T, Huang X, Liu ZH, Xiong L, Li MM, Wu LY, Zhao YQ, Zhu LL, Fan M It has been shown that induction of HSP70 by administration of geranylgeranylacetone (GGA) leads to protection against ischemia/reperfusion injury. The present study was performed to determine the effect of GGA on the survival of mice and on brain damage under acute hypobaric hypoxia. The data showed that the mice injected with GGA survived significantly longer than control animals (survival time of 9.55 +/- 3.12 min, n = 16 vs. controls at 4.28 +/- 4.29 min, n = 15, P < 0.005). Accordingly, the cellular necrosis or degeneration of the hippocampus and the cortex induced by sublethal hypoxia for 6 h could be attenuated by preinjection with GGA, especially in the CA2 and CA3 regions of the hippoca... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2063044 Tue, 23 Dec 2008 05:00:00 +0100 2063044 http://www.medworm.com/index.php?rid=2048700&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19089598%26dopt%3DAbstract Authors: Kotoglou P, Kalaitzakis A, Vezyraki P, Tzavaras T, Michalis LK, Dantzer F, Jung JU, Angelidis C For many years, there has been uncertainty concerning the reason for Hsp70 translocation to the nucleus and nucleolus. Herein, we propose that Hsp70 translocates to the nucleus and nucleoli in order to participate in pathways related to the protection of the nucleoplasmic DNA or ribosomal DNA from single-strand breaks. The absence of Hsp70 in HeLa cells, via Hsp70 gene silencing (knockdown), indicated the essential role of Hsp70 in DNA integrity. Therefore, HeLa Hsp70 depleted cells were very sensitive in heat treatment and their DNA breaks were multiple compared to that of control HeLa cells. The molecular mechanism with which Hsp70 performs its role at the level of nucleus and nuc... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2048700 Wed, 17 Dec 2008 05:00:00 +0100 2048700 http://www.medworm.com/index.php?rid=2042558&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19085089%26dopt%3DAbstract In this study, we focused on five polymorphisms in three genes (HSPA1A, HSPA1B, and HSPA1L) of Hsp70 family to explore the genetic contribution, alone and in combination, of these polymorphisms to essential hypertension risk in a Uygur population. Genotyping was performed using PCR-RFLP and direct sequencing techniques. Data were analyzed using haplotype and multifactor dimensionality reduction (MDR) methods. Genotype distributions of all the polymorphisms satisfied the Hardy-Weinberg proportions in cases and controls. Statistical significance was only observed in the genotype (P = 0.0028) and (P = 0.0146) allele distributions of -110A/C polymorphism, with the -110C allele conferring a 1.45- and 2.83-fold of relative risk, assuming the additive and recessive models, respectively, and in 12... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=2042558 Tue, 16 Dec 2008 05:00:00 +0100 2042558 http://www.medworm.com/index.php?rid=1956467&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19002605%26dopt%3DAbstract Authors: Farcy E, Voiseux C, Lebel JM, Fiévet B During the annual cycle, oysters are exposed to seasonal slow changes in temperature, but during emersion at low tide on sunny summer days, their internal temperature may rise rapidly, resulting in acute heat stress. We experimentally exposed oysters to a 1-h acute thermal stress and investigated the transcriptional expression level of some genes involved in cell stress defence mechanisms, including chaperone proteins (heat shock proteins Hsp70, Hsp72 and Hsp90 (HSP)), regulation of oxidative stress (Cu-Zn superoxide dismutase, metallothionein (MT)), cell detoxification (glutathione S-transferase sigma, cytochrome P450 and multidrug resistance (MDR1)) and regulation of the cell cycle (p53). Gene mRNA levels were quantified by reverse... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1956467 Tue, 11 Nov 2008 05:00:00 +0100 1956467 http://www.medworm.com/index.php?rid=1944301&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18989758%26dopt%3DAbstract Authors: Huang M, Wei JN, Peng WX, Liang J, Zhao C, Qian Y, Dai G, Yuan J, Pan FY, Xue B, Sha JH, Li CJ The cell cycle is controlled by regulators functioning at the right time and at the right place. We have found that calmodulin (CaM) has specific distribution patterns during different cell-cycle stages. Here, we identify cell-cycle-specific binding proteins of CaM and examine their function during cell-cycle progression. We first applied immunoprecipitation methods to isolate CaM-binding proteins from cell lysates obtained at different cell-cycle phases and then identified these proteins using mass spectrometry methods. A total of 41 proteins were identified including zinc finger proteins, ribosomal proteins, and heat shock proteins operating in a Ca(2+)-dependent or independent man... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1944301 Sat, 08 Nov 2008 05:00:00 +0100 1944301 http://www.medworm.com/index.php?rid=1940817&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18987993%26dopt%3DAbstract Authors: Kim M, Ahn IY, Kim H, Cheon J, Park H Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that plays a key role in protein synthesis, folding, denaturation prevention, and signal transduction. We cloned the complete complementary DNA (cDNA) sequence of the Laternula elliptica HSP90. The full-length cDNA was 2,823 bp in size and contained an open reading frame of 2,190 bp that was translated into 729 amino acids with a calculated molecular weight of 83.4 kDa. The deduced amino acid sequence of HSP90 showed the highest homology to Haliotis tuberculata HSP90 (83%). Reverse-transcriptase polymerase chain reaction analysis revealed the presence of HSP90 transcripts in all of the tissues examined. We also studied the transcriptional expression pattern of HSP90 ex... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1940817 Thu, 06 Nov 2008 05:00:00 +0100 1940817 http://www.medworm.com/index.php?rid=1940816&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18987994%26dopt%3DAbstract Authors: Souza AP, Albuquerque C, Torronteguy C, Frasson A, Maito F, Pereira L, Duval da Silva V, Zerwes F, Raynes D, Guerriero V, Bonorino C HspBP1 is a co-chaperone that binds to and regulates the chaperone Hsp70 (Hsp70 is used to refer to HSPA1A and HSPA1B). Hsp70 is known to be elevated in breast tumor tissue, therefore the purpose of these studies was to quantify the expression of HspBP1 in primary breast tumors and in serum of these patients with a follow-up analysis after 6 to 7 years. Levels of HspBP1, Hsp70, and anti-HspBP1 antibodies in sera of breast cancer patients and healthy individuals were measured by enzyme-linked immunosorbent assay. Expression of HspBP1 was quantified from biopsies of tumor and normal breast tissue by Western blot analysis. The data obtained were ana... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1940816 Thu, 06 Nov 2008 05:00:00 +0100 1940816 http://www.medworm.com/index.php?rid=1940815&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18987995%26dopt%3DAbstract Authors: Hernández Torres J, Papandreou N, Chomilier J The co-chaperone Hop [heat shock protein (HSP) organising protein] is known to bind both Hsp70 and Hsp90. Hop comprises three repeats of a tetratricopeptide repeat (TPR) domain, each consisting of three TPR motifs. The first and last TPR domains are followed by a domain containing several dipeptide (DP) repeats called the DP domain. These analyses suggest that the hop genes result from successive recombination events of an ancestral TPR-DP module. From a hydrophobic cluster analysis of homologous Hop protein sequences derived from gene families, we can postulate that shifts in the open reading frames are at the origin of the present sequences. Moreover, these shifts can be related to the presence or absence of biological funct... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1940815 Thu, 06 Nov 2008 05:00:00 +0100 1940815 http://www.medworm.com/index.php?rid=1926870&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18958583%26dopt%3DAbstract Authors: Henderson B, Henderson S Over the last 20 years, it has emerged that many molecular chaperones and protein-folding catalysts are secreted from cells and function, somewhat in the manner of cytokines, as pleiotropic signals for a variety of cells, with much attention being focused on the macrophage. During the last decade, it has become clear that macrophages respond to bacterial, protozoal, parasitic and host signals to generate phenotypically distinct states of activation. These activation states have been termed 'classical' and 'alternative' and represent not a simple bifurcation in response to external signals but a range of cellular phenotypes. From an examination of the literature, the hypothesis is propounded that mammalian molecular chaperones are able to induce a wide ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1926870 Wed, 29 Oct 2008 04:00:00 +0100 1926870 http://www.medworm.com/index.php?rid=1926869&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18958584%26dopt%3DAbstract Authors: Liu X, Ren Z, Zhan R, Wang X, Wang X, Zhang Z, Leng X, Yang Z, Qian L Oxidative stress is one of the main causes of myocardial injury, which is associated with cardiomyocyte death. Mitochondria play a key role in triggering the necrosis and apoptosis pathway of cardiomyocytes under oxidative stress. Although prohibitin (PHB) has been acknowledged as a mitochondrial chaperone, its functions in cardiomyocytes are poorly characterized. The present research was designed to investigate the cardioprotective role of PHB in mitochondria. Oxidative stress can increase the PHB content in mitochondria in a time-dependent manner. Overexpression of PHB in cultured cardiomyocytes by transfection of recombinant adenovirus vector containing PHB sense cDNA resulted in an increase of PHB in mit... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1926869 Wed, 29 Oct 2008 04:00:00 +0100 1926869 http://www.medworm.com/index.php?rid=1866337&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18843550%26dopt%3DAbstract Authors: Kavanagh K, Zhang L, Wagner JD The chaperone protein heat shock protein (HSP) 70 has been shown to protect against obesity-associated insulin resistance. Induction of HSPs is thus considered an exciting therapeutic strategy for diabetes (DM). The aims of this study were to (1) determine HSP levels in plasma, hepatic, and pancreatic tissues of type 2 DM primates and (2) assess the relationship between chaperone proteins of the HSP family and cellular protection. We collected plasma from 24 type 2 DM and 25 normoglycemic control (CTL) cynomolgus macaques. A subset of DM monkeys had liver and pancreas samples available which were compared to a second group of CTL monkeys. We found that DM monkeys had 32% lower HSP70 in circulation which remained significant even after adjustment ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1866337 Thu, 09 Oct 2008 04:00:00 +0100 1866337 http://www.medworm.com/index.php?rid=1860586&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18839337%26dopt%3DAbstract Authors: Fortes MB, Whitham M Extra-cellular (e) heat shock protein (Hsp)72 has been shown to be elevated in a number of clinical conditions and has been proposed as a potential diagnostic marker. From a methodological and diagnostic perspective, it is important to investigate if concentrations of eHsp72 fluctuate throughout the day; hence, the purpose of the study was to measure resting concentrations of plasma eHsp72 throughout a 24-h period. Blood samples were taken every hour from 1200-2100 hours and from 0700-1200 hours the following day from seven healthy recreationally active males. Participants remained in the laboratory throughout the trial, performed light sedentary activities and were provided with standardised meals and fluids. Physical activity was quantified throughout by... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1860586 Tue, 07 Oct 2008 04:00:00 +0100 1860586 http://www.medworm.com/index.php?rid=1833977&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18819021%26dopt%3DAbstract In this study, we show that Hsp72 mutants with a functional substrate-binding domain but lacking chaperone activity retain their ability to protect cells against apoptosis induced by heat and tumor necrosis factor alpha. In contrast, a deletion mutant lacking a functional substrate-binding domain has no protective capacity. The ability of the Hsp72 substrate-binding domain to inhibit apoptosis independent of the regulatory effects of the adenosine triphosphate-binding domain indicates that the inhibition of apoptosis may involve a stable binding interaction with a regulatory substrate rather than Hsp72 chaperone activity. PMID: 18819021 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1833977 Fri, 26 Sep 2008 04:00:00 +0100 1833977 http://www.medworm.com/index.php?rid=1830672&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18815895%26dopt%3DAbstract Authors: Bellizzi D, Taverna D, D'Aquila P, De Blasi S, De Benedictis G To explore possible relationships between mitochondrial DNA (mtDNA) polymorphism and the expression levels of stress-responder nuclear genes we assembled five cybrid cell lines by repopulating 143B.TK(-) cells, depleted of their own mtDNA (Rho(0) cells), with foreign mitochondria with different mtDNA sequences (lines H, J, T, U, X). We evaluated, at both basal and under heat stress conditions, gene expression (mRNA) and intra-mitochondrial protein levels of HSP60 and HSP75, two key components in cellular stress response. At basal conditions, the levels of HSP60 and HSP75 mRNA were lower in one cybrid (H) than in the others (p = 0.005 and p = 0.001, respectively). Under stress conditions, the H line over-expressed b... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1830672 Thu, 25 Sep 2008 04:00:00 +0100 1830672 http://www.medworm.com/index.php?rid=1830671&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18815896%26dopt%3DAbstract Authors: Mongkolsuk S, Schumann W PMID: 18815896 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1830671 Thu, 25 Sep 2008 04:00:00 +0100 1830671 http://www.medworm.com/index.php?rid=1807136&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18800238%26dopt%3DAbstract We examined lymphocyte levels of Hsp27 and Hsp70 in 263 lung cancer cases and age- and gender-matched cancer-free controls by flow cytometry. Multivariate logistic regression models were used to estimate the association between lymphocyte Hsps levels and lung cancer risk. Our results showed that Hsp27 levels were significantly lower in lung cancer cases than in controls (16.5 vs 17.8 mean fluorescence intensity, P < 0.001). This was not observed for Hsp70 levels. Further stratification analysis revealed that lymphocyte Hsp27 levels were negatively associated with lung cancer risk especially in males and heavy smokers. There was a statistical trend of low odd ratios (95% confidence intervals) and upper tertile levels of Hsp27 [1.000, 0.904 (0.566-1.444) and 0.382 (0.221-0.658, P (trend) ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1807136 Thu, 18 Sep 2008 04:00:00 +0100 1807136 http://www.medworm.com/index.php?rid=1807135&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18800239%26dopt%3DAbstract In this study, we isolated a complementary DNA (cDNA) encoding p23 from orchardgrass (Dgp23) and characterized its functional roles under conditions of thermal stress. Dgp23 is a 911 bp cDNA with an open reading frame predicted to encode a 180 amino acid protein. Northern analysis showed that expression of Dgp23 transcripts was heat inducible. Dgp23 has a well-conserved p23 domain and interacted with an orchardgrass Hsp90 homolog in vivo, like mammalian and yeast p23 homologs. Recombinant Dgp23 is a small acidic protein with a molecular mass of approximately 27 kDa and pI 4.3. Dgp23 was also shown to function as a chaperone protein by suppression of malate dehydrogenase thermal aggregation. Differential scanning calorimetry thermograms indicated that Dgp23 is a heat-stable protein, capable... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1807135 Thu, 18 Sep 2008 04:00:00 +0100 1807135 http://www.medworm.com/index.php?rid=1807134&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18800240%26dopt%3DAbstract Authors: Cid C, Regidor I, Poveda PD, Alcazar A In addition to the activity of heat shock protein 90 (Hsp90/HSPC) as a chaperone, some recent studies have reported expression of Hsp90 at the cell surface in certain types of cancer and nervous system cells. We study the expression of Hsp90 at the cell surface in human neuroblastoma (NB69) cells. Immunofluorescence experiments labeling with anti-Hsp90 antibodies on both nonpermeabilized cells and live cells detected Hsp90 at the cell surface. Hsp90 was also identified in a membrane fraction from subcellular fractionation. Cell-surface Hsp90 was significantly more expressed in undifferentiated proliferative spherical neuroblastoma cells than in differentiated flattened cells. In addition, spherical cells were significantly more sensitive ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1807134 Thu, 18 Sep 2008 04:00:00 +0100 1807134 http://www.medworm.com/index.php?rid=1761349&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18766470%26dopt%3DAbstract In this report, we induced SAP in Sprague-Dawley (SD) rats by reverse injection of sodium deoxycholate into the pancreatic duct, and examined the dynamic changes of Cpn60 expression in pancreatic tissues from different time points and at different levels with techniques of real-time PCR, western blotting, and immunohistochemistry. At 1 h after SAP induction, the expression of Cpn60 mRNA in the AP pancreatic tissues was higher than those in the sham-operation group and normal control group, but decreased sharply as the time period was extended, and there was a significant difference between 1 h and 10 h after SAP induction (p < 0.05). In the AP process, Cpn60 protein expression showed transient elevation as well, and the increased protein expression occurred predominantly in affected, bu... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1761349 Wed, 03 Sep 2008 04:00:00 +0100 1761349 http://www.medworm.com/index.php?rid=1756225&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18763057%26dopt%3DAbstract In conclusion, mitochondria are critical organelles of the protective effects of heat-shock treatment. Cellular apoptosis during H(2)O(2)-induced oxidative stress is decreased by heat-shock treatment through a decrease in superoxide induction and preservation of the mitochondrial membrane potential. PMID: 18763057 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1756225 Tue, 02 Sep 2008 04:00:00 +0100 1756225 http://www.medworm.com/index.php?rid=1744389&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18726712%26dopt%3DAbstract Authors: Xiong L, Zhao T, Huang X, Liu ZH, Zhao H, Li MM, Wu LY, Shu HB, Zhu LL, Fan M Hypoxia may regulate the proliferation of diverse stem cells. Our previous study showed that hypoxia promoted the proliferation of embryonic neural stem/progenitor cells (NPCs) and that hypoxia inducible factor-1(HIF-1) was critical in this process. HIF-1 could be stabilized under hypoxic conditions, and heat shock protein 90 (HSP90) is an essential protein that controls the activity and stabilization of HIF-1alpha. In the present work, we investigate whether HSP90 is involved in proliferation of NPCs under hypoxia by regulating HIF-1alpha stabilization. Geldanamycin (GA), an HSP90 inhibitor, decreased the expression of HIF-1alpha in NPCs during hypoxia-driven proliferation and reduced the expression... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1744389 Tue, 26 Aug 2008 04:00:00 +0100 1744389 http://www.medworm.com/index.php?rid=1727333&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18720028%26dopt%3DAbstract Authors: Hooper PL, Hooper PL We propose that type 2 diabetes results from a vicious cycle of metabolically induced inflammation, impaired insulin responsiveness, and subsequent loss of homeostatic signaling. A crucial and previously under-recognized event contributing to this loss of homeostasis is a reduction in heat shock proteins (HSPs, or stress proteins). The central causal pathways of this cycle are the following: (a) obesity-driven inflammation promotes insulin resistance; (b) impaired insulin signaling in turn reduces the expression of HSPs, leaving tissues vulnerable to damage and allowing the accumulation of harmful proteins aggregates; and (c) resulting damage to the pancreatic beta-cell leads to further losses in insulin signaling, while a decline in anti-inflammatory HSPs... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1727333 Fri, 22 Aug 2008 04:00:00 +0100 1727333 http://www.medworm.com/index.php?rid=1710897&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18704762%26dopt%3DAbstract Authors: Emanuelli M, Cecati M, Sartini D, Stortoni P, Corradetti A, Giannubilo SR, Turi A, Tranquilli AL AHSP inhibits cellular production of the reactive oxygen species. Reduced AHSP indicates reduced protection against oxidative stressors. Our objective was to investigate AHSP levels in recurrent miscarriage (RM). Trophoblast was collected from women of 10 weeks gestation: voluntary abortion controls (VA, n = 10); spontaneous first miscarriage with subsequent normal pregnancy (SMSN, n = 15) or with subsequent miscarriage (SMSM, n = 5); RM previously investigated (RMPS, n = 5) or not previously investigated (RM, n = 5). AHSP mRNA and protein were determined using real-time quantitative polymerase chain reaction (PCR) and Western blot, respectively. One-way ANOVA was performed to asse... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1710897 Fri, 15 Aug 2008 04:00:00 +0100 1710897 http://www.medworm.com/index.php?rid=1710896&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18704763%26dopt%3DAbstract Authors: Eitam H, Brosh A, Orlov A, Izhaki I, Shabtay A Selection for higher production rate in cattle inhabiting challenging habitats may be considered disadvantageous because of possible deleterious effects on immunity and reproduction and, consequently, on calf crop percentage. In Israel, free-grazing high productive beef cows experience reduction in nutritional quality of forage during up to 8 months of the year. As milk production by dams dictates calf performance, dam's nutritional needs and rebreeding rates, the aim of the present study was to test how lactating beef cows deal with combined caloric and protein stress both at the productive and self protective levels. For this purpose, we studied the effect of long-term caloric stress on milk characteristics and gene expression o... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1710896 Wed, 13 Aug 2008 04:00:00 +0100 1710896 http://www.medworm.com/index.php?rid=1702771&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18696260%26dopt%3DAbstract Authors: Elekonich MM Foraging honey bees frequently leave the hive to gather pollen and nectar for the colony. This period of their lives is marked by periodic extremes of body temperature, metabolic expenditure, and flight muscle activity. Following ecologically relevant episodes of hyperthermia between 33 degrees C and 50 degrees C, heat shock protein 70 (Hsp70) expression and hsp70/hsc70-4 activity in brains of nonflying laboratory-held bees increased by only two to three times baseline at temperatures 46-50 degrees C. Induction was undetectable in thoracic-flight muscles. Yet, thorax hsp70 mRNA (but not hsc70-4 mRNA) levels were up to ten times higher in flight-capable hive bees and foraging bees compared to 1-day-old, flight-incapable bees, while brain hsp70/hsc70-4 mRNA levels w... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1702771 Tue, 12 Aug 2008 04:00:00 +0100 1702771 http://www.medworm.com/index.php?rid=1690194&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18686014%26dopt%3DAbstract In conclusion, increased serum Hsp70 levels seem to reflect systemic inflammation, oxidative stress and hepatocellular injury in preeclampsia. Nevertheless, further studies are required to determine whether circulating Hsp70 plays a causative role in the pathogenesis of the disease. PMID: 18686014 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1690194 Thu, 07 Aug 2008 04:00:00 +0100 1690194 http://www.medworm.com/index.php?rid=1690193&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18686015%26dopt%3DAbstract In this study, we examined if DSG analogs could inhibit HSP70-induced DC activation. Bone marrow derived immature mouse DCs and peripheral blood mononuclear cell-derived immature human DCs were generated and incubated with Alexa 488-labeled Hsp70 in the presence of methoxyDSG (Gus-1) that had comparable HSP70-binding affinity to DSG or DSG analog GUS-7, which had much more reduced binding affinity for HSP70. The binding of HSP70 to immature DCs was analyzed by laser microscopy and flow cytometry. HSP70-induced DC activation was assessed by TNF-alpha release by enzyme-linked immunosorbent assay. Binding of Hsp70 to the cell surface of immature DCs was inhibited under the presence of Gus-1, but not under the presence of Gus-7. Immature DCs were activated and released TNF-alpha by the stimula... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1690193 Thu, 07 Aug 2008 04:00:00 +0100 1690193 http://www.medworm.com/index.php?rid=1690192&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18686016%26dopt%3DAbstract Authors: Hageman J, Kampinga HH In this manuscript, we describe the generation of a gene library for the expression of HSP110/HSPH, HSP70/HSPA and HSP40/DNAJ members. First, the heat shock protein (HSP) genes were collected from the gene databases and the gene families were analyzed for expression patterns, heat inducibility, subcellular localization, and protein homology using several bioinformatics approaches. These results can be used as a working draft model until data are confirmed by experimental approaches. In addition, we describe the generation of a HSPA/DNAJ overexpression library and tested the effect of different fusion tags on HSPA and DNAJ members using different techniques for measuring chaperone activity. These results show that we have cloned a high-quality heat shock ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1690192 Thu, 07 Aug 2008 04:00:00 +0100 1690192 http://www.medworm.com/index.php?rid=1672504&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18668349%26dopt%3DAbstract In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA comprised 2,552 bp, including a 2,181-bp open reading frame encoding 726 amino acids. Both homology analyses using alignment with previously identified HSP90 and a phylogeny tree indicated that FcHSP90 was a cytoplasmic HSP90. Real-time reverse transcription polymerase chain reaction analysis revealed that FcHSP90 was ubiquitously expressed in all the examined tissues but with highest levels in ovary of F. chinensis. FcHSP90 mRNA levels were sensitively induced by heat shock (from 25 degrees C to 35 degrees C) and reached the maximum at 6 h during heat shock treatment. Under hypoxia conditions, FcHSP90 mRNA levels, in both hemocy... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1672504 Thu, 31 Jul 2008 04:00:00 +0100 1672504 http://www.medworm.com/index.php?rid=1672503&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18668350%26dopt%3DAbstract Authors: de Jong PR, Schadenberg AW, Jansen NJ, Prakken BJ Open heart surgery is a unique model to study the interplay between cellular injury, regulation of inflammatory responses and tissue repair. Stress-inducible heat shock protein 70-kDa (Hsp70) provides a molecular link between these events. In addition to molecular chaperoning, Hsp70 exerts modulatory effects on endothelial cells and leukocytes involved in inflammatory networks. Hsp70 residing in the intracellular compartment is part of an inhibitory feedback loop that acts on nuclear factor kappaB (NF-kappaB). In contrast, extracellular Hsp70 is recognized by multiple germline-encoded immune receptors, e.g., Toll-like receptor (TLR) 2, TLR4, LOX-1, CD91, CD94, CCR5 and CD40. Hsp70 is thereby able to enhance chemotaxis, phagocyt... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1672503 Thu, 31 Jul 2008 04:00:00 +0100 1672503 http://www.medworm.com/index.php?rid=1672502&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18668351%26dopt%3DAbstract Authors: Melling CW, Thorp DB, Milne KJ, Noble EG Both protein kinase C (PKC) activation and Hsp70 expression have been shown to be key components for exercise-mediated myocardial protection during ischemia-reperfusion injury. Given that Hsp70 has been shown to undergo inducible phosphorylation in striated muscle and liver, we hypothesized that PKC may regulate myocardial Hsp70 function and subsequent exercise-conferred cardioprotection through this phosphorylation. Hence, acute exercise of male Sprague-Dawley rats (30 m/min for 60 min at 2% grade) was employed to assess the role of PKC and its selected isoforms in phosphorylation of Hsp70 and protection of the myocardium during ischemia-reperfusion injury. It was observed that administration of the PKC inhibitor chelerythrine chloride... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1672502 Thu, 31 Jul 2008 04:00:00 +0100 1672502 http://www.medworm.com/index.php?rid=1666345&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18663603%26dopt%3DAbstract Authors: Hightower LE, Hageman J, Vos MJ, Kubota H, Tanguay RM, Bruford EA, Cheetham ME, Chen B, Kampinga HH The expanding number of members in the various human heat shock protein (HSP) families and the inconsistencies in their nomenclature have often led to confusion. Here, we propose new guidelines for the nomenclature of the human HSP families, HSPH (HSP110), HSPC (HSP90), HSPA (HSP70), DNAJ (HSP40), and HSPB (small HSP) as well as for the human chaperonin families HSPD/E (HSP60/HSP10) and CCT (TRiC). The nomenclature is based largely on the more consistent nomenclature assigned by the HUGO Gene Nomenclature Committee and used in the National Center of Biotechnology Information Entrez Gene database for the heat shock genes. In addition to this nomenclature, we provide a list of the... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1666345 Tue, 29 Jul 2008 04:00:00 +0100 1666345 http://www.medworm.com/index.php?rid=1666344&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18663604%26dopt%3DAbstract In this study, the potential role of calnexin (Cnx) expression in rCHO cells treated with 5 mM NaBu was investigated for rCHO cells producing tumor necrosis factor receptor FC. To regulate the Cnx expression level, a tetracycline-inducible system was used. Clones with different Cnx expression levels were selected and investigated. With regard to productivity per cell (q (p)), NaBu enhanced the q (p) by over twofold. Under NaBu treatment, Cnx overexpression further enhanced the q (p) by about 1.7-fold. However, under NaBu stress, the cells overexpressing Cnx showed a poorer viability profile with a consistent difference of over 25% in the viability when compared to the Cnx-repressed condition. This drop in the viability was attributed to increased apoptosis seen in these cells as evidenced ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1666344 Tue, 29 Jul 2008 04:00:00 +0100 1666344 http://www.medworm.com/index.php?rid=1638375&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18636345%26dopt%3DAbstract This study determined whether ten distinct Hsp90 co-chaperones were encoded by genes in 19 disparate eukaryotic organisms. Surprisingly, none of the co-chaperones were present in all organisms. The co-chaperone Hop/Sti1 was most widely dispersed (18 out of 19 species), while orthologs of Cdc37, which is critical for the stability and activation of diverse protein kinases in yeast and mammals, were identified in only nine out of 19 species examined. The organism with the smallest proteome, Encephalitozoon cuniculi, contained only three of these co-chaperones, suggesting a correlation between client diversity and the complexity of the Hsp90 co-chaperone machine. Our results suggest co-chaperones are critical for cytosolic Hsp90 function in vivo, but that the composition of Hsp90 complexes va... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1638375 Fri, 18 Jul 2008 04:00:00 +0100 1638375 http://www.medworm.com/index.php?rid=1636003&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18633731%26dopt%3DAbstract In conclusion, diabetic alterations to the contents and activation of the NF-kappaB protein were tissue-specific, but did not appear to alter dimer composition of constitutively bound NF-kappaB. These results indicate that diabetes may alter NF-kappaB activity and expression in a muscle-specific manner. PMID: 18633731 [PubMed - as supplied by publisher] (Source: Cell Stress and Chaperones) Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1636003 Thu, 17 Jul 2008 04:00:00 +0100 1636003 http://www.medworm.com/index.php?rid=1628468&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18626791%26dopt%3DAbstract Authors: Faircloth LM, Churchill PF, Caldwell GA, Caldwell KA Regulation of cell division requires the concerted function of proteins and protein complexes that properly mediate cytoskeletal dynamics. NudC is an evolutionarily conserved protein of undetermined function that associates with microtubules and interacts with several key regulators of mitosis, such as polo-kinase 1 (Plk1) and dynein. NudC is essential for proper mitotic progression, and homologs have been identified in species ranging from fungi to humans. In this paper, we report the characterization of the Caenorhabditis elegans NudC homolog, NUD-1, as a protein exhibiting molecular chaperone activity. All NudC/NUD-1 proteins share a conserved p23/HSP20 domain predicted by three-dimensional modeling [Garcia-Ranea, Mirey, ... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1628468 Tue, 15 Jul 2008 04:00:00 +0100 1628468 http://www.medworm.com/index.php?rid=1628467&cid=s_37762_171_f&fid=37762&url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18626792%26dopt%3DAbstract Authors: Doshi BM, Perdrizet GA, Hightower LE This meeting review highlights areas of mutual interest to investigators in the cellular stress response field and to those carrying out wound-healing research. Inflammation, perhaps the major unifying theme of this meeting, is an essential component of the adult wound response and understanding the control of inflammation is a common interest shared with researchers of the cellular stress response. The particular interest of the authors of this review is in chronic non-healing wounds that frequently occur in patients with major illnesses such as diabetes and diseases of the blood vessels. This orientation has undoubtedly influenced the selection of topics. It is fair to say that the authors were often surprised and certainly impressed with... Cell Stress and Chaperones journals http://www.medworm.com/rss/comments.php?id=1628467 Tue, 15 Jul 2008 04:00:00 +0100 1628467