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        <title>Free Radical Biology and Medicine via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'Free Radical Biology and Medicine' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Free+Radical+Biology+and+Medicine&t=Free+Radical+Biology+and+Medicine&s=Search&f=source]]></link>
        <lastBuildDate>Fri, 19 Mar 2010 17:20:43 +0100</lastBuildDate>
        <item>
            <title>Decreased sensitivity associated with an altered formulation of a commercially available kit for detection of protein carbonyls.</title>
            <link>http://www.medworm.com/index.php?rid=3379667&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20230891%26dopt%3DAbstract</link>
            <description>Authors: Wang P, Powell SR
    Carbonylation is a commonly studied form of oxidative modification to proteins which can be conveniently detected using commercially available kits. The most common of these kits is the Oxyblot(TM) Protein Oxidation Detection Kit (Chemicon/Millipore). Over the past year we have observed severely diminished sensitivity of these kits which was shown to be a result of a change in the formulation of one of the components supplied in the kit. This component, the 10X 2,4-dinitrophenylhydrazine derivatization solution, which had previously been dissolved in 100% trifluoroacetic acid (TFA), was now dissolved in 2N hydrochloric acid, which according to our results is not acid enough. Further, we observed that upon storage even DNPH dissolved in TFA is subject to degra...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379667</comments>
            <pubDate>Fri, 12 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Measurement of oxidatively generated base damage in cellular DNA and urine.</title>
            <link>http://www.medworm.com/index.php?rid=3379669&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20227488%26dopt%3DAbstract</link>
            <description>Authors: Cadet J, Poulsen H
    
    PMID: 20227488 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379669</comments>
            <pubDate>Thu, 11 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Dietary Coenzyme Q10 does not Protect Against Cigarette Smoke-augmented Atherosclerosis in ApoE-deficient Mice.</title>
            <link>http://www.medworm.com/index.php?rid=3379668&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20227489%26dopt%3DAbstract</link>
            <description>Authors: Gairola CG, Howatt DA, Daugherty A
    Dietary coenzyme Q10 reduces spontaneous atherosclerosis in the apoE-deficient mouse model of experimental atherosclerosis. We have shown previously that exposure to sidestream cigarette smoke (SSCS) enhances atherosclerotic lesion formation in apoE-deficient mice. The aim of the present study was to determine if CoQ10 protected against SSCS-mediated atherosclerosis. Female apoE-deficient mice were fed a saturated fat-enriched diet (SFD) alone, or supplemented with 1% wt/wt coenzyme Q10 (SFD-Q10). Mice in each diet group were exposed to SSCS for 4hrs/day, 5days/week in a whole-body exposure chamber maintained at 35+/-4mg smoke particulates/m(3). Mice kept in filtered ambient air served as controls. Mice were euthanized after either 6 or 15wee...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379668</comments>
            <pubDate>Thu, 11 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3379668</guid>        </item>
        <item>
            <title>Suppression of allergen-induced respiratory dysfunction and airway inflammation in sensitized guinea pigs by Mn(II)(Me(2)DO2A), a novel superoxide scavenger compound.</title>
            <link>http://www.medworm.com/index.php?rid=3379665&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20227487%26dopt%3DAbstract</link>
            <description>In conclusion, our findings support the potential therapeutic use of Mn(II)(Me(2)DO2A) as novel superoxide scavenger drug in asthma and anaphylactic reactions.
    PMID: 20227487 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379665</comments>
            <pubDate>Thu, 11 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3379665</guid>        </item>
        <item>
            <title>Coenzyme Q10 in human blood: Native levels and determinants for oxidation during processing and storage.</title>
            <link>http://www.medworm.com/index.php?rid=3379671&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20226852%26dopt%3DAbstract</link>
            <description>Authors: Franke AA, Morrison CM, Bakke JL, Custer LJ, Li X, Cooney RV
    Coenzyme Q10 (Q10) is present in the circulation mainly reduced (ubiquinol-10; UL10), but oxidizes quickly ex vivo to ubiquinone-10 (UN10). Therefore, native UL10/UN10 ratios, used as markers of redox status and disease risk, are difficult to measure. We established a RP-(U)HPLC method with coulometric detection to measure natively circulating UL10 and UN10 concentrations by adding a ubiquinol/ubiquinone mixture as internal standards immediately after plasma preparation. This allowed adjustment for unavoidable artificial UL10 oxidation as well as for total losses (or gains) of analytes during sample storage, processing, and analysis since the internal standards exactly paralleled the chemical behavior of Q10. This te...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379671</comments>
            <pubDate>Wed, 10 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3379671</guid>        </item>
        <item>
            <title>The NAD(P)H:Quinone Oxidoreductase 1 Induces Cell Cycle Progression and Proliferation of Melanoma Cells.</title>
            <link>http://www.medworm.com/index.php?rid=3379670&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20226854%26dopt%3DAbstract</link>
            <description>Authors: Garate M, Wani AA, Li G
    The oxidoreductase NQO1 plays a prominent role in maintaining the cellular homeostasis. NQO1 is mainly a cytosolic enzyme which catalyzes the metabolism of quinones and is present in almost all tissue types providing protection against different stresses including xenobiotics, oxidants, UV light, and ionizing radiation. This enzyme is overexpressed in many cancerous tissues and its function in carcinogenesis remains unclear. Due to the relative lack of information on the role of NQO1 in melanoma pathogenesis, we attempted to determine the expression and basic function of NQO1 in melanoma cell proliferation. We found that NQO1 is overexpressed in most melanoma cell lines with respect to melanocytes. Furthermore, the expression of this oxidoreductase sign...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379670</comments>
            <pubDate>Wed, 10 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3379670</guid>        </item>
        <item>
            <title>Hypochlorite-modification of sphingomyelin generates chlorinated lipid species that induce apoptosis and proteome alterations in dopaminergic PC12 neurons in vitro.</title>
            <link>http://www.medworm.com/index.php?rid=3379666&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20226853%26dopt%3DAbstract</link>
            <description>Authors: Nusshold C, Kollroser M, K&amp;#xF6;feler H, Rechberger G, Reicher H, Ullen A, Bernhart E, Waltl S, Kratzer I, Hermetter A, Hackl H, Trajanoski Z, Hrzenjak A, Malle E, Sattler W
    Recent observations link myeloperoxidase (MPO) activation to neurodegeneration. In multiple sclerosis MPO is present in areas of active demyelination where the potent oxidant hypochlorous acid (HOCl), formed by MPO from H(2)O(2) and chloride ions could oxidatively damage myelin-associated lipids. The purpose of the present study was i) to characterize reaction products of sphingomyelin (SM) formed in response to modification by HOCl, ii) to define the impact of exogenously added SM and HOCl-modified SM (HOCl-SM) on viability parameters of a neuronal cell line (PC12), and iii) to study alterations in the PC...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3379666</comments>
            <pubDate>Wed, 10 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3379666</guid>        </item>
        <item>
            <title>Nitric oxide blocks cellular heme insertion into a broad range of heme proteins.</title>
            <link>http://www.medworm.com/index.php?rid=3354642&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20211245%26dopt%3DAbstract</link>
            <description>Authors: Waheed SM, Ghosh A, Chakravarti R, Biswas A, Haque MM, Panda K, Stuehr DJ
    Although heme insertion into proteins enables their function in bioenergetics, metabolism, and signaling, the mechanisms and regulation of this process is not fully understood. We developed a means to study cellular heme insertion into apo-protein targets over a 3h time period, and then investigated how nitric oxide (NO) released from a chemical donor (NOC-18) might influence heme (protoporphyrin IX) insertion into seven targets that present a range of protein structure, heme ligation, and function (three NO synthases, two cytochrome P450's, catalase, and hemoglobin). NO blocked cellular heme insertion into all seven apo-protein targets. The inhibition occurred at relatively low (nM/min) fluxes of NO, wa...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354642</comments>
            <pubDate>Fri, 05 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354642</guid>        </item>
        <item>
            <title>Oxidized low density lipoprotein increases osteopontin expression by generation of an oxidative stress.</title>
            <link>http://www.medworm.com/index.php?rid=3354641&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20211246%26dopt%3DAbstract</link>
            <description>Authors: Mazi&amp;#xE8;re C, Gomila C, Mazi&amp;#xE8;re JC
    Osteopontin (OPN) is an important mediator of inflammation and is involved in generation of atherosclerotic lesions. Oxidized LDL (OxLDL) increased the intracellular and secreted levels of OPN in rat smooth muscle cells in a dose- and time-dependent manner. Experiments with kinase inhibitors demonstrated that this effect is mediated by ERK and JNK, but not p38. OxLDL induced an oxidative stress, measured by the intracellular levels of reactive oxygen species (ROS) and lipid peroxidation products. The increase in OPN levels is reproduced by the lipid extract of the particle and prevented by the antioxidant vitamin E. Furthermore, ROS generated by UVA irradiation, or treatment with pro-oxidant compounds such as buthionine sulfoximine (BS...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354641</comments>
            <pubDate>Fri, 05 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354641</guid>        </item>
        <item>
            <title>Reactions of superoxide with the myoglobin tyrosyl radical.</title>
            <link>http://www.medworm.com/index.php?rid=3354640&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20211247%26dopt%3DAbstract</link>
            <description>Authors: Das AB, Nagy P, Abbott HF, Winterbourn CC, Kettle AJ
    The contribution of superoxide-mediated injury to oxidative stress is not fully understood. A potential mechanism is the reaction of superoxide with tyrosyl radicals, which either results in repair of the tyrosine or formation of tyrosine hydroperoxide by addition. Whether these reactions occur with protein tyrosyl radicals is of interest because they could alter protein structure or modulate enzyme activity. Here, we have used a xanthine oxidase/acetaldehyde system to generate tyrosyl radicals on sperm whale myoglobin in the presence of superoxide. Using mass spectrometry we found that superoxide prevented myoglobin dimer formation by repairing the protein tyrosyl radical. An addition product of superoxide at Tyr151 was als...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354640</comments>
            <pubDate>Fri, 05 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354640</guid>        </item>
        <item>
            <title>Mechanism of the Peroxidase Activity of Cu, Zn Superoxide Dismutase.</title>
            <link>http://www.medworm.com/index.php?rid=3354639&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20211248%26dopt%3DAbstract</link>
            <description>Authors: Liochev SI, Fridovich I
    In addition to its very efficient catalysis of the dismutation of superoxide ( O(2)(-) ) into O(2) plus H(2)O(2), Cu, Zn SOD acts less efficiently as a non-specific peroxidase. This peroxidase activity is CO(2) dependent although very slow peroxidation of some substrates occurs in the absence of CO(2). The mechanism of that CO(2) dependence is explained by the generation of a strong oxidant at the copper site by two sequential reactions with H(2)O(2), followed by the oxidation of CO(2) to the carbonate radical that then diffuses into the bulk solution. This diffusible carbonate radical is then responsible for the diverse oxidations that have been reported. A different mechanism that involves the reduction of peroxymonocarbonate by the reduced superoxide...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354639</comments>
            <pubDate>Fri, 05 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354639</guid>        </item>
        <item>
            <title>Reactive oxygen species mediate hepatotoxicity induced by the Hsp90 inhibiting anti-cancer geldanamycin and its analogs.</title>
            <link>http://www.medworm.com/index.php?rid=3354638&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20211249%26dopt%3DAbstract</link>
            <description>Authors: Samuni Y, Ishii H, Hyodo F, Samuni U, Krishna MC, Goldstein S, Mitchell JB
    Geldanamycin (GM), a benzoquinone ansamycin antibiotic, is a natural product inhibitor of Hsp90 with potent and broad anti-cancer properties. Because of its adverse effects on liver, its less toxic derivatives 17-(allylamino)-17-demethoxygeldanamycin (17-AAG) and 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG) are currently being evaluated for the treatment of cancer. Previously, it has been demonstrated that the redox cycling of GM by NADPH-cytochrome P450 reductase leads to the formation of the GM semiquinone and superoxide radicals, the latter being identified using spin-trapping. We hypothesized that the different hepatotoxicity induced by GM, 17-AAG and 17-DMAG reflects the redox ac...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354638</comments>
            <pubDate>Fri, 05 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354638</guid>        </item>
        <item>
            <title>Low extracellular zinc increases neuronal oxidant production through nadph oxidase and nitric oxide synthase activation.</title>
            <link>http://www.medworm.com/index.php?rid=3354637&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20211250%26dopt%3DAbstract</link>
            <description>Authors: Aimo L, Cherr GN, Oteiza PI
    A decrease in zinc (Zn) levels increases the production of cell oxidants, affects the oxidant defense system and triggers oxidant sensitive signals in neuronal cells. However, the underlying mechanisms are still unclear. This work tested the hypothesis that the increase in neuronal oxidants that occurs when cellular Zn decreases is mediated by the activation of the NMDA receptor. Differentiated PC12 cells were cultured in control, Zn-deficient or Zn-repleted media. The incubation in Zn deficient media led to a rapid increase in cellular calcium levels, which was prevented by a NMDA receptor antagonist (MK-801). Cellular calcium accumulation was associated with NADPH oxidase and nitric oxide synthase (NOS) activation, an increase in cell oxidant leve...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354637</comments>
            <pubDate>Fri, 05 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354637</guid>        </item>
        <item>
            <title>Glutathione synthesis inhibitor butathione sulfoximine regulates ceruloplasmin by dual but opposite mechanism: Implication in hepatic iron overload.</title>
            <link>http://www.medworm.com/index.php?rid=3354636&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20211720%26dopt%3DAbstract</link>
            <description>Authors: Tapryal N, Mukhopadhyay C, Kumar Mishra M, Das D, Biswas S, Mukhopadhyay CK
    Glutathione (GSH) depletion is often detected in chronic pathological conditions like hepatitis C infection, alcohol consumption or xenobiotic assault with simultaneous reactive oxygen species (ROS) generation and hepatic iron overload. However, relation between GSH depletion and regulators of iron homeostasis is not clear so far. To determine that hepatic HepG2 cells were treated with GSH synthesis inhibitor butathione sulfoximine (BSO) and a dual regulation of ceruloplasmin (Cp) that involves in hepatic iron release was detected unlike other iron homeostasis regulators. BSO treatment that caused marginal GSH deficiency increased Cp synthesis due to increased transcription mediated by activator protei...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354636</comments>
            <pubDate>Thu, 04 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354636</guid>        </item>
        <item>
            <title>Membrane cholesterol contents modify the protective effects of quercetin and rutin on integrity and cellular viability in oxidized erythrocytes.</title>
            <link>http://www.medworm.com/index.php?rid=3347067&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20206255%26dopt%3DAbstract</link>
            <description>Authors: S&amp;#xE1;nchez-Gallego JI, L&amp;#xF3;pez-Revuelta A, Sardina JL, Hern&amp;#xE1;ndez-Hern&amp;#xE1;ndez A, S&amp;#xE1;nchez-Yag&amp;#xFC;e J, Llanillo M
    Flavonoids protect cells damaged by oxidative stress. This, together with other biological activities, is governed by structural features of flavonoids and the nature and physical state of the cell membrane. We have previously proved that membrane cholesterol contents modify the protective power of quercetin and rutin against oxidative stress in erythrocytes. Here we analyzed the lipid asymmetry, the integrity, and cell viability of native and cholesterol-modified erythrocytes exposed to tert-butyl hydroperoxide in presence of both antioxidants. Our results provides clear evidence that quercetin affords better protection than rutin against lipid pe...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347067</comments>
            <pubDate>Tue, 02 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Activation of apoptosis signal-regulating kinase 1 is a key factor in paraquat-induced cell death. Modulation by the Nrf2/Trx axis.</title>
            <link>http://www.medworm.com/index.php?rid=3347068&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20202476%26dopt%3DAbstract</link>
            <description>This study identifies ASK1/JNK and ASK1/p38 and two critical pathways involved in activation of cell death under oxidative stress conditions and identifies the Nrf2/Trx axis as a new target to block these pathways and protect from oxidant exposure such as that found in Parkinson's and other neurodegenerative diseases.
    PMID: 20202476 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347068</comments>
            <pubDate>Mon, 01 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3347068</guid>        </item>
        <item>
            <title>DNA-PKcs deficiency leads to persistence of oxidatively-induced clustered DNA lesions in human tumor cells.</title>
            <link>http://www.medworm.com/index.php?rid=3328007&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20193758%26dopt%3DAbstract</link>
            <description>Authors: Peddi P, Loftin CW, Dickey JS, Hair JM, Burns KJ, Aziz K, Francisco DC, Panayiotidis MI, Sedelnikova OA, Bonner WM, Winters TA, Georgakilas AG
    DNA-dependent protein kinase (DNA-PK) is a key non-homologous end joining (NHEJ) nuclear serine/threonine protein kinase involved in various DNA metabolic and damage signaling pathways contributing to the maintenance of genomic stability and prevention of cancer. In order to examine the role of DNA-PK in processing of non-DSB clustered DNA damage, we have used three different models of DNA-PK deficiency i.e. chemical inactivation of its kinase activity by novel inhibitors IC86621 and NU7026, knock-down and complete absence of the protein in human breast cancer (MCF-7) and glioblastoma cell lines (MO59-J/K). Compromised DNA-PK repair pat...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328007</comments>
            <pubDate>Fri, 26 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328007</guid>        </item>
        <item>
            <title>Application of the Amplex Red/Horseradish Peroxidase Assay to Measure Hydrogen Peroxide Generation by Recombinant Microsomal Enzymes.</title>
            <link>http://www.medworm.com/index.php?rid=3328012&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20188819%26dopt%3DAbstract</link>
            <description>Authors: Mishin V, Gray JP, Heck DE, Laskin DL, Laskin JD
    The formation of reactive oxygen species by the cytochrome P450 monoxygenase system is thought to be due to autooxidation of NADPH-cytochrome P450 reductase and the non-productive decay of oxygen-bound cytochrome P450 intermediates. To characterize this process in recombinant microsomal enzymes, we used a highly sensitive hydrogen peroxide assay based on Amplex-Red oxidation. This assay is 20 times more sensitive (LLD = 5.0 pmoles/assay, and LLQ = 30 pmoles/assay) than the standard ferrous thiocyanate assay for detection of hydrogen peroxide. We found low, but detectable spontaneous generation of hydrogen peroxide by recombinant human NADPH-cytochrome P450 reductase complexes (0.34 nmoles hydrogen peroxide/min/100 Units of NADPH...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328012</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328012</guid>        </item>
        <item>
            <title>Enhanced expression of mitochondrial superoxide dismutase leads to prolonged in vivo cell cycle progression and up-regulation of mitochondrial thioredoxin.</title>
            <link>http://www.medworm.com/index.php?rid=3328011&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20188820%26dopt%3DAbstract</link>
            <description>Authors: Kim A, Joseph S, Khan A, Epstein CJ, Sobel R, Huang TT
    Mn superoxide dismutase (MnSOD) is an important mitochondrial antioxidant enzyme, and elevated MnSOD levels have been shown to reduce tumor growth in part by suppressing cell proliferation. Studies with fibroblasts have shown that increased MnSOD expression prolongs cell cycle transition time in G1/S and favors entrance into the quiescent state. To determine if the same effect occurs during tissue regeneration in vivo, we used a transgenic mouse system with liver-specific MnSOD expression and a partial hepatectomy paradigm to induce synchronized in vivo cell proliferation during liver regeneration. We show in this experimental system that a 2.6 fold increase in MnSOD activities leads to delayed entry into S phase, as measu...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328011</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328011</guid>        </item>
        <item>
            <title>Cigarette smoke particle phase extract induces HO-1 expression in human tracheal smooth muscle cells: Role of c-Src/NADPH oxidase/MAPKs/Nrf2 signaling pathway.</title>
            <link>http://www.medworm.com/index.php?rid=3328010&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20188821%26dopt%3DAbstract</link>
            <description>In this study, we report that cigarette smoke particle phase extract (CSPE) is an inducer of HO-1 expression mediated through various signaling pathways in human tracheal smooth muscle cells (HTSMCs). CSPE-induced HO-1 protein, mRNA expression, and promoter activity were attenuated by pretreatment with the ROS scavenger (N-acetyl-L-cysteine) and the inhibitors of c-Src (PP1), NADPH oxidase [diphenylene iodonium chloride (DPI) and apocynin (APO)], MEK1/2 (U0126), p38 MAPK (SB202190), and JNK1/2 (SP600125) or transfection with siRNA of Src, p47(phox), NOX2, p42, p38, JNK2, or NF-E2-related factor 2 (Nrf2). CSPE-stimulated translocation of p47(phox) and Nrf2, ROS production, and NADPH oxidase activity were attenuated by transfection with siRNAs of Src, p47(phox), and NOX2 or pretreatment with...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328010</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328010</guid>        </item>
        <item>
            <title>Arsenite down-regulates the cytochrome P450 1A1 at transcriptional and post-translational levels in human HepG2 cells.</title>
            <link>http://www.medworm.com/index.php?rid=3328009&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20188822%26dopt%3DAbstract</link>
            <description>This study demonstrates that As(III) down-regulates CYP1A1 through transcriptional and post-translational mechanisms. In addition, HO-1 is involved in the As(III)-mediated down-regulation of CYP1A1 at the catalytic activity level.
    PMID: 20188822 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328009</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328009</guid>        </item>
        <item>
            <title>Contribution of type 1 diabetes to rat liver dysfunction and cellular damage via activation of NOS, PARP, IkappaBalpha/NF-kappaB, MAPKs and mitochondria dependent pathways: Prophylactic role of arjunolic acid.</title>
            <link>http://www.medworm.com/index.php?rid=3328008&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20188823%26dopt%3DAbstract</link>
            <description>Authors: Manna P, Das J, Ghosh J, Sil PC
    Diabetic mellitus, a chronic metabolic disorder, is one of the most important health problems in the world; especially in developing countries. Our earlier investigations reported the beneficial action of arjunolic acid (AA) against streptozotocin (STZ) mediated type 1 hyperglycemia. We have demonstrated that AA possesses protective roles against drugs and chemicals (environmental toxins) induced hepatotoxicity. Liver is the main organ of detoxifying processes. The purpose of the present study was to explore whether AA plays any protective role against hyperglycaemic hepatic dysfunctions; and if so, what molecular pathways it utilizes for the mechanism of its protective action. In the experimental rats, type 1 hyperglycaemia was induced by strep...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328008</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328008</guid>        </item>
        <item>
            <title>Increased Protein Hydrophobicity in Response to Aging and Alzheimer's disease.</title>
            <link>http://www.medworm.com/index.php?rid=3328015&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20188163%26dopt%3DAbstract</link>
            <description>Authors: Dasuri K, Ebenezer P, Zhang L, Fernandez-Kim SO, Bruce-Keller AJ, Markesbery WR, Keller JN
    Increased levels of misfolded and damaged proteins occur in response to brain aging and Alzheimer's disease (AD), which presumably increases the amount of aggregation prone proteins via elevations in hydrophobicity. The proteasome is an intracellular protease which degrades oxidized and ubiquitinated proteins, with the function of the proteasome known to be impaired in response to both aging and AD. In the present study we sought to determine the potential for increased levels of protein hydrophobicity occurring in response to aging and AD, identify the contribution of proteasome inhibition to increased protein hydrophobicity, and lastly to identify the contribution of ubiquitinated and ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328015</comments>
            <pubDate>Tue, 23 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328015</guid>        </item>
        <item>
            <title>HIV proteins (gp120 and Tat) and methamphetamine in oxidative stress-induced damage in the brain: Potential role of the thiol antioxidant N-acetylcysteine amide.</title>
            <link>http://www.medworm.com/index.php?rid=3328014&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20188164%26dopt%3DAbstract</link>
            <description>The objective of this study was to determine if N-acetylcysteine amide (NACA) protects the blood brain barrier (BBB) from oxidative stress-induced damage in animals exposed to gp120, Tat and METH. To study this, CD-1 mice pre-treated with NACA/saline, received injections of gp120, Tat, gp120 + Tat or saline for 5 days, followed by three injections of METH/saline on the fifth day, and sacrificed 24 h after the final injection. Various oxidative stress parameters were measured, and animals treated with gp120+Tat+Meth were found to be the most challenged group, as indicated by their GSH and MDA levels. Treatment with NACA significantly rescued the animals from oxidative stress. Further, NACA-treated animals had significantly higher expression of TJ proteins and BBB permeability as compared to...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328014</comments>
            <pubDate>Tue, 23 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328014</guid>        </item>
        <item>
            <title>Reactive oxygen species produced by the knockdown of manganese-superoxide dismutase up-regulate hypoxia-inducible factor-1alpha expression in oral squamous cell carcinoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=3328013&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20188165%26dopt%3DAbstract</link>
            <description>In this study, we investigated the influence of ROS on HIF-1alpha signaling in OSCC cells by the transfection of manganese-superoxide dismutase (Mn-SOD)-specific small interfering RNA (siRNA). The levels of HIF-1alpha protein and mRNA were increased by siRNA under both normoxic and hypoxic conditions in parallel with the increase of intracellular ROS levels. The accumulation of HIF-1alpha protein was enhanced through inhibition of the recruitment of von Hippel-Lindau protein and HIF-1alpha ubiquitination without a change in prolyl hydroxylase mRNA and protein levels. Furthermore, the transactivation of HIF-1alpha was enhanced via cap-dependent and an internal ribosome entry site-mediated mechanisms. These results suggest that intracellular ROS produced by the knockdown of Mn-SOD enhance HI...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328013</comments>
            <pubDate>Tue, 23 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328013</guid>        </item>
        <item>
            <title>Quercetin is a substrate for the transmembrane oxidoreductase, Dcytb.</title>
            <link>http://www.medworm.com/index.php?rid=3315398&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20184953%26dopt%3DAbstract</link>
            <description>Authors: Vlachodimitropoulou E, Naftalin RJ, Sharp PA
    Duodenal cytochrome b (Dcytb) is a transmembrane oxidoreductase protein found in apical membranes of duodenal enterocytes, as well as human erythrocytes, with the capacity to transport electrons donated by cytosolic ascorbate to extracellular electron receptors such as Fe(III), dehydroascorbate, or molecular O(2). We have investigated the capacity of the flavonoid quercetin to act as an electron donor for Dcytb in a similar manner to ascorbate by observing reduction of extracellular Fe(III) to Fe(II) in either Madin Darby Canine Kidney (MDCK) cells overexpressing Dcytb (Dcytb+), or in Dcytb null MDCK cells. In Dcytb+cells there is a saturable increase in extracellular Fe(lll) reduction in response to increasing intracellular quercet...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3315398</comments>
            <pubDate>Mon, 22 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3315398</guid>        </item>
        <item>
            <title>Oxidative Stress, Mitochondrial Bioenergetics and Cardiolipin in Aging.</title>
            <link>http://www.medworm.com/index.php?rid=3311001&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20176101%26dopt%3DAbstract</link>
            <description>Authors: Paradies G, Petrosillo G, Paradies V, Ruggiero FM
    Aging is a natural, complex and multifactorial biological process associated with impairment of bioenergetic function, increased oxidative stress, attenuated ability to respond to stresses and increased risk of contracting age-associated diseases. Oxidative stress is widely thought to underpin many aging processes. Mitochondria, the powerhouse of the cell, are considered to be the most important cellular organelles to contribute to the aging process, mainly through respiratory chain dysfunction and formation of reactive oxygen species, leading to damage to mitochondrial proteins, lipids and mitochondrial DNA. Cardiolipin, a phospholipid located at the level of the inner mitochondrial membrane, is known to be intimately involved...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3311001</comments>
            <pubDate>Fri, 19 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3311001</guid>        </item>
        <item>
            <title>Depletion Of Oxidative And Endoplasmic Reticulum Stress Regulators In Pick's Disease.</title>
            <link>http://www.medworm.com/index.php?rid=3311000&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20176102%26dopt%3DAbstract</link>
            <description>In this study, we assessed the implication of ER stress associated with oxidative stress in PiD as a potential mechanism involved in its pathogenesis. Samples from morphologically affected frontal cortex and apparently pathologically preserved occipital cortex showed region-dependent increases in different protein oxidative damage pathways. The oxidative modifications targeted antioxidant enzymes, proteases, heat shock proteins and synaptic proteins. These effects were associated with compromised proteasomal function and ER stress in frontal cortex samples. In adidtion, we observed depletion in ER chaperones (glucose-regulated proteins Grp78/BiP and glucose-regulated protein 94) and differences in tissue content and distribution of nuclear factor-erythroid 2 p45-related respiratory 2 (Nrf2...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3311000</comments>
            <pubDate>Fri, 19 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3311000</guid>        </item>
        <item>
            <title>Degree of roasting is the main determinant of the effects of coffee on NF-kappaB and EpRE.</title>
            <link>http://www.medworm.com/index.php?rid=3310999&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20176103%26dopt%3DAbstract</link>
            <description>Authors: Paur I, Balstad TR, Blomhoff R
    Coffee, one of the most popular beverages worldwide, is a major contributor of phytochemicals in the diet and contributes more than 50% of dietary antioxidants in many countries. A moderate intake of coffee has been linked to reduced risk of chronic diseases. Furthermore, experimental studies demonstrate bioactivity of coffee or coffee compounds in inflammation and oxidative stress, two major, related biological processes. We show that degree of roasting correlates with the efficiency to dampen inflammation induced NF-kappaB activity and induce antioxidant defense through Nrf2/EpRE activity. Extracts of dark roasted coffee inhibit NF-kappaB activity by more than 80 % and induce EpRE activity more than 25 fold in vitro. In transgenic NF-kappaB-luc...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3310999</comments>
            <pubDate>Fri, 19 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3310999</guid>        </item>
        <item>
            <title>Iron mediated oxidative stress plays an essential role in ferritin induced cell death.</title>
            <link>http://www.medworm.com/index.php?rid=3311003&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20172024%26dopt%3DAbstract</link>
            <description>In conclusion, based on their iron storing ability, secreted acidic isoferritins may act as soluble mediators of oxidative stress under certain physiological and pathophysiological conditions.
    PMID: 20172024 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3311003</comments>
            <pubDate>Thu, 18 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3311003</guid>        </item>
        <item>
            <title>Action of 6-amino-3-pyridinols as novel antioxidants against free radicals and oxidative stress in solution, plasma, and cultured cells.</title>
            <link>http://www.medworm.com/index.php?rid=3311002&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20172025%26dopt%3DAbstract</link>
            <description>In this study, the capacity of novel 6-amino-2,4,5-trimethyl-3-pyridinols for scavenging peroxyl radicals, inhibiting plasma lipid peroxidation in vitro, and preventing cytotoxicity induced by glutamate, 6-hydroxydopamine, 1-methyl-4-phenylpyridium (MPP(+) ), and hydroperoxyoctadecadienoic acid was assessed. It was found that they exerted higher reactivity toward peroxyl radicals and more potent activity for inhibiting the above oxidative stress than alpha-tocopherol, the most potent natural antioxidant, except against the cytotoxicity induced by MPP(+). These results suggest that the novel 6-amino-3-pyridinols may be potent antioxidant against oxidative stress.
    PMID: 20172025 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3311002</comments>
            <pubDate>Thu, 18 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3311002</guid>        </item>
        <item>
            <title>Interpretation of urinary 8-oxo-7,8-dihydro-2'-deoxyguanosine is adversely affected by methodological inaccuracies when using a commercial ELISA.</title>
            <link>http://www.medworm.com/index.php?rid=3311007&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20171272%26dopt%3DAbstract</link>
            <description>Authors: Garratt LW, Mistry V, Singh R, Sandhu J, Sheil B, Cooke MS, Sly PD, 
    The DNA lesion 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxodG), a urinary marker of oxidative stress, is produced from reactions of reactive oxygen species with host DNA 2'-deoxyribonucleotides. The current gold standard assessment is by complex chromatographic methods using HPLC or LC-MS/MS. Several studies have reported that commercial 8-oxodG ELISA kits correlate sufficiently with chromatographic techniques to be an easier alternative for laboratories without access to gold-standard techniques. However, the assumption that significant correlation translates into a similar ability to differentiate disease categories or treatment groups is yet to be determined. Using LC-MS/MS and two variants of a commercial E...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3311007</comments>
            <pubDate>Wed, 17 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3311007</guid>        </item>
        <item>
            <title>Nox1 is involved with p53 deacetylation and suppression of its transcriptional activity and apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=3311006&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20171273%26dopt%3DAbstract</link>
            <description>Authors: Puca R, Nardinocchi L, Starace G, Rechavi G, Sacchi A, Givol D, D'Orazi G
    HIPK2 is a stress-induced kinase and a transcriptional co-repressor that functionally cooperates with p53 to suppress cancer. Activation of the p53 pro-apoptotic function requires a cascade of phosphorylations and acetylations and HIPK2 takes part is both modifications in that it phosphorylates p53Ser46 and induces p53Lys382 acetylation. Here, to further investigate the role of HIPK2 in p53 activation, we started by the finding that HIPK2 inhibition up-regulated Nox1, a homologue of the catalytic subunit of the superoxide-generating NADPH-oxidase, involved in tumor progression and ROS production. We found that Nox1 inhibited p53Lys382 acetylation, which is a target of SirT1 deacetylase, and impaired p53 ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3311006</comments>
            <pubDate>Wed, 17 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3311006</guid>        </item>
        <item>
            <title>Modulation of thiol homeostasis induced by H(2)S-releasing aspirin.</title>
            <link>http://www.medworm.com/index.php?rid=3311005&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20171274%26dopt%3DAbstract</link>
            <description>Authors: Giustarini D, Del Soldato P, Sparatore A, Rossi R
    The H(2)S-releasing aspirin (ACS14) containing a dithiolethione moiety has been demonstrated to maintain the thromboxane-suppressing activity of the parent compound, but it seems to spare the gastric mucosa by affecting redox imbalance through increased H(2)S/glutathione (GSH) formation. Nevertheless, the mechanisms by which ACS14 is able to elevate the levels of these agents has not been fully elucidated so far. In this manuscript the effect of an acute ip administration of ACS14 and of its dithiolethione moiety (5-(4-hydroxyphenyl)-3H-1,2-dithiole-3-thione, ADTOH) on the overall thiol content of rat tissues and on the main enzymes involved in the maintenance of thiol homeostasis is reported. ACS14 and ADTOH treatments were sh...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3311005</comments>
            <pubDate>Wed, 17 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3311005</guid>        </item>
        <item>
            <title>Increased levels of 4-hydroxynonenal and acrolein in the brain in preclinical Alzheimer's disease (PCAD).</title>
            <link>http://www.medworm.com/index.php?rid=3311004&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20171275%26dopt%3DAbstract</link>
            <description>Authors: Bradley MA, Markesbery WR, Lovell MA
    Previous studies demonstrate increased levels of 4-hydroxynonenal (HNE) and acrolein in vulnerable brain regions of subjects with mild cognitive impairment (MCI) and late-stage Alzheimer's disease (AD). Recently preclinical AD (PCAD) subjects, who demonstrate normal antemortem neuropsychological test scores but abundant AD pathology at autopsy, have become the focus of increased study. Levels of extractable HNE and acrolein were quantified by gas chromatography mass spectrometry with negative chemical ionization and protein-bound HNE and acrolein was quantified by dot-blot immunohistochemistry in the hippocampus/parahippocampal gyrus (HPG), superior and middle temporal gyri (SMTG), and cerebellum (CER) of 10 PCAD and 10 age-matched normal c...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3311004</comments>
            <pubDate>Wed, 17 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3311004</guid>        </item>
        <item>
            <title>Oxidative stress resistance in hippocampal cells is associated with altered membrane fluidity and enhanced non-amyloidogenic cleavage of endogenous amyloid precursor protein.</title>
            <link>http://www.medworm.com/index.php?rid=3284567&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20156550%26dopt%3DAbstract</link>
            <description>Authors: Clement AB, Gimpl G, Behl C
    Reactive oxygen species (ROS) have important roles as signaling molecules in the regulation of a variety of biological processes. On the other hand, chronic oxidative stress exerted by ROS is widely considered as a causative factor for aging. Therefore, cells need to be able to adapt to a chronic oxidative challenge, and do so to a certain cell-type specific extent. Recently, we have shown in oxidative stress-resistant cell lines, HT22(H2O2) and HT22(Glu), derived from the neuronal cell line HT22 by chronic exposure to sublethal concentrations of H(2)O(2) and glutamate, that, in addition to the known antioxidant defence mechanisms, e.g. activation of antioxidant enzymes or up-regulation of heat shock proteins, oxidative stress resistance depends on ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284567</comments>
            <pubDate>Fri, 12 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284567</guid>        </item>
        <item>
            <title>Oxidative stress in skeletal muscle causes severe disturbance of exercise activity without muscle atrophy.</title>
            <link>http://www.medworm.com/index.php?rid=3284566&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20156551%26dopt%3DAbstract</link>
            <description>Authors: Kuwahara H, Horie T, Ishikawa S, Tsuda C, Kawakami S, Noda Y, Kaneko T, Tahara S, Tachibana T, Okabe M, Melki J, Takano R, Toda T, Morikawa D, Nojiri H, Kurosawa H, Shirasawa T, Shimizu T
    The increase in reactive oxygen species (ROS) levels that occurs during intense exercise has been proposed to be one of the major causes of muscle fatigue. In addition, the accumulation of cellular damage due to ROS is widely regarded to be one of the factors triggering age-related pathological conditions in skeletal muscle. In order to investigate the pathological significance of oxidative stress in skeletal muscle, we generated skeletal muscle-specific manganese superoxide dismutase (Mn-SOD)-deficient (muscle-Sod2(-/-)) mice. The mutant mice showed severe disturbances in exercise activity, ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284566</comments>
            <pubDate>Fri, 12 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284566</guid>        </item>
        <item>
            <title>Safe and targeted anticancer efficacy of a novel class of antioxidant-conjugated difluoro-diarylidenylpiperidones: Differential cytotoxicity in healthy and cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=3284565&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20156552%26dopt%3DAbstract</link>
            <description>We report a novel class of bifunctional compounds based on diarylidenylpiperidone (DAP) conjugated with an N-hydroxypyrroline (NOH, a nitroxide precursor) group. We hypothesized that the DAP would have cytotoxic (anti-cancer) activity, while the NOH moiety would function as a tissue-specific modulator (anti-oxidant) of cytotoxicity. The study used four DAPs, namely H-4073 and H-4318 without NOH and HO-3867 and HO-4200 with NOH substitution. The goal of the study was to evaluate the 'proof-of-concept' anticancer-versus-antioxidant efficacy of the DAPs using a number of cancerous (breast, colon, head and neck, liver, lung, ovarian, and prostate cancer) and noncancerous (smooth muscle, aortic endothelial, and ovarian surface epithelial cells) human cell lines. Cytotoxicity was determined usin...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284565</comments>
            <pubDate>Fri, 12 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284565</guid>        </item>
        <item>
            <title>Changes and Expression of Mitochondrial Peroxiredoxin and Thioredoxin in Neurons and Glia and Their Protection in Experimental Cerebral Ischemic Damage.</title>
            <link>http://www.medworm.com/index.php?rid=3284564&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20156553%26dopt%3DAbstract</link>
            <description>Authors: Hwang IK, Yoo KY, Kim DW, Lee CH, Choi JH, Kwon YG, Kim YM, Choi SY, Won MH
    We observed chronological changes of mitochondrial specific antioxidant enzymes, peroxiredoxin 3 (Prx3) and thioredoxin 2 (Trx2) and their neuroprotective effects in the hippocampal CA1 region after 5 min of transient cerebral ischemia in gerbils. In sham-operated group, weak Prx3 and Trx2 immunoreactivity was detected in the stratum pyramidale. Prx3 immunoreactivity was increased in pyramidal neurons and expressed in microglia 1 day and 3 days, respectively, after ischemia/reperfusion (I/R). Trx2 immunoreactivity in pyramidal neurons increased 30 min and 1 day after I/R, and decreased 6 h after I/R. Trx2 immunoreaction was expressed in astrocytes at 3 days post-ischemia. The intraventricular administr...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284564</comments>
            <pubDate>Fri, 12 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284564</guid>        </item>
        <item>
            <title>Modulation of arachidonic and linoleic acid metabolites in myeloperoxidase deficient mice during acute inflammation.</title>
            <link>http://www.medworm.com/index.php?rid=3284563&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20156554%26dopt%3DAbstract</link>
            <description>Authors: Kubala L, Schmelzer KR, Klinke A, Kolarova H, Baldus S, Hammock BD, Eiserich JP
    Acute inflammation is a common feature of many life-threatening pathologies, including septic shock. One hallmark of acute inflammation is the peroxidation of polyunsaturated fatty acids forming bioactive products, which regulate inflammation. Myeloperoxidase (MPO) is an abundant phagocyte-derived hemoprotein released during phagocyte activation. Here, we investigated the role of MPO in modulating biologically active arachidonic acid (AA) and linoleic acid (LA) metabolites during acute inflammation. Wild-type and MPO-knockout (KO) mice were exposed to intraperitoneally injected endotoxin for 24 h, and plasma LA and AA oxidation products were comprehensively analyzed using a liquid chromatography-ma...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284563</comments>
            <pubDate>Fri, 12 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284563</guid>        </item>
        <item>
            <title>Chronic exposure to cadmium and arsenic strongly influences concentrations of 8-oxo-7,8-dihydro-2'-deoxyguanosine in urine.</title>
            <link>http://www.medworm.com/index.php?rid=3276598&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153423%26dopt%3DAbstract</link>
            <description>Authors: Engstr&amp;#xF6;m KS, Vahter M, Johansson G, Lindh CH, Teichert F, Singh R, Kippler M, Nermell B, Raqib R, Str&amp;#xF6;mberg U, Broberg K
    Exposure to arsenic (As), cadmium (Cd) and lead (Pb) may generate oxidative stress, which can be assessed by 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxodG) in urine, a sensitive marker of oxidatively damaged DNA. We have evaluated oxidative stress induced by mixed chronic exposure to As, Cd, Pb, as well as the influence of As metabolism and nutritional status, i.e. ferritin (Ft), selenium (Se), zinc (Zn), manganese (Mn) and body weight. 8-oxodG was measured in urine from 212 women in early pregnancy from Matlab, rural Bangladesh, using LC-MS/MS. Cd and Pb were analyzed in urine and erythrocytes, while Se, Mn and Zn were analyzed in erythrocytes, all...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276598</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276598</guid>        </item>
        <item>
            <title>Aging and oxidatively damaged nuclear DNA in animal organs.</title>
            <link>http://www.medworm.com/index.php?rid=3268001&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20149865%26dopt%3DAbstract</link>
            <description>Authors: M&amp;#xF8;ller P, L&amp;#xF8;hr M, Folkmann JK, Mikkelsen L, Loft S
    Oxidative stress is considered to contribute to aging and is associated with generation of oxidatively damaged DNA, including 8-oxo-7,8-dihydroguanine. We have identified 69 studies that have measured the level of oxidatively damaged DNA in organs of animals at different ages. In general, organs with limited cell proliferation, i.e. liver, kidney, brain, heart, pancreas and muscle tended to show accumulation of DNA damage with age, whereas organs with highly proliferating cells, such as intestine, spleen and testis showed more equivocal or no effect of age. A restricted analysis of studies reporting baseline levels of damaged DNA that was less than 5 lesions/10(6) dG showed that 21 out of 29 studies reported age-asso...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3268001</comments>
            <pubDate>Mon, 08 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3268001</guid>        </item>
        <item>
            <title>Suppression of mutagenesis by 8-hydroxy-2'-deoxyguanosine 5'-triphosphate (7,8-dihydro-8-oxo-2'-deoxyguanosine 5'-triphosphate) by human MTH1, MTH2, and NUDT5.</title>
            <link>http://www.medworm.com/index.php?rid=3262853&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144704%26dopt%3DAbstract</link>
            <description>Authors: Hori M, Satou K, Harashima H, Kamiya H
    To assess the functions of the three human MutT-type enzymes, MTH1, MTH2, and NUDT5, mutation induction by an oxidized form of dGTP, 8-hydroxy-2'-deoxyguanosine 5'-triphosphate (8-OH-dGTP, 7,8-dihydro-8-oxo-2'-deoxyguanosine 5'-triphosphate), was examined using human 293T cells treated with their specific siRNAs. Shuttle plasmid DNA containing the supF gene was first transfected into the cells, and then 8-OH-dGTP was introduced by means of osmotic pressure. Escherichia coli cells were transformed with the DNAs replicated in the treated cells. The knock-downs of the MTH1, MTH2, and NUDT5 proteins increased the A:T&amp;#xE0;C:G substitution mutations induced by 8-OH-dGTP. In addition, the increase in the induced mutation frequency was more evid...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262853</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262853</guid>        </item>
        <item>
            <title>Thiol-sensitive mutant forms of human SOD2, L60F and I58T: The role of Cys140.</title>
            <link>http://www.medworm.com/index.php?rid=3262850&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144705%26dopt%3DAbstract</link>
            <description>Authors: Hernandez-Saavedra D, Quijano C, Demicheli V, Souza JM, Radi R, McCord JM
    We recently described a coding mutation (L60F) in the mitochondrial superoxide dismutase (SOD2) gene of the human T-cell leukemia-derived cell line, Jurkat. In cell extracts the L60F mutant enzyme showed unusual inhibition by thiol reagents not seen in wild type enzyme. Here we compare the properties of purified recombinant L60F SOD2 with a previously described SOD2 mutant, I58T. Both mutant proteins display a weakened dimer-dimer interaction and thermal instability at 55 degrees C. Both I58T and L60F lose activity at 37 degrees C in the presence of 5 mM N-ethylmaleimide, whereas the wild type SOD2 does not. Each subunit contains one exposed, reactive cysteine residue at position 196, and a second cystei...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262850</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262850</guid>        </item>
        <item>
            <title>Zinc induces depletion and aggregation of endogenous TDP-43.</title>
            <link>http://www.medworm.com/index.php?rid=3254947&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138212%26dopt%3DAbstract</link>
            <description>Authors: Caragounis A, Price KA, Soon CP, Filiz G, Masters CL, Li QX, Crouch PJ, White AR
    Ubiquitinated neuronal aggregates containing TDP-43 are pathological hallmarks in the spectrum of frontotemporal lobar dementia and amyotrophic lateral sclerosis. In affected neurons, the TDP-43 undergoes C-terminal fragmentation, phosphorylation and ubiquitination and forms aggregates in the cytoplasm or nucleus. While in vitro studies have been able to re-capitulate these features using transfected cell culture models, little is known about the biochemical mechanisms that underlie pathological changes to endogenous TDP-43. As altered metal ion homeostasis and increased oxidative stress are central features of neurodegeneration, including FTLD and ALS, we sought to determine the affects of these ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3254947</comments>
            <pubDate>Wed, 03 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3254947</guid>        </item>
        <item>
            <title>Treatment with the catalytic metalloporphyrin AEOL 10150 reduces inflammation and oxidative stress due to inhalation of sulfur mustard analog 2-chloroethyl ethyl sulfide (CEES).</title>
            <link>http://www.medworm.com/index.php?rid=3254950&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138141%26dopt%3DAbstract</link>
            <description>Authors: O'Neill HC, White CW, Veress LA, Hendry-Hofer TB, Loader JE, Min E, Huang J, Rancourt RC, Day BJ
    Sulfur mustard (bis-2-(chloroethyl) sulfide, SM) is a highly reactive vesicating and alkylating chemical warfare agent. A SM analog, 2-chloroethyl ethyl sulfide (CEES) has been utilized to elucidate mechanisms of toxicity and as a screen for therapeutics. Previous studies with SM and CEES have demonstrated a role for oxidative stress as well as decreased injury with antioxidant treatment. We tested whether post-treatment with the metalloporphyrin catalytic antioxidant AEOL 10150 would improve outcome in CEES-induced lung injury. Anesthetized rats inhaled 5% CEES for 15 minutes via a nose-only inhalation system. At one and nine hours following CEES exposure, rats were given AEOL 101...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3254950</comments>
            <pubDate>Tue, 02 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3254950</guid>        </item>
        <item>
            <title>Frog skins keep redox homeostasis by antioxidant peptides with rapid radical-scavenging ability.</title>
            <link>http://www.medworm.com/index.php?rid=3254949&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138142%26dopt%3DAbstract</link>
            <description>Authors: Liu C, Hong J, Yang H, Wu J, Ma D, Li D, Lin D, Lai R
    The question of how amphibians can protect themselves from reactive oxygen species (ROS) when exposed to the sun in an oxygen rich atmosphere is important and interesting not only from an evolutionary viewpoint but also as a primer for researchers interested in mammalian skin biology, where such peptide systems for antioxidant defense are not well studied. The identification of an antioxidant peptide named antioxidin-RL from the frog (Odorrana livida) skin in this report underpins that peptide antioxidant system may be a widespread antioxidant strategy among amphibian skins. Its ability of eliminating most of the 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) radical (ABTS(+)) tested within 2 s, which is much faste...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3254949</comments>
            <pubDate>Tue, 02 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3254949</guid>        </item>
        <item>
            <title>Cytoprotective Induction of Nitric Oxide Synthase in a Cellular Model of 5-Aminolevulinic Acid-Based Photodynamic Therapy.</title>
            <link>http://www.medworm.com/index.php?rid=3254948&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138143%26dopt%3DAbstract</link>
            <description>Authors: Bhowmick R, Girotti AW
    Photodynamic therapy (PDT) employs a photosensitizing agent, molecular oxygen, and visible light to generate reactive species that kill tumor and tumor vasculature cells. Nitric oxide produced by these cells could be pro-carcinogenic by inhibiting apoptosis or promoting angiogenesis and tumor growth. The purpose of this study was to determine whether tumor cells upregulate NO as a cytoprotective measure during PDT. Breast tumor COH-BR1 cells sensitized in mitochondria with 5-aminolevulinic acid (ALA)-derived protoporphyrin IX died apoptotically following irradiation, ALA- and light-only controls showing no effect. Western analysis revealed that inducible nitric oxide synthase (iNOS) was upregulated &amp;gt;3-fold within 4 h after ALA/light treatment, while o...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3254948</comments>
            <pubDate>Tue, 02 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3254948</guid>        </item>
        <item>
            <title>Redox-Mediated Reciprocal Regulation of SERCA and Na(+)/Ca(2+)-Exchanger Contributes to SR Ca(2+)-Depletion in Cardiac Myocytes.</title>
            <link>http://www.medworm.com/index.php?rid=3248860&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20132882%26dopt%3DAbstract</link>
            <description>In conclusion, redox-mediated SR Ca(2+)-depletion involves reciprocal regulation of SERCA and NCX, possibly via direct oxidative modification of both proteins.
    PMID: 20132882 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3248860</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3248860</guid>        </item>
        <item>
            <title>Influence of serum albumin and the flavonol quercetin on the peroxidase activity of metmyoglobin.</title>
            <link>http://www.medworm.com/index.php?rid=3248859&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20132883%26dopt%3DAbstract</link>
            <description>Authors: Lorrain B, Dufour C, Dangles O
    Metmyoglobin (MbFe(III)), a major form of dietary iron, is an efficient inducer of lipid and protein oxidation. Indeed, MbFe(III) is able to cleave hydrogen peroxide and lipid hydroperoxides with subsequent formation of ferrylmyoglobin (MbFe(IV)=O) and lipid oxyl and peroxyl radicals. In the first part of this work, the mechanism of the reaction between MbFe(III) and H(2)O(2) is revisited with an emphasis on the influence of bovine serum albumin (BSA). BSA does not affect the rate of MbFe(IV)=O formation but inhibits the formation of the redox-inactive green pigment (heme-protein cross-link species). Although tightly bound to BSA, the flavonol quercetin is still able to reduce MbFe(IV)=O as a likely result of long-range electron transfers within ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3248859</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3248859</guid>        </item>
        <item>
            <title>Capsiate inhibits ultraviolet B-induced skin inflammation by inhibiting Src family kinases and epidermal growth factor receptor signaling.</title>
            <link>http://www.medworm.com/index.php?rid=3244605&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20123015%26dopt%3DAbstract</link>
            <description>Authors: Lee EJ, Jeon MS, Kim BD, Kim JH, Kwon YG, Lee H, Lee YS, Yang JH, Kim TY
    Capsiate, one of the major capsaicinoids is non-pungent, and present in sweet pepper. We investigated the effects of capsiate on the ultraviolet B (UVB)-induced inflammatory response in skin and its molecular mechanisms. Capsiate-pretreated human keratinocytes inhibited intracellular reactive oxygen species (ROS), which activate mitogen-activated protein kinase (MAPK) and nuclear factor-B (NF-B) pathways. Therefore, we determined the effect of capsiate on these pathways. Capsiate inhibited UVB-induced cyclooxygenase-2 (COX-2) expression, extracellular signal-related kinase 1/2 (ERK1/2) phosphorylation, nuclear translocation of NF-B, and the expression of proinflammatory cytokines and potent angiogenic fac...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3244605</comments>
            <pubDate>Fri, 29 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244605</guid>        </item>
        <item>
            <title>Regulation of DHICA-mediated antioxidation by dopachrome tautomerase: Implication for skin photoprotection against UVA radiation.</title>
            <link>http://www.medworm.com/index.php?rid=3244604&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20123016%26dopt%3DAbstract</link>
            <description>Authors: Jiang S, Liu XM, Dai X, Zhou Q, Lei TC, Beermann F, Wakamatsu K, Xu SZ
    Dopachrome tautomerase (Dct) is a critical enzyme in the melanogenesis pathway that isomerizes the intermediate dopachrome to 5,6-dihydroxyindole-2-carboxylic acid (DHICA) and influences the proportion of DHICA monomer incorporated into the 5,6-dihydroxyindole (DHI) polymer in eumelanin. To investigate whether Dct inactivation affects skin photoprotection against ultraviolet radiation, we examined levels of reactive oxygen species (ROS), sunburn cell formation, epidermal cell apoptosis, and melanin composition in skins of Dct-/-knockout mice compared with skins of wild-type C57 BL/6 mice under UVA-induced oxidative stress. The results demonstrate that Dct inactivation elevates the level of ROS, increases th...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3244604</comments>
            <pubDate>Fri, 29 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244604</guid>        </item>
        <item>
            <title>Hydroethidine- and Mito-SOX-derived red fluorescence is not a reliable indicator of intracellular superoxide formation: Another inconvenient truth.</title>
            <link>http://www.medworm.com/index.php?rid=3236622&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20116425%26dopt%3DAbstract</link>
            <description>Authors: Zielonka J, Kalyanaraman B
    Hydroethidine (or dihydroethidium) (HE) is the most popular fluorogenic probe used for detecting intracellular superoxide radical anion. The reaction between superoxide and HE generates a highly specific red fluorescent product, 2-hydroxyethidium (2-OH-E(+)). In biological systems, another red fluorescent product, ethidium (E(+)), is also formed, usually at a much higher concentration than 2-OH-E(+). In this article, we have reviewed the methods to selectively detect the superoxide-specific product (2-OH-E(+)) and the factors affecting its levels in cellular and biological systems. The most important conclusion of the present review is that it is nearly impossible to assess the intracellular levels of the superoxide specific product, 2-OH-E(+), using...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3236622</comments>
            <pubDate>Wed, 27 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3236622</guid>        </item>
        <item>
            <title>Lipofuscin-bound iron is a major intracellular source of oxidants: role in senescent cells.</title>
            <link>http://www.medworm.com/index.php?rid=3236621&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20116426%26dopt%3DAbstract</link>
            <description>In this study for the first time a lipofuscin-mediated formation of oxidants and the role of iron in this process was directly shown in a model of senescent fibroblasts, as well as in vitro with artificial lipofuscin. We could demonstrate that this oxidant production is independent on mitochondria and is having cytotoxic effects. The ability of lipofuscin to produce oxidants is dependent on the amount of transition metals incorporated. Although the amount of oxidants formed by cellular lipofuscin turned out to be moderate, it is chronic and thus lipofuscin is able to catalyze its own formation.
    PMID: 20116426 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3236621</comments>
            <pubDate>Wed, 27 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3236621</guid>        </item>
        <item>
            <title>Protection of podocytes from hyperhomocysteinemia-induced injury by deletion of gp91(phox) gene.</title>
            <link>http://www.medworm.com/index.php?rid=3236620&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20116427%26dopt%3DAbstract</link>
            <description>Authors: Zhang C, Hu JJ, Xia M, Boini KM, Brimson CA, Laperle LA, Li PL
    In the present study, mice lacking gp91(phox) gene were used to address the role of NADPH oxidase in hyperhomocysteinemia-induced podocyte injury. It was found that the folate-free diet increased plasma homocysteine levels, but failed to increase O(2)(.-) production in the glomeruli from gp91(phox) gene knockout (gp91(-/-)) mice, compared with wild-type (gp91(+/+)) mice. Proteinuria and glomerular damage index (GDI) were significantly lower, while the glomerular filtration rate (GFR) was higher in gp91(-/-) than gp91(+/+) mice when they were on the folate-free diet (Urine albumin excretion: 21.23+/-1.88 vs. 32.86+/-4.03 mug/24 h; GDI: 1.17+/-0.18 vs. 2.59 +/-0.49; and GFR: 53.01+/-4.69 vs. 40.98+/-1.44 muL/min). Hy...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3236620</comments>
            <pubDate>Wed, 27 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3236620</guid>        </item>
        <item>
            <title>Protective effects of hemoglobin-based oxygen carrier given to isolated heart during ischemia via attenuation of mitochondrial oxidative damage.</title>
            <link>http://www.medworm.com/index.php?rid=3236624&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20114072%26dopt%3DAbstract</link>
            <description>In conclusion, our results demonstrated the cardioprotective effect of HBOC on I/R heart and revealed this protection was mediated in large part by attenuation of mitochondrial oxidative damage.
    PMID: 20114072 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3236624</comments>
            <pubDate>Tue, 26 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3236624</guid>        </item>
        <item>
            <title>Induction of caspase - independent apoptotic-like cell death of mouse mammary tumor TA3Ha cells in vitro and reduction of their lethality in vivo by the novel chemotherapeutic agent GIT-27NO.</title>
            <link>http://www.medworm.com/index.php?rid=3236623&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20114073%26dopt%3DAbstract</link>
            <description>Authors: Mijatovic S, Maksimovic-Ivanic D, Timotijevic G, Miljkovic D, Donia M, Libra M, Coco M, McCubrey J, Al-Abed Y, Korac A, Stosic-Grujicic S, Nicoletti F
    New chemical entity ( NCE ) GIT-27NO has been created by the covalent link of the of a NO moiety to the antinflammatory isoxazoline VGX-1027. The compound has been shown to possess powerful anticancer effects both in vitro and in vivo. However, its effect on nonsolid and metastatic forms of tumors has not yet been investigated. We have presently studied the effects of GIT-27NO on the highly invasive mouse mammary TA3Ha cell line in vitro and in vivo. Oppositely to the conventional exogenous NO donor SNP, GIT-27NO successfully enhanced intracellular NO concentration on TA3Ha cells. Intracellular accumulation of NO was followed by...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3236623</comments>
            <pubDate>Tue, 26 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3236623</guid>        </item>
        <item>
            <title>Cellular effects of peptide and protein hydroperoxides.</title>
            <link>http://www.medworm.com/index.php?rid=3223880&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20109544%26dopt%3DAbstract</link>
            <description>In this study exposure of murine macrophage-like cells to pre-formed peptide or protein hydroperoxides is shown to result in hydroperoxide consumption and cellular thiol oxidation; these effects precede loss of cell viability. N-acetyl tryptophan methyl ester hydroperoxides, but not the decomposed species, decreased total cellular thiols and GSH, with the latter occurring more rapidly. Time-dependent inhibition of lysosomal cathepsins B and L was also observed, together with diminished caspase 3/7 activity. A number of other cytosolic thiol- and non-thiol dependent enzymes were not affected significantly. Hydroperoxides formed on BSA did not deplete total thiols or GSH within cells, although such reactions are rapid in model systems. In contrast, selective inhibition of cathepsins B and L ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3223880</comments>
            <pubDate>Mon, 25 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3223880</guid>        </item>
        <item>
            <title>Dynamic and Interacting Profiles of (.)NO and O2 in Rat Hippocampal Slices.</title>
            <link>http://www.medworm.com/index.php?rid=3212739&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100565%26dopt%3DAbstract</link>
            <description>Authors: Ledo A, Barbosa R, Cadenas E, Laranjinha J
    Nitric oxide ((.)NO) is a ubiquitous signaling molecule that participates in the neuromolecular phenomena associated with memory formation. In the hippocampus, neuronal (.)NO production is coupled to the activation of the NMDA-type of glutamate receptor. Although, (.)NO-mediated signaling has been associated with soluble guanylate cyclase activation, cytochrome oxidase is also a target for this gaseous free radical, for which (.)NO competes with O(2). Here, we show, for the first time in a model preserving tissue cytoarchitecture (rat hippocampal slices) and at a physiological O(2) concentration, that endogenous NMDA-evoked (.)NO production inhibits tissue O(2) consumption for submicromolar concentrations. The simultaneous real-time r...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212739</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212739</guid>        </item>
        <item>
            <title>Photoactivated multivitamin preparation induces poly(ADP-ribosyl)ation, a DNA damage response in mammalian cells.</title>
            <link>http://www.medworm.com/index.php?rid=3212738&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100566%26dopt%3DAbstract</link>
            <description>This study also underlines the importance of protecting MVP solution from light before use in preterm infants.
    PMID: 20100566 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212738</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212738</guid>        </item>
        <item>
            <title>Transduced Tat-SAG fusion protein protects against oxidative stress and brain ischemic insult.</title>
            <link>http://www.medworm.com/index.php?rid=3212737&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100567%26dopt%3DAbstract</link>
            <description>Authors: Kim DW, Lee SH, Jeong MS, Sohn EJ, Kim MJ, Jeong HJ, An JJ, Jang SH, Won MH, Hwang IK, Cho SW, Kang TC, Lee KS, Park J, Yoo KY, Eum WS, Choi SY
    Reactive oxygen species (ROS) have been implicated in the pathogenesis of ischemic brain injury. Sensitive to apoptosis gene (SAG) is a RING finger protein that exhibits antioxidant activity against a variety of redox reagents. However, the protective effect of SAG in brain ischemic injury is unclear. Here, we investigated the protective effects of Tat-SAG fusion protein against cell death and ischemic insults. When Tat-SAG fusion protein was added to the culture medium of astrocye cells, it rapidly entered the cells and protected them against oxidative stress-induced cell death. Immunohistochemical analysis revealed that, when Tat-SAG...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212737</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212737</guid>        </item>
        <item>
            <title>Dynamics of H(2)O(2) Availability to ARPE-19 Cultures in Models of Oxidative Stress.</title>
            <link>http://www.medworm.com/index.php?rid=3212736&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100568%26dopt%3DAbstract</link>
            <description>Authors: Kaczara P, Sarna T, Burke JM
    Oxidative injury to cells such as the retinal pigment epithelium (RPE) is often modeled using H(2)O(2)-treated cultures, but H(2)O(2) concentrations are not sustained in culture medium. Here medium levels of H(2)O(2) and cytotoxicity were analyzed in ARPE-19 cultures following H(2)O(2) delivery as a single pulse or with continuous generation using glucose oxidase (GOx). When added as a pulse, H(2)O(2) is rapidly depleted (within 2 hr); cytotoxicity at 24, determined by the MTT assay for mitochondrial function, is unaffected by medium replacement at 2 hr. Continuous generation of H(2)O(2) produces complex outcomes. At low GOx concentrations, H(2)O(2) levels are sustained by conditions in which generation matches depletion, but when GOx concentration...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212736</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212736</guid>        </item>
        <item>
            <title>The NRF2-heme oxygenase-1 system modulates cyclosporine A-induced epithelial-mesenchymal transition and renal fibrosis.</title>
            <link>http://www.medworm.com/index.php?rid=3212740&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096777%26dopt%3DAbstract</link>
            <description>Authors: Shin DH, Park HM, Jung KA, Choi HG, Kim JA, Kim DD, Kim SG, Kang KW, Ku SK, Kensler TW, Kwak MK
    Epithelial-mesenchymal transition (EMT) is an underlying mechanism of tissue fibrosis by generating myofibroblasts, which serve as the primary source of extracellular matrix production from tissue epithelial cells. Recently, it has been suggested that EMT is implicated in immunosuppressive cyclosporine A (CsA)-induced renal fibrosis. In the present study, the potential role of NRF2, which is the master regulator of genes associated with the cellular antioxidant defense system, in CsA-induced EMT-renal fibrosis has been investigated. Pre-treatment of rat tubular epithelial NRK-52E cells with sulforaphane, an activator of NRF2, could prevent EMT gene changes such as the loss of E-cadh...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212740</comments>
            <pubDate>Wed, 20 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212740</guid>        </item>
        <item>
            <title>Early and late administration of MnTE-2-PyP(5+) in mitigation and treatment of radiation-induced lung damage.</title>
            <link>http://www.medworm.com/index.php?rid=3212742&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096348%26dopt%3DAbstract</link>
            <description>CONCLUSION: The catalytic manganese porphyrin antioxidant and modulator of redox-based signalling pathways, MnTE-2-PyP(5+), mitigates radiation-induced lung injury when given within the first 12 hours after IR. More importantly, this is the first study to demonstrate MnTE-2-PyP(5+)can reverse overall lung damage when started at the time of established lung injury 8 weeks post IR. The radioprotective effects are presumably mediated through both its ability to suppress oxidative stress as well as to decrease activation of key transcription factors and proangiogenic and profibrogenic cytokines.
    PMID: 20096348 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212742</comments>
            <pubDate>Tue, 19 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212742</guid>        </item>
        <item>
            <title>Zinc inhibits oxidative stress induced iron signaling and apoptosis in Caco-2 cells.</title>
            <link>http://www.medworm.com/index.php?rid=3212741&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096349%26dopt%3DAbstract</link>
            <description>Authors: Kilari S, Pullakhandam R, Nair KM
    Studies in humans and animals have suggested negative interactions of iron and zinc during their intestinal absorption. Further, zinc appears to prevent the iron induced oxidative damage in rats, which was hypothesized to be through the modulation of intracellular iron signaling pathway. The aim of the present study was, therefore, to understand the effect of zinc on oxidant induced iron signaling and cell death in human enterocyte like Caco-2 cells. We demonstrated that zinc decreases the glucose/glucose oxidase (H(2)O(2) generating system) induced iron uptake, inhibits the iron regulatory protein 1 activation, and divalent metal ion transporter 1 expression. There was also a concomitant decrease in oxidant induced intracellular labile iron a...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212741</comments>
            <pubDate>Tue, 19 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212741</guid>        </item>
        <item>
            <title>Mitochondrial reserve capacity in endothelial cells: The impact of nitric oxide and reactive oxygen species.</title>
            <link>http://www.medworm.com/index.php?rid=3200961&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20093177%26dopt%3DAbstract</link>
            <description>In this study, we used extracellular flux analysis to measure mitochondrial function in adherent bovine aortic endothelial cells (BAEC). Under basal conditions, BAEC use only ~35% of their maximal respiratory capacity. We calculate that this represents an intermediate respiratory State between States 3 and 4 which we define as Stateapparent equal to 3.64. Interestingly, the apparent respiratory control ratio (maximal mitochondrial oxygen consumption/non-ADP linked respiration) in these cells is on the order of 23 which is substantially higher than that which is frequently obtained with isolated mitochondria. These results suggest that mitochondria in endothelial cells are highly coupled and possess a considerable bioenergetic reserve. Since endothelial cells are exposed to both reactive ox...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3200961</comments>
            <pubDate>Mon, 18 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3200961</guid>        </item>
        <item>
            <title>Repeated pulmonary exposure to single-walled carbon nanotubes exacerbates allergic inflammation of the airway: Possible role of oxidative stress.</title>
            <link>http://www.medworm.com/index.php?rid=3200960&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20093178%26dopt%3DAbstract</link>
            <description>This study examined the effects of pulmonary exposure to a type of nano-sized carbon nanotube (single-walled nanotubes: SWCNT) on allergic airway inflammation and sought their cellular mechanisms. In vivo, ICR mice were divided into four experimental groups to repeatedly administer vehicle, SWCNT (50mug/animal), ovalbumin (OVA: allergen), or OVA + SWCNT through intratracheal route; thereafter assayed. SWCNT aggravated allergen-induced pulmonary inflammation with mucus hyperplasia. SWCNT with allergen amplified lung protein levels of helper T (Th) cytokines and chemokines related to allergy and exhibited adjuvant activity for allergen-specific IgG(1) (and IgE) compared with allergen alone. SWCNT accentuated the level/activity of oxidative stress-related biomarkers in the airways in the pres...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3200960</comments>
            <pubDate>Mon, 18 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3200960</guid>        </item>
        <item>
            <title>Linking oxidative stress to inflammation: Toll-like receptors.</title>
            <link>http://www.medworm.com/index.php?rid=3194527&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20083193%26dopt%3DAbstract</link>
            <description>Authors: Gill R, Tsung A, Billiar TR
    Injury caused by oxidative stress occurs in many clinical scenarios involving ischemia and reperfusion such as organ transplantation, hemorrhagic shock (HS), myocardial infarction and cerebral vascular accidents. Activation of the immune system as a result of disturbances in the redox state of cells appears to contribute to tissue and organ damage in these conditions. The link between oxidative stress and inflammatory pathways is poorly understood. Recently, Toll like receptors (TLRs) have been shown to mediate the inflammatory response seen in experimental ischemia and reperfusion (I/R). The TLR family of receptors involved in alerting the innate immune system of danger appears to be activated by damage associated molecular pattern molecules (DAMPs...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3194527</comments>
            <pubDate>Fri, 15 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3194527</guid>        </item>
        <item>
            <title>Paclitaxel Combined with Inhibitors of Glucose and Hydroperoxide Metabolism Enhances Breast Cancer Cell Killing Via H(2)O(2)-Mediated Oxidative Stress.</title>
            <link>http://www.medworm.com/index.php?rid=3194526&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20083194%26dopt%3DAbstract</link>
            <description>Authors: Hadzic T, Aykin-Burns N, Zhu Y, Coleman MC, Leick K, Jacobson GM, Spitz DR
    Cancer cells (relative to normal cells) demonstrate alterations in oxidative metabolism characterized by increased steady-state levels of reactive oxygen species [i.e. hydrogen peroxide, H(2)O(2)] that may be compensated for by increased glucose metabolism but the therapeutic significance of these observations is unknown. In the current study, inhibitors of glucose [i.e., 2-deoxy-D-glucose, 2DG] and hydroperoxide [i.e., L-buthionine-S, R-sulfoximine, BSO] metabolism were utilized in combination with a chemotherapeutic agent paclitaxel [PTX], thought to induce oxidative stress, to treat breast cancer cells. 2DG+PTX were found to be more toxic than either agent alone in T47D and MDA-MB231 human breast can...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3194526</comments>
            <pubDate>Fri, 15 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3194526</guid>        </item>
        <item>
            <title>Celecoxib activates PI-3K/Akt and mitochondrial redox signaling to enhance heme oxygenase-1-mediated anti-inflammatory activity in vascular endothelium.</title>
            <link>http://www.medworm.com/index.php?rid=3194525&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20083195%26dopt%3DAbstract</link>
            <description>Authors: Hamdulay SS, Wang B, Birdsey GM, Ali F, Dumont O, Evans PC, Haskard DO, Wheeler-Jones CP, Mason JC
    Although non-steroidal anti-inflammatory drugs provide important control of pain and inflammation, they have been over-shadowed by concerns regarding atherothrombotic complications. However, celecoxib appears to have a relatively good cardiovascular profile and may improve endothelial function in coronary heart disease. This led us to the hypothesis that celecoxib induces the vasculoprotective enzyme heme oxygenase-1 (HO-1). In human umbilical vein and aortic endothelial cells, 24-48 hours treatment with celecoxib induced HO-1 mRNA and protein expression and increased HO-1 enzyme activity. This effect was not seen with rofecoxib or indomethacin. Supplementation of culture media w...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3194525</comments>
            <pubDate>Fri, 15 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3194525</guid>        </item>
        <item>
            <title>Regulation of Glycolysis and Expression of Glucose Metabolism-related Genes by Reactive Oxygen Species in Contracting Skeletal Muscle Cells.</title>
            <link>http://www.medworm.com/index.php?rid=3186216&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20080177%26dopt%3DAbstract</link>
            <description>Authors: da Justa Pinheiro CH, Silveira LR, Nachbar RT, Vitzel KF, Curi R
    Contractile activity induces marked increase of glycolytic activity and gene expression of enzymes and transporters involved in glucose metabolism in skeletal muscle. Muscle contraction also increases production of reactive oxygen species (ROS). In the present study, the effect of treatment with N-acetylcysteine (NAC), a potent antioxidant compound, on contraction-stimulated glycolysis was investigated in electrically stimulated primary rat skeletal muscle cells. The following parameters were measured: [(3)H]-2-deoxyglucose (2-DG) uptake, activities of hexokinase (HK), phosphofructokinase (PFK) and glucose-6-phosphate dehydrogenase (G6PDH), lactate production, and expression of glucose transporter 4 (GLUT4), hexo...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186216</comments>
            <pubDate>Thu, 14 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186216</guid>        </item>
        <item>
            <title>CDK2-Nitrosylation and loss of Mitochondrial Potential mediates NO dependent Biphasic Effect on HL-60 Cell Cycle.</title>
            <link>http://www.medworm.com/index.php?rid=3186217&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079829%26dopt%3DAbstract</link>
            <description>Authors: Kumar S, Barthwal MK, Dikshit M
    Nitric oxide (NO), a multifaceted signalling molecule, regulates a wide array of cell functions including proliferation, differentiation, cytostasis and apoptosis, which depends on the cell type and redox status. The present study systematically explores the effect of NO donors on promyelocytic HL-60 cell proliferation and apoptosis. NO donor (DETA-NO) modulated HL-60 cell cycle in a biphasic manner. DETA-NO in lower concentrations (1-100microM) had proliferative effect as investigated by (3)H-thymidine incorporation, BrdU labelling and cell cycle analysis, while cells treated with higher concentrations (250microM-1mM) showed cytostasis, apoptosis, mitochondrial membrane potential loss, caspase-3 activity and dUTP nick end labelling. The prolife...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186217</comments>
            <pubDate>Wed, 13 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186217</guid>        </item>
        <item>
            <title>Monomerized Cu, Zn-superoxide dismutase induces oxidative stress through aberrant Cu binding.</title>
            <link>http://www.medworm.com/index.php?rid=3186224&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079423%26dopt%3DAbstract</link>
            <description>Authors: Kishigami H, Nagano S, Bush AI, Sakoda S
    Mutations in Cu, Zn-superoxide dismutase (SOD1) gene cause familial amyotrophic lateral sclerosis (FALS). Lowering intracellular Cu improves FALS-like phenotype of mutant SOD1 mice. Using immobilized Cu affinity chromatography, we have previously shown that mutant SOD1 is expressed as two affinity fractions, one with high affinity for Cu (SOD1(HAC)), one with low affinity(SOD1(LAC)), whereas wild-type SOD1 is only expressed as SOD1(LAC). Here we further characterize SOD1(HAC) to ascertain the toxicity of mutant SOD1 species. We found that SOD1(HAC) was modified at cysteine residues (Cys) and could be generated from wild-type SOD1 by oxidation of Cys. SOD1(HAC) mainly consisted of monomer, while SOD1(LAC) was dimer. Mutant SOD1s possesse...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186224</comments>
            <pubDate>Tue, 12 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186224</guid>        </item>
        <item>
            <title>Modulation of CTNS Gene Expression By Intracellular Thiols.</title>
            <link>http://www.medworm.com/index.php?rid=3186223&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079424%26dopt%3DAbstract</link>
            <description>Authors: Bellomo F, Corallini S, Pastore A, Palma A, Laurenzi C, Emma F, Taranta A
    The Cysteine/Cystine (Cys/CySS) couple represents one of the major cell thiol/disulfide systems, which is involved in the regulation of several metabolic pathways and cell redox state. Nephropathic cystinosis (NC) is an autosomal recessive disease characterized by renal cellular dysfunction due to mutations in the CTNS gene that encodes for cystinosin, a CySS lysosomal transporter. To analyze the mechanisms involved in cell damage in NC, we have investigated the effects of CTNS gene over-expression or inhibition on cell thiol/disulphide systems and vice versa. Over-expression of the CTNS gene had no remarkable effect on intracellular Cys/CySS and GSH/GSSG redox state. Silencing the CTNS gene increased ce...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186223</comments>
            <pubDate>Tue, 12 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186223</guid>        </item>
        <item>
            <title>Hypoxic Neonatal Pulmonary Arterial Myocytes Are Sensitized To ROS-Generated 8-Isoprostane.</title>
            <link>http://www.medworm.com/index.php?rid=3186222&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079425%26dopt%3DAbstract</link>
            <description>Authors: Gong Y, Yi M, Fediuk J, Lizotte PP, Dakshinamurti S
    8-isoprostane, a ROS-derived prostanoid which acts via thromboxane receptor (TP), is implicated in neonatal pulmonary hypertension. The purpose of this study was to examine the effect of hypoxia on vascular smooth muscle ROS generation, 8-isoprostane activity and TP binding. First passage neonatal porcine pulmonary artery myocytes were exposed to 10% O(2) (hypoxic myocytes; HM) or 21% O(2) (normoxic myocytes; NM) for 72h. Hypoxia increased in vitro generation of ROS, superoxide and 8-isoprostane. ROS generation was ablated by inhibition of mitochondrial complex III. SOD1 and 3 activities were increased, but SOD2 activity decreased by 45% in HM. 8-isoprostane generation was driven by addition of peroxide and nitric oxide; incu...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186222</comments>
            <pubDate>Tue, 12 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186222</guid>        </item>
        <item>
            <title>Implication of oxidative stress as a cause of autoimmune hemolytic anemia in NZB mice.</title>
            <link>http://www.medworm.com/index.php?rid=3186221&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079426%26dopt%3DAbstract</link>
            <description>Authors: Iuchi Y, Kibe N, Tsunoda S, Suzuki S, Mikami T, Okada F, Uchida K, Fujii J
    We have recently shown that deficiency of the superoxide dismutase 1 gene (SOD1) causes anemia and autoimmune responses against red blood cells (RBC), and that transgenic expression of human SOD1 in erythroid cells rescues them. Since these phenotypes observed in SOD1-deficient mice are similar to autoimmune hemolytic anemia (AIHA), a causal connection between reactive oxygen species (ROS) and AIHA was examined using an AIHA-prone New Zealand black (NZB) mouse. ROS levels in RBC were high in young NZB mice, compared to control New Zealand white (NZW) mice, and increased during aging. Methemoglobin and lipid peroxidation products were elevated during aging, consistent with the elevated oxidative stress i...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186221</comments>
            <pubDate>Tue, 12 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186221</guid>        </item>
        <item>
            <title>Oxidative Stress in Skeletal Muscle Stimulates Early Expression of Rad in a Mouse Model of Amyotrophic Lateral Sclerosis.</title>
            <link>http://www.medworm.com/index.php?rid=3186220&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079427%26dopt%3DAbstract</link>
            <description>Authors: Halter B, Gonzalez de Aguilar JL, Rene F, Petri S, Fricker B, Echaniz-Laguna A, Dupuis L, Larmet Y, Loeffler JP
    Motor neuron degeneration and progressive muscle atrophy characterizes amyotrophic lateral sclerosis (ALS) in man and related mutant superoxide dismutase-1 (SOD1) transgenic mice. Our previous microarray studies on ALS muscle revealed strong up-regulation of Ras-related associated with diabetes (Rad), an inhibitor of voltage-gated calcium channels. The mechanisms controlling Rad expression upon disease are unknown. We analysed Rad expression in skeletal muscle from ALS patients and animal models, and investigated whether it is regulated by oxidative stress. In mutant SOD1 mice, Rad up-regulation preceded motor symptoms and markedly increased as disease progressed. In...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186220</comments>
            <pubDate>Tue, 12 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186220</guid>        </item>
        <item>
            <title>Oxidative and nitrative modifications of alpha-enolase in cardiac proteins from diabetic rats.</title>
            <link>http://www.medworm.com/index.php?rid=3186219&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079428%26dopt%3DAbstract</link>
            <description>Authors: Lu N, Zhang Y, Li H, Gao Z
    Many studies reported that oxidative and nitrative stress might be important in the pathogenesis of diabetes. By means of immunoprecipitation analysis, alpha-enolase (EC 4.2.1.11, 2-phospho-D-glycerate hydrolase) was identified as the important target for oxidative and nitrative modifications in diabetic cardiac proteins. The levels of protein carbonyls (PC) and 3-nitrotyrosine (3-NT) residues in alpha-enolase (biomarkers of oxidative and nitrative damage respectively) from cardiac proteins of diabetic rats were determined and compared with age-matched control. After 6 weeks of streptozotocin -administration, the cardiac proteins from diabetic rats showed: (a) the levels of alpha-enolase expression and nitration were clearly increased; (b) whereas th...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186219</comments>
            <pubDate>Tue, 12 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186219</guid>        </item>
        <item>
            <title>CpG Methylation Attenuates Sp1 and Sp3 binding to human extracellular superoxide dismutase promoter and regulates its cell-specific expression.</title>
            <link>http://www.medworm.com/index.php?rid=3186218&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079429%26dopt%3DAbstract</link>
            <description>Authors: Zelko IN, Mueller MR, Folz RJ
    Extracellular superoxide dismutase (EC-SOD) plays an important role in maintaining normal redox homeostasis in the lung. It is expressed at very high levels in pulmonary fibroblasts, alveolar type II epithelial cells and smooth muscle cells. The molecular mechanism(s) governing this cell-specific expression of EC-SOD are mostly unknown. In our previous studies we showed that EC-SOD cell specific expression was not attributed to differential transcriptional regulation, suggesting that other, possibly epigenetic, mechanisms are involved in regulation of its expression. In this paper, we found high levels of promoter methylation in A549 cells and correspondingly low levels of methylation in MRC5 cells. Inhibition of DNA methyltransferase activity by ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186218</comments>
            <pubDate>Tue, 12 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186218</guid>        </item>
        <item>
            <title>Exposure to polychlorinated biphenyls enhances lipid peroxidation in human normal peritoneal and adhesion fibroblasts: a potential role for myeloperoxidase.</title>
            <link>http://www.medworm.com/index.php?rid=3172258&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20067832%26dopt%3DAbstract</link>
            <description>The objective of this study was to determine the effects of polychlorinated biphenyls (PCBs) on LPO, superoxide dismutase (SOD3), myeloperoxidase (MPO), and nitrite/nitrate in human normal peritoneal and adhesion fibroblasts. PCB treatment reduced iNOS expression as well as levels of nitrite/nitrate in both cell lines. Although there was no difference in iNOS expression between the two cell lines, adhesion fibroblasts manifested lower basal levels of MPO as compared to normal peritoneal fibroblasts. There was a reduction in MPO expression and its activity in response to PCB treatment in normal peritoneal fibroblasts; however this effect was minimal in adhesion fibroblasts. Moreover, adhesion fibroblasts manifested higher levels of LPO as compared to normal peritoneal fibroblasts, whereas P...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172258</comments>
            <pubDate>Sat, 09 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172258</guid>        </item>
        <item>
            <title>Green tea averts age-dependent decline of hippocampal signaling systems related to antioxidant defenses and survival.</title>
            <link>http://www.medworm.com/index.php?rid=3172260&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20064606%26dopt%3DAbstract</link>
            <description>Authors: Assun&amp;#xE7;&amp;#xE3;o M, Santos-Marques MJ, Carvalho F, Andrade JP
    We previously found that prolonged consumption of green tea (GT), a rich source of antioxidant polyphenols, protected proteins and lipids against oxidation and reduced lipofuscin deposition in the rat hippocampal formation as well as improved spatial memory during aging. In this work, we sought to investigate whether GT treatment could interfere with age-related changes of redox status and cellular signaling systems related to oxidative stress and survival in the same brain region. To address this issue, 5 male Wistar rats were fed with GT from 12 to 19 months of age (GT-19M) and results compared to those obtained in controls aged 19 months (C-19M). A third group of rats was evaluated at 12 months of age (C-12M) t...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172260</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172260</guid>        </item>
        <item>
            <title>Mutated glutathione-S-transferase in combination with reduced glutathione shows synergistic effect in ameliorating oxidative stress and airway inflammation.</title>
            <link>http://www.medworm.com/index.php?rid=3172259&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20064607%26dopt%3DAbstract</link>
            <description>In conclusion, mGST in combination with GSH has synergistic effect in reducing airway inflammation as compared to individual antioxidants and has potential for the treatment of asthma.
    PMID: 20064607 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172259</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172259</guid>        </item>
        <item>
            <title>Mitochondrial Superoxide Dismutase SOD2, but not Cytosolic SOD1, Plays a Critical Role in Protection against Glutamate-Induced Oxidative Stress and Cell Death in HT22 Neuronal Cells.</title>
            <link>http://www.medworm.com/index.php?rid=3164242&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060889%26dopt%3DAbstract</link>
            <description>Authors: Fukui M, Zhu BT
    Oxidative cell death is an important contributing factor in neurodegenerative diseases. Using HT22 mouse hippocampal neuronal cells as a model, we sought to demonstrate that mitochondria are crucial early targets of glutamate-induced oxidative cell death. We showed that when HT22 cells were transfected with shRNA for knockdown of the mitochondrial superoxide dismutase (SOD2), these cells became more susceptible to glutamate-induced oxidative cell death. The increased susceptibility was accompanied by increased accumulation of mitochondrial superoxide and loss of normal mitochondrial morphology and functions at early time points following glutamate exposure. However, overexpression of SOD2 in these cells reduced mitochondrial superoxide level, protected its morp...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164242</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164242</guid>        </item>
        <item>
            <title>Reactive oxygen species, cellular redox systems and apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=3146718&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20045723%26dopt%3DAbstract</link>
            <description>Authors: Circu ML, Aw TY
    Reactive oxygen species (ROS) are products of normal metabolism and xenobiotic exposure, and depending on concentrations, ROS can be beneficial or harmful to cells and tissues. At physiological low levels, ROS function as &quot;redox messengers&quot; in intracellular signaling and regulation while excess ROS induce oxidative modification of cellular macromolecules, inhibit protein function and promote cell death. Additionally, various redox systems, such as the glutathione, thioredoxin, and pyridine nucleotide redox couples, participate in cell signaling and modulation of cell function, including apoptotic cell death. Cell apoptosis is initiated by extracellular and intracellular signals via two main pathways, the death receptor- or mitochondria-mediated pathways. Variou...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146718</comments>
            <pubDate>Thu, 31 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146718</guid>        </item>
        <item>
            <title>A novel giant peroxisomal superoxide dismutase motif-containing protein.</title>
            <link>http://www.medworm.com/index.php?rid=3146717&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20045724%26dopt%3DAbstract</link>
            <description>Authors: Toutzaris D, Lewerenz J, Albrecht P, Jensen LT, Letz J, Geerts A, Golz S, Methner A
    Oxidative glutamate toxicity in the neuronal cell line HT22 is a model for neuronal cell death by oxidative stress. In this model, extracellular glutamate blocks cystine uptake via the glutamate/cystine-antiporter system x(c)(), eventually leading to depletion of the antioxidant glutathione and cell death. We used subtractive suppression hybridization and a screening procedure using different HT22 sublines to identify transcripts relevantly upregulated in resistance against oxidative glutamate toxicity. One of these coded for a novel protein of 3440 amino acids comprising a superoxide dismutase (SOD) motif, which we named TIGR for &quot;transcript increased in glutamate resistance&quot;. TIGR is mainly e...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146717</comments>
            <pubDate>Thu, 31 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146717</guid>        </item>
        <item>
            <title>Carnosine protects against permanent cerebral ischemia in histidine decarboxylase knock-out mice through reducing glutamate excitotoxicity.</title>
            <link>http://www.medworm.com/index.php?rid=3137080&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20043985%26dopt%3DAbstract</link>
            <description>Authors: Shen Y, He P, Fan YY, Zhang JX, Yan HJ, Hu WW, Ohtsu H, Chen Z
    Recently, we have shown that carnosine protects against NMDA-induced excitotoxicity in differentiated PC12 cells through a histaminergic pathway. However, whether the protective effect of the carnosine metabolic pathway also occurs in ischemic brain is unknown. Utilizing the model of permanent middle cerebral artery occlusion (pMCAO) in mice, we found that carnosine significantly improved neurological function and decreased infarct size both in histidine decarboxylase knock-out and the corresponding wild type mice, to the same extent. Carnosine decreased the glutamate levels, and preserved the expression of glutamate transporter-1 (GLT-1) but not glutamate/aspartate transporter in astrocytes exposed to ischemia in ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3137080</comments>
            <pubDate>Mon, 28 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3137080</guid>        </item>
        <item>
            <title>Oxidative modification sensitizes mitochondrial Apoptosis-Inducing Factor to calpain-mediated processing.</title>
            <link>http://www.medworm.com/index.php?rid=3137079&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20043986%26dopt%3DAbstract</link>
            <description>Authors: Norberg E, Gogvadze V, Vakifahmetoglu H, Orrenius S, Zhivotovsky B
    Although processing of mitochondrial Apoptosis-Inducing Factor (AIF) is essential for its function during apoptosis in most cell types, the detailed mechanisms of AIF cleavage remain elusive. Recent findings indicate that the proteolytic process is Ca(2+)-dependent, and that it is mediated by a calpain located in the mitochondrial intermembrane space. We can now report that, in addition to a sustained intracellular Ca(2+) elevation, enhanced formation of reactive oxygen species (ROS) was a prerequisite step for AIF to be cleaved and released from mitochondria in staurosporine-treated cells. These events occurred independently of the redox state of the mitochondria and were not influenced by binding of pyridine ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3137079</comments>
            <pubDate>Mon, 28 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3137079</guid>        </item>
        <item>
            <title>Nitric Oxide Synthase-2 Regulates Mitochondrial HSP60 Chaperone Function during Bacterial Peritonitis in Mice.</title>
            <link>http://www.medworm.com/index.php?rid=3137078&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20043987%26dopt%3DAbstract</link>
            <description>Authors: Suliman HB, Babiker A, Withers CM, Sweeney TE, Carraway MS, Tatro LG, Bartz RR, Welty-Wolf KE, Piantadosi CA
    Nitric oxide synthase-2 (NOS2) plays a critical role in reactive nitrogen species generation and cysteine modifications that influence mitochondrial function and signaling during inflammation. Here, we investigated the role of NOS2 in hepatic mitochondrial biogenesis during E. coli peritonitis in mice. NOS2(-/-) mice displayed smaller mitochondrial biogenesis responses than Wt mice during E. coli infection according to differences in mRNA levels for the PGC-1alpha co-activator, nuclear respiratory factor-1, mitochondrial transcription factor-A (Tfam), and mtDNA polymerase (Polgamma). NOS2(-/-) mice did not significantly increase mitochondrial Tfam and Polgamma protein l...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3137078</comments>
            <pubDate>Mon, 28 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3137078</guid>        </item>
        <item>
            <title>Regulation of Phagocyte NADPH Oxidase by Hydrogen Peroxide through a Ca(2+)/c-Abl Signaling Pathway.</title>
            <link>http://www.medworm.com/index.php?rid=3137077&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20043988%26dopt%3DAbstract</link>
            <description>In conclusion, H(2)O(2) stimulates NOX2-mediated superoxide generation in neutrophils and K562/NOX2 cells via a signaling pathway involving Ca(2+) influx and c-Abl tyrosine kinase acting upstream of PKCdelta. This positive feedback regulatory pathway has important implications for amplifying the innate immune response and contributing to oxidative stress in inflammatory disorders.
    PMID: 20043988 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3137077</comments>
            <pubDate>Mon, 28 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3137077</guid>        </item>
        <item>
            <title>Photoinflammatory Responses to UV-irradiated Ketoprofen Mediated by the Induction of ROS Generation, Enhancement of Cyclooxygenase-2 Expression and Regulation of Multiple Signaling Pathways.</title>
            <link>http://www.medworm.com/index.php?rid=3129949&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20036733%26dopt%3DAbstract</link>
            <description>In conclusion, this study highlights the particular inflammatory response to a photooxidative drug and suggests that KP-photoinduced inflammatory responses are predominantly attributable to induction of ROS generation and directly impair DNA repair.
    PMID: 20036733 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3129949</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3129949</guid>        </item>
        <item>
            <title>Superoxide anion and proteasomal dysfunction contributes to curcumin-induced paraptosis of malignant breast cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=3129948&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20036734%26dopt%3DAbstract</link>
            <description>Authors: Yoon MJ, Kim EH, Lim JH, Kwon TK, Choi KS
    Curcumin is considered a pharmacologically safe agent that may be useful in cancer chemoprevention and therapy. Here, we show for the first time that curcumin effectively induces paraptosis in malignant breast cancer cell lines, including MDA-MB-435S, MDA-MB-231 and Hs578T cells, by promoting vacuolation that results from swelling and fusion of mitochondria and/or the endoplasmic reticulum (ER). Inhibition of protein synthesis by cycloheximide blocked curcumin-induced vacuolation and subsequent cell death, indicating that protein synthesis is required for this process. The levels of AIP-1/Alix protein, a known inhibitor protein of paraptosis, were progressively downregulated in curcumin-treated malignant breast cancer cells, and AIP-1/...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3129948</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3129948</guid>        </item>
        <item>
            <title>Impairment of mitochondrial respiratory chain activity in aortic endothelial cells induced by glycated LDL.</title>
            <link>http://www.medworm.com/index.php?rid=3129947&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20036735%26dopt%3DAbstract</link>
            <description>Authors: Sangle GV, Chowdhury SK, Xie X, Stelmack GL, Halayko AJ, Shen GX
    Coronary artery disease (CAD) is the leading cause of mortality in diabetic patients. Mitochondrial dysfunction and increased production of reactive oxygen species (ROS) are associated with diabetes and CAD. Elevated levels of glycated LDL (glyLDL) were detected in patients with diabetes. Our previous studies demonstrated that glyLDL increased the generation of ROS and altered the activities of antioxidant enzymes in vascular endothelial cells (EC). The present study examined the effects of glyLDL on oxygen consumption in mitochondria and the activities of key enzymes in mitochondrial electron transport chain (ETC) in cultured porcine aortic EC. The results demonstrated that glyLDL treatment significantly impaire...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3129947</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3129947</guid>        </item>
        <item>
            <title>Update on the oxidative stress theory of aging: Does oxidative stress play a role in aging or healthy aging?</title>
            <link>http://www.medworm.com/index.php?rid=3129946&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20036736%26dopt%3DAbstract</link>
            <description>Authors: Salmon AB, Richardson A, P&amp;#xE9;rez VI
    The oxidative stress theory of aging predicts that manipulations that alter oxidative stress/damage will alter aging. The gold standard for determining whether aging is altered is lifespan, i.e., does altering oxidative stress/damage change lifespan? Mice with genetic manipulations in the antioxidant defense system designed to directly address this prediction have, with few exceptions, shown no change in lifespan. However, when these transgenic/knockout mice are tested using models that develop various types of age-related pathology, they show alterations in progression and/or severity of pathology as predicted by the oxidative stress theory; increased oxidative stress accelerates pathology and reduced oxidative stress retards pathology. ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3129946</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3129946</guid>        </item>
        <item>
            <title>Tempol ameliorates murine viral encephalomyelitis by preserving the blood-brain barrier, reducing viral load and lessening inflammation.</title>
            <link>http://www.medworm.com/index.php?rid=3129950&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20035861%26dopt%3DAbstract</link>
            <description>Authors: Tsuhako MH, Augusto O, Linares E, Chadi G, Giorgio S, Pereira CA
    Multiple sclerosis (MS) is a progressive inflammatory and/or demyelinating disease of the human central nervous system (CNS). Most of the knowledge on the pathogenesis of MS has been derived from murine models, such as experimental autoimmune encephalomyelitis and viral encephalomyelitis. Here, we infected female C57BL/6 mice with a neurotropic strain of the mouse hepatitis virus (MHV-59A) to evaluate whether treatment with the multifunctional antioxidant tempol (4-hydroxy-2,2,6,6-tetramethyl-1-piperidinyloxy) affects the ensuing encephalomyelitis. In non-treated animals, neurological symptoms developed fast: 90% of infected mice died 10 days after virus inoculation and the few survivors presented neurological de...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3129950</comments>
            <pubDate>Tue, 22 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3129950</guid>        </item>
        <item>
            <title>In Vivo Detection of Inducible Nitric Oxide Synthase (iNOS) in Rodent Gliomas.</title>
            <link>http://www.medworm.com/index.php?rid=3122546&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20034558%26dopt%3DAbstract</link>
            <description>Authors: Towner RA, Smith N, Doblas S, Garteiser P, Watanabe Y, He T, Saunders D, Herlea O, Silasi-Mansat R, Lupu F
    Increased iNOS expression is often found in brain tumors, such as gliomas. The goal was to develop and assess a novel molecular MRI (mMRI) probe for in vivo detection of iNOS in rodent models for gliomas (intracerebral implantation of rat C6 or RG2 cells, or ethyl nitroso urea (ENU)-induced glioma). The probe we used incorporated a Gd-DTPA (gadolinium (III) complex of diethylentriamine-N,N,N',N&quot;,N&quot;-penta acetate) backbone with albumin and biotin moieties, and covalent binding of an anti-iNOS antibody (Ab) to albumin (anti-iNOS probe). We used mMRI with the anti-iNOS probe to detect in vivo iNOS levels in gliomas. Non-immune normal rat IgG coupled to albumin-Gd-DTPA-biotin...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122546</comments>
            <pubDate>Mon, 21 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122546</guid>        </item>
        <item>
            <title>Defective Repair of 5-Hydroxy-2'deoxycytidine in Cockayne Syndrome Cells and its Complementation by E.coli Formamidopyrimidine DNA Glycosylase and Endonuclease III.</title>
            <link>http://www.medworm.com/index.php?rid=3119414&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20026203%26dopt%3DAbstract</link>
            <description>Authors: Foresta M, Ropolo M, Degan P, Pettinati I, Kow YW, Damonte G, Poggi A, Frosina G
    Repair of the oxidized purine 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxodG) is inefficient in cells belonging to both complementation groups A and B of Cockayne syndrome (CS), a developmental and neurological disorder characterized by defective transcription coupled-repair. We show here that both CS-A and CS-B cells are further defective in repair of 5-hydroxy-2'-deoxycytidine (5-OHdC), an oxidized pyrimidine with cytotoxic and mutagenic properties. The defect in repair of oxidatively damaged DNA in CS cells thus extends to oxidized pyrimidines, indicating a general flaw in repair of oxidized lesions in this syndrome. The defect could not be reproduced in in vitro repair experiments on oligonucleo...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3119414</comments>
            <pubDate>Wed, 16 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3119414</guid>        </item>
        <item>
            <title>Dietary phenolic acids and ascorbic acid: influence on acid-catalysed nitrosative chemistry in presence and absence of lipids.</title>
            <link>http://www.medworm.com/index.php?rid=3119413&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20026204%26dopt%3DAbstract</link>
            <description>Authors: Combet E, Mesmari AE, Preston T, Crozier A, McColl KE
    Acid-catalysed nitrosation and production of potentially carcinogenic nitrosative species is focused at the gastro-oesophageal junction where salivary nitrite, derived from dietary nitrate, encounters the gastric juice. Ascorbic acid provides protection by converting nitrosative species to nitric oxide (NO). However, NO may diffuse into adjacent lipid, where it reacts with O(2) to reform nitrosative species and N-nitrosocompounds (NOC). In this way, ascorbic acid promotes acid nitrosation. Using a novel benchtop model representing the gastro-oesophageal junction, this study aimed to clarify the action of a range of water-soluble antioxidants on the nitrosative mechanisms in presence or absence of lipids. Caffeic, ferulic, g...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3119413</comments>
            <pubDate>Wed, 16 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3119413</guid>        </item>
        <item>
            <title>Chromatin repair after oxidative stress: Role of PARP-mediated proteasome activation.</title>
            <link>http://www.medworm.com/index.php?rid=3119417&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20025963%26dopt%3DAbstract</link>
            <description>In this study, a potential chromatin repair mechanism during oxidative stress was investigated in HT22 cells. The 20S proteasome has been shown to be largely responsible for the degradation of oxidatively modified histone proteins in the nucleus. Poly(ADP-ribosyl)ation reactions also play an important role in DNA repair as a consequence of oxidative damage and single strand breaks. Such a reaction may occur also with the 20S proteasome -with a known increase in enzymatic activity-and also with histones - reducing their proteolytic susceptibility as shown for the first time here. After hydrogen peroxide treatment of HT22 cells, degradation of the model peptide substrate suc-LLVY-MCA and degradation of oxidized histones by nuclear proteasome increased. During the removal of protein carbonyls...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3119417</comments>
            <pubDate>Tue, 15 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3119417</guid>        </item>
        <item>
            <title>Association of urinary 15-F(2t)-isoprostane level with oxygen desaturation and carotid intima-media thickness in non-obese sleep apnea patients.</title>
            <link>http://www.medworm.com/index.php?rid=3119416&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20025964%26dopt%3DAbstract</link>
            <description>Conclusions: These results showed a relationship between lipid peroxidation, carotid intima-media thickness and intermittent hypoxia in non obese OSA patients, thus reinforcing the hypothesis that oxidative stress could be involved in the early atherosclerostic process.
    PMID: 20025964 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3119416</comments>
            <pubDate>Tue, 15 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3119416</guid>        </item>
        <item>
            <title>Effects of age and calorie restriction on tryptophan nitration, protein content and activity of succinyl-CoA:3-ketoacid CoA transferase in rat kidney mitochondria.</title>
            <link>http://www.medworm.com/index.php?rid=3119415&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20025965%26dopt%3DAbstract</link>
            <description>This study examined the protein targets of nitration and the consequent impact on protein function in the rat kidney mitochondria at 4-, 13-, 19-and 24-months of age. Succinyl-CoA transferase (SCOT), a rate-limiting enzyme in the degradation of ketone bodies was the most intensely reactive protein against anti-3-nitrotyrosine antibody in the rat kidney mitochondria. However, subsequent mass spectrometric and amino acid analysis of purified SCOT indicated that tryptophan 372, rather than a tyrosine residue, was the actual site of simultaneous additions of nitro and hydroxy groups. This finding suggests that identification of nitrated tyrosine residues, solely based on reactivity with anti-3-nitrotyrosine antibody, can be potentially misleading. Between 4 and 24 months of age, the amount of ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3119415</comments>
            <pubDate>Tue, 15 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3119415</guid>        </item>
        <item>
            <title>Stabilization of Mitochondrial Function by Tetramethylpyrazine Protects against Kainate-Induced Oxidative Lesions in the Rat Hippocampus.</title>
            <link>http://www.medworm.com/index.php?rid=3105433&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20006702%26dopt%3DAbstract</link>
            <description>In this study, we demonstrate TMP neuroprotection against kainate-induced excitotoxicity in vitro and in vivo. We found that TMP could partly alleviate kainate-induced status epilepticus in rats, prevented and rescued neuronal loss in hippocampal CA3 but not CA1 region. The partial prevention and rescue of neuronal loss by TMP were attributed to the preservation of the structural and functional integrity of mitochondria, evidenced by maintaining mitochondrial membrane potential, ATP production and complexes I and III activities. Stabilization of mitochondrial function was linked to that TMP could function as a reductant/antioxidant to quench ROS, block lipid peroxidation and protect enzymatic antioxidants such as glutathione peroxidase and glutathione reductase. These results suggest that ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3105433</comments>
            <pubDate>Fri, 11 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3105433</guid>        </item>
        <item>
            <title>Inhibition of SREBP-1c-mediated hepatic steatosis and oxidative stress by sauchinone, an AMPK-activating lignan in Saururus chinensis.</title>
            <link>http://www.medworm.com/index.php?rid=3105436&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20005944%26dopt%3DAbstract</link>
            <description>Authors: Kim YW, Kim YM, Yang YM, Kim TH, Hwang SJ, Lee JR, Kim SC, Kim SG
    Sauchinone as an AMP-activating kinase (AMPK)-activating lignan in Saururus chinensis has been shown to prevent iron-induced oxidative stress and liver injury. Sterol regulatory element binding protein-1c (SREBP-1c) plays a key role in hepatic steatosis, which promotes oxidative stress in obese subjects. Previously, we identified the role of AMPK in liver X receptor-alpha (LXRalpha)-mediated SREBP-1c-dependent lipogenesis. Since sauchinone as an antioxidant has the efficacy to activate AMPK, this study investigated its effects on SREBP-1c-dependent lipogenesis in hepatocytes, and high fat diet (HFD)-induced hepatic steatosis and oxidative injury. Sauchinone prevented the ability of LXRalpha agonist (T0901317) to...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3105436</comments>
            <pubDate>Thu, 10 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3105436</guid>        </item>
        <item>
            <title>Modulation of redox status and calcium handling by extremely low-frequency electromagnetic fields in C2C12 muscle cells: A real-time, single-cell approach.</title>
            <link>http://www.medworm.com/index.php?rid=3105435&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20005945%26dopt%3DAbstract</link>
            <description>In conclusion, our data support a possible link between exposure to ELF-EMFs and modification of the cellular redox state, which could, in turn, increase the level of intracellular Ca(2+) and thus modulate the metabolic activity of C2C12 cells.
    PMID: 20005945 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3105435</comments>
            <pubDate>Thu, 10 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3105435</guid>        </item>
        <item>
            <title>Extracellular Superoxide Dismutase Polymorphism in Mice: Allele- Specific Effects on Phenotype.</title>
            <link>http://www.medworm.com/index.php?rid=3105434&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20005946%26dopt%3DAbstract</link>
            <description>Authors: Jun S, Pierce A, Dory L
    Extracellular superoxide dismutase (ecSOD) protects the extracellular matrix (ECM) from oxidative stress. We previously reported a new allele for ecSOD, expressed in 129P3/J mice (129), which differs from the wild-type (wt), expressed in C57BL/6J and other strains, by two amino acid substitutions and a 10 bp deletion in the 3' UTR of the mRNA [1]. The newly discovered allele is associated with a phenotype of significantly increased circulating and heparin-releasable enzyme activities and levels. In order to examine the properties of the two forms of ecSOD in an identical environment we generated, by extensive backcrossing of ecSOD heterozygous progeny to C57BL/6J females, a congenic C57 strain with the 129 (or wt) allele of ecSOD. These mice are homozyg...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3105434</comments>
            <pubDate>Thu, 10 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3105434</guid>        </item>
        <item>
            <title>Thymoquinone rich fraction greatly improves plasma antioxidant capacity and expression of antioxidant genes in hypercholesterolemic rats.</title>
            <link>http://www.medworm.com/index.php?rid=3105437&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20005291%26dopt%3DAbstract</link>
            <description>In conclusion, TQRF and TQ effectively improve the plasma and liver antioxidant capacity and enhanced the expression of liver antioxidant genes of hypercholesterolemic- induced rats.
    PMID: 20005291 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3105437</comments>
            <pubDate>Wed, 09 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3105437</guid>        </item>
        <item>
            <title>Estrogen down-regulates uncoupling proteins and increases oxidative stress in breast cancer.</title>
            <link>http://www.medworm.com/index.php?rid=3072358&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969066%26dopt%3DAbstract</link>
            <description>Authors: Sastre-Serra JJ, Valle AA, Company MM, Garau II, Oliver JJ, Roca PP
    Oxidative stress has been postulated as one of the mechanisms underlying the estrogen carcinogenic effect in breast cancer. Estrogens are known to increase mitochondrial-derived reactive oxygen species (ROS) by an unknown mechanism. Given that uncoupling proteins (UCPs) are a key regulator of mitochondrial energy efficiency and ROS production, our aim was to check the presence and activity of UCPs in ER-positive and-negative breast cancer cells and tumours, as well as their relation with oxidative stress. 1 nM estrogen induced higher oxidative stress in the ER-positive MCF-7, showing increased mitochondrial membrane potential, H2O2 levels and DNA and protein damage than ER-negative MDA-MB-231 cells. All isofor...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072358</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072358</guid>        </item>
        <item>
            <title>Oxidative stress in ALS: Key role in motor neuron injury and therapeutic target.</title>
            <link>http://www.medworm.com/index.php?rid=3072357&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969067%26dopt%3DAbstract</link>
            <description>Authors: Barber SC, Shaw PJ
    Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disorder characterized by death of motor neurons leading to muscle wasting, paralysis and death, usually within 2-3 years of symptom onset. The causes of ALS are not completely understood, and the neurodegenerative processes involved in disease progression are diverse and complex. There is substantial evidence implicating oxidative stress as a central mechanism by which motor neuron death occurs, including: elevated markers of oxidative damage in ALS patient spinal cord and cerebrospinal fluid; and mutations in the anti-oxidant enzyme superoxide dismutase 1 causing approximately 20 % of familial ALS cases. However, the precise mechanism(s) by which mutant SOD1 leads to motor neuron degene...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072357</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072357</guid>        </item>
        <item>
            <title>Iron induces protection and necrosis in cultured cardiomyocytes: Role of reactive oxygen species and nitric oxide.</title>
            <link>http://www.medworm.com/index.php?rid=3072356&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969068%26dopt%3DAbstract</link>
            <description>In conclusion, we propose that Fe-NTA (20 muM) stimulates iNOS activity and that the enhanced NO production, by promoting hypertrophy and enhancing survival mechanisms through ROS reduction, is beneficial to cardiomyocytes. At higher concentrations, however, iron triggers cardiomyocyte death by necrosis.
    PMID: 19969068 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072356</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072356</guid>        </item>
        <item>
            <title>Rutin Metabolites: Novel Inhibitors of Non-oxidative Advanced Glycation End Products.</title>
            <link>http://www.medworm.com/index.php?rid=3072355&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969069%26dopt%3DAbstract</link>
            <description>Authors: Pashikanti S, de Alba DR, Boissonneault GA, Laurean DC
    Glycation is a non-enzymatic condensation reaction between reducing sugars and amino groups of proteins that undergo rearrangements to stable ketoamines, leading to the formation of advanced glycation end products (AGEs) including fluorescent (argpyrimidine) and non-fluorescent (N(varepsilon)-carboxymethyllysine, CML) protein adducts and protein cross-links. AGEs are formed via protein glycation and correlate with processes resulting in aging and diabetes complications. Reactive carbonyl species (RCS) such as glyoxal and methylglyoxal are ubiquitous by-products of cell metabolism, which potently induce formation of AGEs by non-enzymatic protein glycation and may achieve plasma concentrations of 0.3-1.5 mumol/L (1-5). In th...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072355</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072355</guid>        </item>
        <item>
            <title>Oxidative damage in Parkinson disease. Measurement using accurate biomarkers.</title>
            <link>http://www.medworm.com/index.php?rid=3072354&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969070%26dopt%3DAbstract</link>
            <description>Authors: Seet RC, Lee CY, Lim EC, Tan JJ, Quek AM, Chong WL, Looi WF, Huang SH, Wang H, Chan YH, Halliwell B
    Oxidative damage has been implicated in the pathogenesis of Parkinson disease (PD) but literature data are confusing. Using products of lipid and DNA oxidation measured by accurate methods, we assessed the extent of oxidative damage in PD patients. The levels of plasma F(2)-isoprostanes (F(2)-IsoPs), hydroxyeicosatetraenoic acid products (HETEs), cholesterol oxidation products (COPs), neuroprostanes (F(4)-NPs), phospholipase A(2) (PLA(2)) and platelet activating factor-acetylhydrolase (PAF-AH) activities, urinary 8-hydroxy-2'-deoxyguanosine (8-OHdG) and serum high-sensitivity C-reactive protein (hs-CRP) were compared in 61 PD patients and 61 age-matched controls. The levels of p...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072354</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072354</guid>        </item>
        <item>
            <title>Oxygen Regulates the Effective Diffusion Distance of Nitric Oxide in the Aortic Wall.</title>
            <link>http://www.medworm.com/index.php?rid=3072353&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969071%26dopt%3DAbstract</link>
            <description>In this study, a recently developed experimental setup was used to measure the NO diffusion fluxes across the aortic wall at different oxygen concentrations. It was observed that for a constant NO concentration at the endothelial surface, the measured NO diffusion flux out of the adventitial surface at [O(2)]=0 muM is around 5-fold greater than at [O(2)]=150 muM, indicating that NO is consumed in the aortic wall in an oxygen-dependent manner. Analysis of experimental data shows that the rate of NO consumption in the aortic wall is first order with respect to [NO] and first order with respect to [O(2)], and the rate constant k(1) was determined as (4.0 +/- 0.3)x10(3) M(-1)s(-1). Computer simulations demonstrate that NO concentration distribution significantly changes with oxygen concentrati...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072353</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072353</guid>        </item>
        <item>
            <title>Cannabinoid-2 receptor limits inflammation, oxidative/nitrosative stress and cell death in nephropathy.</title>
            <link>http://www.medworm.com/index.php?rid=3072352&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969072%26dopt%3DAbstract</link>
            <description>Authors: Mukhopardhyay P, Rajesh M, Pan H, Patel V, Mukhopadhyay B, B&amp;#xE1;tkai S, Gao B, Hask&amp;#xF3; G, Pacher P
    Cisplatin is an important chemotherapeutic agent available; however the nephrotoxicity is limiting its clinical use. Enhanced inflammatory response and oxidative/nitrosative stress appear to play a key role in the development of cisplatin-induced nephropathy. Activation of cannabinoid-2 (CB(2)) receptors with selective agonists exerts anti-inflammatory and tissue protective effects in various disease models. We have investigated the role of CB(2) receptors in cisplatin-induced nephrotoxicity using selective CB(2) receptor agonist HU-308 and CB(2) knockout mice. Cisplatin significantly increased inflammation (leukocyte infiltration, CXCL1/2, MCP-1, TNF-alpha and IL1beta level...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072352</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072352</guid>        </item>
        <item>
            <title>The Effect of Disruption of Genes for Peroxiredoxin-2, Glutathione Peroxidase-1 and Catalase on Erythrocyte Oxidative Metabolism.</title>
            <link>http://www.medworm.com/index.php?rid=3072351&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969073%26dopt%3DAbstract</link>
            <description>Authors: Johnson RM, Ho YS, Yu DY, Kuypers FA, Ravindranath Y, Goyette GW
    Peroxiredoxin-2 (Prdx2), a potent peroxide reductant, is the third most abundant protein in the erythrocyte and might be expected to play a major role in the cell's oxidative defenses. However, in this study, experiments with erythrocytes from mice with a disrupted Prdx2 gene found that the cells were not more sensitive to exogenous H(2)O(2) or organic peroxides than wild-type. Intraerythrocytic H(2)O(2) was increased, however, indicating an important role for Prdx2 in detoxifying endogenously-generated H2O2. These results are consistent with proposals that red cell Prdx2 acts stoichiometrically, not catalytically, in reducing peroxides. Additional experiments with mice with disrupted catalase or glutathione pero...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072351</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072351</guid>        </item>
        <item>
            <title>Up-Regulation of Heme Oxygenase-1 in Rat Spleen Following Aniline Exposure.</title>
            <link>http://www.medworm.com/index.php?rid=3072350&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969074%26dopt%3DAbstract</link>
            <description>Authors: Wang J, Ma H, Boor PJ, Ramanujam VM, Ansari GA, Khan MF
    Splenic toxicity of aniline is characterized by vascular congestion, hyperplasia, fibrosis and development of a variety of sarcomas in rats. However, underlying mechanisms by which aniline elicits splenotoxic response are not well understood. Previously we have shown that aniline exposure causes oxidative damage to the spleen. To further explore the oxidative mechanism of aniline toxicity, we evaluated the potential contribution of heme oxygenase-1 (HO-1), which catalyzes heme degradation and releases free iron. Male SD rats were given 1 mmol/kg/day aniline in water by gavage for 1, 4 or 7 days, while respective controls received water only. Aniline exposure led to significant increases in HO-1 mRNA expression in the sple...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072350</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072350</guid>        </item>
        <item>
            <title>Arjunolic acid, a triterpenoid saponin, prevents acetaminophen (APAP) induced liver and hepatocytes injury via the inhibition of APAP bioactivation and JNK-mediated mitochondrial protection.</title>
            <link>http://www.medworm.com/index.php?rid=3072349&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969075%26dopt%3DAbstract</link>
            <description>In conclusion, data suggest that arjunolic acid afforded protection against acetaminophen-induced hepatotoxicity through inhibition of P450-mediated APAP bioactivation and inhibition of JNK-mediated activation of mitochondrial permeabilization.
    PMID: 19969075 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072349</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072349</guid>        </item>
        <item>
            <title>Formation of Methionine-sulfoxide by peroxynitrite at position 1606 of von Willebrand factor inhibits its cleavage by ADAMTS-13. A new prothrombotic mechanism in diseases associated with oxidative stress.</title>
            <link>http://www.medworm.com/index.php?rid=3072348&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969076%26dopt%3DAbstract</link>
            <description>In conclusion, peroxynitrite may contribute to prothrombotic effects, hindering the proteolytic processing by ADAMTS-13 of high molecular weight VWF multimers, which have the highest ability to bind and activate platelets in the microcirculation.
    PMID: 19969076 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3072348</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3072348</guid>        </item>
        <item>
            <title>Hydrogen Peroxide is the Major Oxidant Product of Xanthine Oxidase.</title>
            <link>http://www.medworm.com/index.php?rid=3036426&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19941951%26dopt%3DAbstract</link>
            <description>Authors: Kelley EE, Khoo NK, Hundley NJ, Malik UZ, Freeman BA, Tarpey MM
    Xanthine oxidase (XO) is a critical source of reactive oxygen species (ROS) in inflammatory disease. Focus, however, has centered almost exclusively on XO-derived superoxide (O(2)(-)) while direct H(2)O(2) production from XO has been less well-investigated. Therefore, we examined the relative quantities of O(2)(-) and H(2)O(2) produced by XO under a range (1-21%) of O(2) tensions. At O(2) concentrations between 10 and 21 %, H(2)O(2) accounted for ~ 75% of ROS production. As O(2) concentrations were lowered, there was a concentration-dependent increase in H(2)O(2) formation, accounting for 90% of ROS production at 1% O(2). Alterations in pH between 5.5 and 7.4 did not affect the relative proportions of H(2)O(2) and...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036426</comments>
            <pubDate>Mon, 23 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036426</guid>        </item>
        <item>
            <title>Evidence for NAD(P)H:quinone oxidoreductase 1 (NQO1)-mediated quinone dependent redox cycling via plasma membrane electron transport (PMET): a sensitive cellular assay for NQO1.</title>
            <link>http://www.medworm.com/index.php?rid=3031350&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19932748%26dopt%3DAbstract</link>
            <description>In conclusion, we have developed a simple real-time cellular assay for NQO1 and show that PMET plays a significant role in DMNQ redox cycling via NQO1 leading to cellular toxicity in cells with high NQO1 levels.
    PMID: 19932748 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031350</comments>
            <pubDate>Fri, 20 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031350</guid>        </item>
        <item>
            <title>Yeast frataxin mutants display decreased superoxide dismutase activities crucial to promote protein oxidative damage.</title>
            <link>http://www.medworm.com/index.php?rid=3031355&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19932164%26dopt%3DAbstract</link>
            <description>Authors: Irazusta V, Obis E, Moreno-Cerme&amp;#xF1;o A, Cabiscol E, Ros J, Tamarit J
    Iron overload is involved in several pathological conditions, including Friedreich ataxia, a disease caused by decreased expression of the mitochondrial protein frataxin. In a previous study,we identified 14 proteins selectively oxidized in yeast cells lacking Yfh1, the yeast frataxin homolog. Most of these were magnesium-binding proteins. Decreased Mn-SOD activity, oxidative damage to CuZn-SOD, and increased levels of chelatable iron were also observed in this model. The present study explores the relationship between low SOD activity, the presence of chelatable iron and protein damage was investigated in more detail. We observed that addition of copper and manganese to the culture medium restored SOD act...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031355</comments>
            <pubDate>Thu, 19 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031355</guid>        </item>
        <item>
            <title>Nitrated oleic acid up-regulates PPAR-gamma and attenuates experimental inflammatory bowel disease.</title>
            <link>http://www.medworm.com/index.php?rid=3031354&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19932165%26dopt%3DAbstract</link>
            <description>Authors: Borniquel S, Jansson EA, Cole MP, Freeman BA, Lundberg JO
    Nitric oxide and its metabolites undergo nitration reactions with unsaturated fatty acids during oxidative inflammatory conditions, forming electrophilic nitro-fatty acid derivatives. These endogenous electrophilic mediators activate anti-inflammatory signalling reactions, serving as high affinity ligands for peroxisome proliferator-activated receptor gamma (PPARgamma). Here we examined the therapeutic effects of 9- or 10-nitro-octadecenoicoleic acid (OA-NO(2)) and native oleic acid (OA) in a mouse model of colitis. OA-NO(2) reduced the Disease Activity Index (DAI) and completely prevented the Dextran Sulfate Sodium (DSS)-induced colon shortening, and the increase in colonic p65 expression. Increased PPARgamma expressio...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031354</comments>
            <pubDate>Thu, 19 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031354</guid>        </item>
        <item>
            <title>Ginsenoside protopanaxatriol protects endothelial cells from hydrogen peroxide induced cell injury and cell death via modulating intracellular redox status.</title>
            <link>http://www.medworm.com/index.php?rid=3031353&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19932166%26dopt%3DAbstract</link>
            <description>Authors: Kwok HH, Ng WY, Yang MS, Mak NK, Wong RN, Yue PY
    Ginsenosides, the active components of the famous Chinese herb ginseng, has been suggested to possess cardiovascular-protective effects. The mechanism of ginsenosides is believed to associate with their ability to prevent cellular oxidative stress. The purpose of this study is to explore the cyto-protective effect of ginsenoside protopanaxatriol (PPT) on hydrogen peroxide (H(2)O(2)) induced endothelial cell injury and cell death. Pre-treatment of human umbilical vein endothelial cells (HUVECs) with PPT for 24 hours was able to protect the cells against H(2)O(2)-induced injury. Besides cell death, pre-treatment with PPT could also reduce H(2)O(2)-induced DNA damage, over-activation of the DNA repair enzyme PARP-1 and concomitant ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031353</comments>
            <pubDate>Thu, 19 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031353</guid>        </item>
        <item>
            <title>A common mutation of the MYH gene is associated with increased DNA oxidation and age-related diseases.</title>
            <link>http://www.medworm.com/index.php?rid=3031352&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19932167%26dopt%3DAbstract</link>
            <description>We describe a common mutation of the MYH gene, which is involved in the repair of oxidative damage to DNA, and its relationship to age, levels of 8-OHdG, and the circulating levels of interleukin-1. We studied 1146 &quot;healthy&quot; and 562 unselected Chinese subjects. We observed a reverse insertion of AluYb8 sequence (AluYb8MYH) to be homozygous in ~25.8% of a &quot;healthy&quot; Chinese population aged 20-29 years, with the incidence of homozygosity decreasing to 15.7% by age 50-59 years. Since subjects were selected on the basis of absence of disease during medical screening, this suggests that homozygosity for this gene has a marked impact on the development of age-related or chronic &quot;diseases&quot; or mortality. Since the MYH gene is involved with DNA repair we assessed whether homozygous carriage of this ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031352</comments>
            <pubDate>Thu, 19 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031352</guid>        </item>
        <item>
            <title>Curcumin prevents free radical mediated cataractogenesis through modulations in lens calcium.</title>
            <link>http://www.medworm.com/index.php?rid=3031351&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19932168%26dopt%3DAbstract</link>
            <description>Authors: Manikandan R, Thiagarajan R, Beulaja S, Sudhandiran G, Arumugam M
    The generation of free radicals has been implicated in the causation of cataract and compounds that can scavenge free radicals ameliorate the disease process. The present study was aimed to investigate the possible free radical scavenging potential of curcumin at a dose of 75 mg/ kg body weight on selenium-induced cataract in rat pups. Intraperitoneal injection of sodium selenite (15 micromole/ kg body wt.) to 8-10 days old rat pups led to severe oxidative stress in eye lens as evidenced by increased nitric oxide, superoxide anion, hydroxyl radical generation and inducible nitric oxide synthase expression that probably led to cataract formation. Selenium exposure also caused an increase in total calcium in eye l...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031351</comments>
            <pubDate>Thu, 19 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031351</guid>        </item>
        <item>
            <title>In vivo radioprotection studies of 3,3'-Diselenodipropionic acid (DSePA), a selenocystine derivative.</title>
            <link>http://www.medworm.com/index.php?rid=3031356&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19931386%26dopt%3DAbstract</link>
            <description>In conclusion, these findings clearly confirm that DSePA exhibits protective effects against whole body gamma-radiation and the probable mechanisms of action involve the maintenance of antioxidant enzymes, the prophylactic action through the attenuation of the DNA damage and the inhibition of apoptosis.
    PMID: 19931386 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3031356</comments>
            <pubDate>Tue, 17 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3031356</guid>        </item>
        <item>
            <title>Total body irradiation causes residual bone marrow injury by induction of persistent oxidative stress in murine hematopoietic stem cells.</title>
            <link>http://www.medworm.com/index.php?rid=3019370&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19925862%26dopt%3DAbstract</link>
            <description>Authors: Wang Y, Liu L, Pazhanisamy SK, Li H, Meng A, Zhou D
    Ionizing radiation (IR) and/or chemotherapy cause not only acute tissue damage but also late effects including long-term (or residual) bone marrow (BM) injury. The induction of residual BM injury is primarily attributable to the induction of hematopoietic stem cell (HSC) senescence. However, neither the molecular mechanisms by which IR and/or chemotherapy induce HSC senescence have been clearly defined, nor has an effective treatment been developed to ameliorate the injury. Thus, they were investigated in the present study. The results from this study showed that exposure of mice to a sublethal dose total body irradiation (TBI) induced a persistent increase in reactive oxygen species (ROS) production in HSCs only. The inducti...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3019370</comments>
            <pubDate>Mon, 16 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3019370</guid>        </item>
        <item>
            <title>Inhibition of hepatic mitochondrial aldehyde dehydrogenase by carbon tetrachloride through JNK-mediated phosphorylation.</title>
            <link>http://www.medworm.com/index.php?rid=3019371&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19922789%26dopt%3DAbstract</link>
            <description>Authors: Moon KH, Lee YM, Song BJ
    The aim of this study was to investigate the inhibitory mechanism of mitochondrial aldehyde dehydrogenase (ALDH2) by carbon tetrachloride (CCl(4)). CCl(4) administration caused marked hepatocyte ballooning and necrosis in the pericentral region. CCl(4) also inhibited hepatic ALDH2 activity in a time-dependent manner without altering the protein level, suggesting ALDH2 inhibition through covalent modifications such as phosphorylation by JNK. To demonstrate phosphorylation, isoelectric points (pI) of ALDH2 in CCl(4)-exposed rats were compared to those of untreated controls. Immunoblot analysis revealed that immunoreactive ALDH2 bands in CCl(4)-exposed rats were shifted to acidic pI ranges on two-dimensional electrophoresis (2-DE) gels. Incubation with al...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3019371</comments>
            <pubDate>Fri, 13 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3019371</guid>        </item>
        <item>
            <title>Loss of Nrf2 markedly exacerbates non-alcoholic steatohepatitis.</title>
            <link>http://www.medworm.com/index.php?rid=3000554&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19914374%26dopt%3DAbstract</link>
            <description>Authors: Chowdhry S, Nazmy MH, Meakin PJ, Dinkova-Kostova AT, Walsh SV, Tsujita T, Dillon JF, Ashford ML, Hayes JD
    Non-alcoholic steatohepatitis (NASH) arises from non-alcoholic fatty liver disease (NAFLD) as a consequence of oxidative stress. Herein we report that the development of NASH is greatly accelerated in mice lacking transcription factor Nrf2 when they are challenged with a methionine- and choline-deficient (MCD) diet. Following 14-days feeding on an MCD diet, livers from Nrf2(-/-) mice showed a substantial increase in macro- and micro-vesicular steatosis and a massive increase in the number of neutrophil polymorphs, when compared to livers from wild-type mice treated similarly. Livers of Nrf2(-/-) mice on the MCD diet suffered more oxidative stress than their wild-type count...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000554</comments>
            <pubDate>Thu, 12 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000554</guid>        </item>
        <item>
            <title>Dietary nitrate reduces maximal oxygen consumption while maintaining work performance at maximal exercise.</title>
            <link>http://www.medworm.com/index.php?rid=3000555&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19913611%26dopt%3DAbstract</link>
            <description>Conclusion: A moderate dietary dose of nitrate significantly reduces VO(2)max during maximal exercise with a large active muscle mass. This reduction occurred with a trend towards increased time to exhaustion implying that two separate mechanisms are involved; one that reduces VO(2)max and another that improves the energetic function of the working muscles.
    PMID: 19913611 [PubMed - as supplied by publisher] (Source: Free Radical Biology and Medicine)</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000555</comments>
            <pubDate>Wed, 11 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000555</guid>        </item>
        <item>
            <title>Ferroportin1 but not hephaestin contributes to iron accumulation in a cell model of Parkinson's disease.</title>
            <link>http://www.medworm.com/index.php?rid=3000557&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19913091%26dopt%3DAbstract</link>
            <description>Authors: Song N, Wang J, Jiang H, Xie J
    Iron induced oxidative stress was thought to play a crucial role in the pathogenesis of Parkinson's disease (PD). Based on our previously in vivo experiments that iron transporters ferroportin1 (FP1) and hephaestin (HP) down-regulations might account for the nigral iron accumulation in 6-hydroxydopamine (6-OHDA) lesioned animal models, in the present study we investigated whether FP1 and HP were involved in cellular iron accumulation and the underlying mechanisms in a cell model of PD. The findings showed that 6-OHDA induced FP1 and HP down-regulation, followed by decreased iron efflux and iron accumulation in primary ventral mesencephalic neurons and MES23.5 dopaminergic cells. Silencing of FP1 but not HP led to increased iron level and aggravat...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000557</comments>
            <pubDate>Tue, 10 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000557</guid>        </item>
        <item>
            <title>Reactions of Nitrite in Erythrocyte Suspensions Measured by Membrane Inlet Mass Spectrometry.</title>
            <link>http://www.medworm.com/index.php?rid=3000556&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19913092%26dopt%3DAbstract</link>
            <description>Authors: Mikulski R, Tu C, Swenson ER, Silverman DN
    The reactions of nitrite with deoxygenated human erythrocytes were examined using membrane inlet mass spectrometry to detect the accumulation of NO in extracellular solution. In this method an inlet utilizing a silicon rubber membrane is submerged in cell suspensions and allows NO to pass from extracellular solution into the mass spectrometer. This provides a direct, continuous, and quantitative determination of nitric oxide concentrations over long periods without the necessity of purging the suspension with inert gas. We have not observed accumulation of NO when compared with controls on a physiologically relevant time scale and conclude that, within the limitations of the mass spectrometric method and our experimental conditions, e...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000556</comments>
            <pubDate>Tue, 10 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000556</guid>        </item>
        <item>
            <title>Benzene and dopamine catechol quinones could initiate cancer or neurogenic disease.</title>
            <link>http://www.medworm.com/index.php?rid=3000558&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19909805%26dopt%3DAbstract</link>
            <description>Authors: Zahid M, Saeed M, Rogan EG, Cavalieri EL
    Catechol quinones of estrogens react with DNA by 1,4-Michael addition to form depurinating N3Ade and N7Gua adducts. Loss of these adducts from DNA creates apurinic sites that can generate mutations leading to cancer initiation. We compared reaction of the catechol quinones of the leukemogenic benzene (CAT-Q) and N-acetyldopamine (NADA-Q) with dG or DNA. NADA was used to prevent intramolecular cyclization of dopamine quinone. Reaction of CAT-Q or NADA-Q with dG at pH 4 afforded CAT-4-N7dG or NADA-6-N7dG, which lost deoxyribose with a half-life of 3 h to form CAT-4-N7Gua or 4 h to form NADA-6-N7Gua. When CAT-Q or NADA-Q was reacted with DNA, N3Ade adducts were formed and lost from DNA instantaneously, whereas N7Gua adducts were lost over ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000558</comments>
            <pubDate>Mon, 09 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000558</guid>        </item>
        <item>
            <title>Nitration of the Mitochondrial Complex I Subunit NDUFB8 Elicits RIP1 and 3-Mediated Necrosis.</title>
            <link>http://www.medworm.com/index.php?rid=2977842&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19897030%26dopt%3DAbstract</link>
            <description>Authors: Davis CW, Hawkins BJ, Ramasamy S, Irrinki KM, Cameron BA, Islam K, Daswani VP, Doonan PJ, Manevich Y, Madesh M
    Nitric oxide and other reactive nitrogen species target multiple sites in the mitochondria to impact cellular bioenergetics and survival. Kinetic imaging studies revealed that NO from either activated macrophages or donor compounds rapidly diffuses to the mitochondria, causing a dose dependent progressive increase in NO-dependent DAF fluorescence that corresponded to mitochondrial membrane potential loss, and initiated alterations in cellular bioenergetics that ultimately led to necrotic cell death. Cellular dysfunction is mediated by an elevated 3-nitrotyrosine signature of the mitochondrial complex I subunit NDUFB8, which is vital for normal mitochondrial function a...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2977842</comments>
            <pubDate>Thu, 05 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977842</guid>        </item>
        <item>
            <title>Variation in gene expression profiles of human monocytic U937 cells exposed to various fluxes of nitric oxide.</title>
            <link>http://www.medworm.com/index.php?rid=2972181&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19892011%26dopt%3DAbstract</link>
            <description>We examined early and late alterations in gene expression patterns and phosphorylation levels of key regulators of selected signaling pathways in U937 cells exposed to different (.)NO fluxes. cDNA microarray analysis and real-time quantitative PCR identified NO-sensitive 45 genes (&amp;gt;/=2-fold change) among which KLF2, KLF6, TSC22D3, DDIT4, MKP-5 (up-regulated), KIF23, histone H4, ARL6IP2, CLNS1A, SLC7A6, CDKN3, SRP19, BCL11A (down-regulated) have not been reported before. For two selected genes, KLF2 and DDIT4, the sensitivity to (.)NO was also proved at the protein level. Among the examined genes, only KLF2 had a higher sensitivity to slow release of NO (DETA-NO) than to high-dose, short duration exposure (DPTA-NO), reaching about 50-fold increase in mRNA level. Our study revealed that f...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2972181</comments>
            <pubDate>Mon, 02 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2972181</guid>        </item>
        <item>
            <title>Induction of COX-2/PGE(2)/IL-6 is crucial for cigarette smoke extract-induced airway inflammation: Role of TLR4-dependent NADPH oxidase activation.</title>
            <link>http://www.medworm.com/index.php?rid=2972180&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19892012%26dopt%3DAbstract</link>
            <description>Authors: Lin CC, Lee IT, Yang YL, Lee CW, Kou YR, Yang CM
    Exposure to cigarette smoke extract (CSE) leads to airway and lung inflammation through oxidant-antioxidant imbalance. Cyclooxygenase-2 (COX-2) and prostaglandin E(2) (PGE(2)) have been demonstrated to play critical roles in respiratory inflammation. Here, we show that COX-2/PGE(2)/IL-6 induction is dependent on Toll-like receptor 4 (TLR4)/NADPH oxidase signaling in human tracheal smooth muscle cells (HTSMCs). CSE induced COX-2 expression in vitro in HTSMCs and in vivo in the airways of mice. CSE also directly caused an increase in TLR4. Moreover, CSE-regulated COX-2, PGE(2), and IL-6 generation were inhibited by pretreatment with TLR4 Ab, the inhibitors of c-Src (PP1), NADPH oxidase (diphenylene iodonium chloride and apocynin),...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2972180</comments>
            <pubDate>Mon, 02 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2972180</guid>        </item>
        <item>
            <title>Dps proteins prevent Fenton mediated oxidative damage by trapping hydroxyl radicals within the protein shell.</title>
            <link>http://www.medworm.com/index.php?rid=2972179&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19892013%26dopt%3DAbstract</link>
            <description>Authors: Bellapadrona G, Ardini M, Ceci P, Stefanini S, Chiancone E
    Dps proteins (DNA binding proteins from starved cells) belong to a widespread bacterial family expressed under nutritional and oxidative stress conditions. In particular, Dps proteins protect DNA against Fenton mediated oxidative stress as they catalyze iron oxidation by hydrogen peroxide at highly conserved ferroxidase centers and thus reduce significantly hydroxyl radicals production. The present work investigates the possible generation of intraprotein radicals during the ferroxidation reaction by Escherichia coli and Listeria innocua Dps, two representative members of the family. Stopped flow analyses show that the conserved tryptophan and tyrosine residues located near the metal binding/oxidation center are in a r...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2972179</comments>
            <pubDate>Mon, 02 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2972179</guid>        </item>
        <item>
            <title>Increased levels of cell-free hemoglobin, oxidation markers, and the antioxidative heme scavenger alpha(1)-microglobulin in preeclampsia.</title>
            <link>http://www.medworm.com/index.php?rid=2959854&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19879940%26dopt%3DAbstract</link>
            <description>Authors: Olsson MG, Centlow M, Rutard&amp;#xF3;ttir S, Stenfors I, Larsson J, Hosseini-Maaf B, Olsson ML, Hansson SR, Akerstr&amp;#xF6;m B
    Preeclampsia is a major cause of morbidity and mortality during pregnancy. To date, the pathogenesis of the disease is not fully understood. Recent studies show that preeclampsia is associated with overexpression of hemoglobin genes alpha2 and gamma and accumulation of the protein in the vascular lumen of the placenta. Hypothesizing that cell-free hemoglobin leaks from the placenta into the maternal circulation and contributes to the endothelial damage and symptoms by inducing oxidative stress, we analysed fetal and adult hemoglobin (HbF, HbA), haptoglobin, oxidation markers and the heme scavenger and antioxidant alpha(1)-microglobulin in plasma, urine and ...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2959854</comments>
            <pubDate>Thu, 29 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2959854</guid>        </item>
        <item>
            <title>Improvement of the sensitivity of EPR spin trapping in biological systems by cyclodextrins: A model study with thylakoids and photosystem II particles.</title>
            <link>http://www.medworm.com/index.php?rid=2959853&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19879941%26dopt%3DAbstract</link>
            <description>Authors: Snyrychov&amp;#xE1; I
    Electron paramagnetic resonance (EPR) spin trapping spectroscopy is an important method used in free radical research, however, its application in biological systems is hindered by EPR silencing of spin adducts. Previous studies in superoxide-generating chemical systems have shown that spin adducts can be partially stabilized by cyclodextrins. In this work, for the first time, this proposed protective effect of cyclodextrins is investigated in a real biological sample - in isolated thylakoid membranes and photosystem II (PSII) particles with EMPO as a spin trap. It has been shown that i) randomly methylated-beta-cyclodextrin and 2-hydroxypropyl-beta-cyclodextrin form inclusion complexes with EMPO-superoxide adduct (EMPO-OOH), ii) both cyclodextrins increase t...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2959853</comments>
            <pubDate>Thu, 29 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2959853</guid>        </item>
        <item>
            <title>A key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential.</title>
            <link>http://www.medworm.com/index.php?rid=2959852&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19879942%26dopt%3DAbstract</link>
            <description>Authors: Go YM, Park H, Koval M, Orr M, Reed M, Liang Y, Smith D, Pohl J, Jones DP
    The redox potential (E(h)) of the plasma cysteine/cystine (Cys/CySS) couple (E(h)CySS) is oxidized in association with risk factors for cardiovascular disease (CVD), including age, smoking, type II diabetes, obesity, and alcohol abuse. Previous in vitro findings support a cause-effect relationship of extracellular E(h)CySS in cell signaling pathways associated with CVD, including those controlling monocyte adhesion to endothelial cells. In the present study, we provide evidence that mitochondria are a major source of reactive oxygen species (ROS) in the signaling response to a more oxidized extracellular E(h)CySS. This increase in ROS was blocked by overexpression of mitochondrial thioredoxin-2 (Trx2) in...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2959852</comments>
            <pubDate>Thu, 29 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2959852</guid>        </item>
        <item>
            <title>A Novel Role for Cytochrome c: Efficient Catalysis of S-Nitrosothiol Formation.</title>
            <link>http://www.medworm.com/index.php?rid=2959855&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19879353%26dopt%3DAbstract</link>
            <description>Authors: Basu S, Keszler A, Azarova NA, Nwanze N, Perlegas A, Shiva S, Broniowska KA, Hogg N, Kim-Shapiro DB
    While S-nitrosothiols are regarded as important elements of many NO-dependent signal transduction pathways, the physiological mechanism of their formation remains elusive. Here, we demonstrate a novel mechanism by which cytochrome c may represent an efficient catalyst of S-nitrosation in vivo. In this mechanism, initial binding of GSH to ferric cytochrome c is followed by reaction of NO with this complex, yielding ferrous cytochrome c and GSNO. We show that when submitochondrial particles or cell lysates are exposed to NO in the presence of cytochrome c, there is a robust formation of protein S-nitrosothiols. In the case of submitochondrial particles protein S-nitrosation is par...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2959855</comments>
            <pubDate>Wed, 28 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2959855</guid>        </item>
        <item>
            <title>Ethanol withdrawal increases glutathione adducts of 4-hydroxy-2-hexenal but not 4-hydroxyl-2-nonenal in the rat cerebral cortex.</title>
            <link>http://www.medworm.com/index.php?rid=2959856&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19878718%26dopt%3DAbstract</link>
            <description>In this study rats received an ethanol containing diet for six weeks followed by withdrawal ranging between 0 to 7 days. GSHHE content was elevated (&amp;gt;350%) in the cerebral cortex following two days of withdrawal with no change in GSHNE. The levels of GSHHE were significantly greater (2 to 20-fold) than GSHNE in multiple brain regions. Experiments demonstrated that intoxication and withdrawal did not alter the enzymatic rate of formation of GSHHE or GSHNE, but the rate of formation of GSHHE was higher (~50%) than that of GSHNE. These results indicate that selective oxidative damage to n-3 PUFA occurs in the cerebral cortex as a result of ethanol withdrawal and that 4-hydroxy-hexenal is metabolized to the GSH adduct more efficiently than HNE.
    PMID: 19878718 [PubMed - as supplied by pu...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2959856</comments>
            <pubDate>Tue, 27 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2959856</guid>        </item>
        <item>
            <title>A role for Bach1 and HO-2 in suppression of basal and UVA-induced HO-1 expression in human keratinocytes.</title>
            <link>http://www.medworm.com/index.php?rid=2947942&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19874887%26dopt%3DAbstract</link>
            <description>Authors: Li Zhong J, Raval C, Edwards GP, Tyrrell RM
    Ultraviolet A (UVA) radiation is an oxidizing agent that strongly induces the heme oxygenase 1 (HO1) gene and expression of the protein in cultured human skin fibroblasts but weakly induces it in skin keratinocytes. Lower basal levels of HO-1 and much higher basal levels of HO-2 protein are observed in keratinocytes compared with fibroblasts. Using both over-expression and knock-down approaches, we demonstrate that HO-2 modulates basal and UVA-induced HO-1 protein levels while HO-1 levels do not affect HO-2 levels in skin fibroblasts and keratinocytes. Silencing of Bach1 strongly increases HO-1 levels in HaCaT transformed keratinocytes and these HO-1 levels are not further increased by either UVA irradiation or silencing of HO-2. Thi...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2947942</comments>
            <pubDate>Mon, 26 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2947942</guid>        </item>
        <item>
            <title>Increased thrombin-induced polymerization of fibrinogen associated with high protein carbonyl levels in plasma from patients post myocardial infarction.</title>
            <link>http://www.medworm.com/index.php?rid=2935271&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19857568%26dopt%3DAbstract</link>
            <description>In this study, we have examined representative plasma samples from this group of patients. We show that carbonyls are formed preferentially on fibrinogen and that there is a strong correlation between fibrinogen and total plasma protein carbonyls. Functional properties of fibrinogen isolated from post myocardial plasmas were investigated by measuring thrombin-catalysed polymerization. Fibrinogen from plasma with upper quartile protein carbonyls (mean 0.16 nmol/mg protein) polymerized ~1.4 times more rapidly and gave 1.4 fold higher maximum turbidity (12 per group, p&amp;lt;0.001) than fibrinogen from lower quartile carbonyl plasma (mean 0.007 nmol/mg), which behaved similarly to control plasma. Significant differences were also apparent when related to the carbonyl content of the fibrinogen it...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
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            <pubDate>Fri, 23 Oct 2009 00:00:00 +0100</pubDate>
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        <item>
            <title>Activation of vascular Endothelial Nitric Oxide Synthase and Heme Oxygenase-1 Expression by electrophilic nitro-fatty acids.</title>
            <link>http://www.medworm.com/index.php?rid=2935270&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19857569%26dopt%3DAbstract</link>
            <description>Authors: Khoo NK, Rudolph V, Cole MP, Golin-Bisello F, Schopfer FJ, Woodcock SR, Batthyany C, Freeman BA
    Reactive oxygen species mediate a decrease in nitric oxide (NO) bioavailability and endothelial dysfunction, with secondary oxidized and nitrated byproducts of these reactions contributing to the pathogenesis of numerous vascular diseases. While oxidized lipids and lipoproteins exacerbate inflammatory reactions in the vasculature, in stark contrast the nitration of polyunsaturated fatty acids and complex lipids yield electrophilic products that exhibit pluripotent anti-inflammatory signaling capabilities acting via both cGMP-dependent and -independent mechanisms. Herein we report that nitro-oleic acid (OA-NO(2)) treatment increases expression of endothelial nitric oxide synthase (eN...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935270</comments>
            <pubDate>Fri, 23 Oct 2009 00:00:00 +0100</pubDate>
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        <item>
            <title>Oxidants Induce Alternative Splicing of alpha-Synuclein: Implications for Parkinson's Disease.</title>
            <link>http://www.medworm.com/index.php?rid=2935269&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19857570%26dopt%3DAbstract</link>
            <description>Authors: Kalivendi SV, Yedlapudi D, Hillard CJ, Kalyanaraman B
    alpha-Synuclein (alpha-syn) is a presynaptic protein that is widely implicated in the pathophysiology of Parkinson's disease (PD). Emerging evidence indicates a strong correlation between alpha-syn aggregation and proteasomal dysfunction as one of the major pathways responsible for destruction of the dopamine neurons. Using Parkinsonism mimetics (MPP(+), rotenone) and related oxidants, we have identified an oxidant-induced alternative splicing of alpha-syn mRNA, generating a shorter isoform of alpha-syn with deleted exon-5 (112-syn). This spliced isoform has an altered localization and profoundly inhibits proteasomal function. The generation of 112-syn was suppressed by constitutively active MEK-1 and enhanced by inhibition...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
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            <pubDate>Fri, 23 Oct 2009 00:00:00 +0100</pubDate>
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        <item>
            <title>PKC-delta controls the fMLF-induced overproduction of superoxide by neutrophils.</title>
            <link>http://www.medworm.com/index.php?rid=2935277&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19854263%26dopt%3DAbstract</link>
            <description>Authors: Matron C, Chakravarti A, Allaeys I, Poubelle PE
    Anti-microbial defense by neutrophils implicates the production of reactive oxygen species. Neutrophil responses can be modulated by agonists like bacterial peptides and pro-inflammatory factors that modulate neutrophil activity and survival. We evaluated the production of superoxide anions (O(2)(-)) in response to fMLF by normal human neutrophils after 3 days of preincubation with GM-CSF+IL-4+TNF-alpha (survival medium). After 3 days of incubation with survival medium, long-lived neutrophils produced up to 6 times more O(2)(-) relative to control neutrophils in response to fMLF and WKYMVM. This augmented response to fMLF was preferentially linked to FPR, whereas the response to WKYMVM was dependent on FPRL- 1. Real time RT-PCR r...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935277</comments>
            <pubDate>Thu, 22 Oct 2009 00:00:00 +0100</pubDate>
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        <item>
            <title>Antioxidants Rescue Photoreceptors in Rd1 Mice: Relationship with Thiol Metabolism.</title>
            <link>http://www.medworm.com/index.php?rid=2935276&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19854264%26dopt%3DAbstract</link>
            <description>Authors: Miranda M, Arnal E, Ahuja S, Ekstr&amp;#xF6;m P, Bosch-Morell F, van Veen T, Romero FJ
    We have previously shown that the use of a combination of antioxidants delayed the degeneration process in rd1mouse retina. In an effort to understand the mechanism of action of these substances (zeaxanthin, lutein, alpha lipoic acid, glutathione and Lycium barbarum extract) the changes in the levels of several proteins and oxidative stress markers in the rd1 retina have been studied. The treatment increased glutathione peroxidase activity and glutathione levels, and decreased cystine concentrations in rd1 retinas. Considering all the results obtained from treated and untreated animals, a high correlation was present between glutathione concentration and glutathione peroxidase activity and, ther...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935276</comments>
            <pubDate>Thu, 22 Oct 2009 00:00:00 +0100</pubDate>
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        <item>
            <title>Puerarin Attenuates High Glucose and Diabetes-induced Vascular Smooth Muscle Cell Proliferation Via Blocking PKC-beta2/Rac-1-Dependent Signaling.</title>
            <link>http://www.medworm.com/index.php?rid=2935275&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19854265%26dopt%3DAbstract</link>
            <description>Authors: Zhu LH, Wang L, Wang D, Jiang H, Tang QZ, Yan L, Bian ZY, Wang XA, Li H
    Oxidative stress has been implicated in several steps leading to the development of diabetic vascular complications. The purpose of current study was to determine the efficacy and the possible mechanism of puerarin on high glucose (25 mM, HG)-induced proliferation of cultured rat vascular smooth muscle cells (VSMCs) and neointimal formation in a carotid arterial balloon injury model of obese Zucker rats. Our data demonstrated that puerarin significantly inhibited rat VSMCs proliferation as well as reactive oxygen species (ROS) generation and NAPDH oxidase activity induced by HG treatment. Further studies revealed that HG treatment resulted in phosphorylation and membrane translocation of PKCbeta2 as well a...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935275</comments>
            <pubDate>Thu, 22 Oct 2009 00:00:00 +0100</pubDate>
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        <item>
            <title>Consequences of long-term oral administration of the mitochondria-targeted antioxidant MitoQ to wild-type mice.</title>
            <link>http://www.medworm.com/index.php?rid=2935274&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19854266%26dopt%3DAbstract</link>
            <description>Authors: Rodriguez-Cuenca S, Cochem&amp;#xE9; HM, Logan A, Abakumova I, Prime TA, Rose C, Vidal-Puig A, Smith AC, Rubinsztein DC, Fearnley IM, Jones BA, Pope S, Heales SJ, Lam BY, Neogi SG, McFarlane I, James AM, Smith RA, Murphy MP
    The mitochondria-targeted quinone MitoQ protects mitochondria in animal studies of pathologies in vivo, and is being developed as a human therapy. However, it is unclear if the protective action of MitoQ is entirely due to its antioxidant properties, since long-term MitoQ administration may alter whole body metabolism and gene expression. To address this point, we administered high levels of MitoQ orally to wild-type C57BL/6 mice for up to 28 weeks, and investigated the effects on whole body physiology, metabolism, and gene expression, finding no measurable del...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935274</comments>
            <pubDate>Thu, 22 Oct 2009 00:00:00 +0100</pubDate>
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        <item>
            <title>In Vivo Oxidative Stress in Brain of Alzheimer Disease Transgenic Mice: Requirement for Methionine 35 in Amyloid Beta-Peptide Of APP.</title>
            <link>http://www.medworm.com/index.php?rid=2935273&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19854267%26dopt%3DAbstract</link>
            <description>Authors: Butterfield DA, Galvan V, Lange MB, Tang H, Sowell RA, Spilman P, Fombonne J, Gorostiza O, Zhang J, Sultana R, Bredesen DE
    Numerous studies have demonstrated oxidative damage in the central nervous system in subjects with Alzheimer disease and in animal models of this dementing disorder. In the current study, we show that transgenic mice modeling Alzheimer disease-PDAPP mice with Swedish and Indiana mutations in human amyloid precursor protein (APP)-develop oxidative damage in brain, including elevated levels of protein oxidation (indexed by protein carbonyls and 3-nitrotyrosine) and lipid peroxidation (indexed by protein-bound 4-hydroxy-2-nonenal). This oxidative damage requires the presence of a single methionine residue at position 35 of the amyloid beta-peptide (Abeta), si...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935273</comments>
            <pubDate>Thu, 22 Oct 2009 00:00:00 +0100</pubDate>
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            <title>Isoprostanes in Fetal and Neonatal Health and Disease.</title>
            <link>http://www.medworm.com/index.php?rid=2935272&amp;cid=s_35577_62_f&amp;fid=35577&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19854268%26dopt%3DAbstract</link>
            <description>Authors: Belik J, Luis GE, Vizcaino FP, Villamor E
    Isoprostanes are prostaglandin-like bioactive molecules generated via nonenzymatic peroxidation of lipid membrane-derived arachidonic acid by free radicals and reactive oxygen species. Their cognate receptors, biological actions, and signaling pathways are poorly understood. Aside from being sensitive and specific biomarkers of oxidative stress, E- and F-ring isoprostanes have important biological functions and likely mediate many of the disease-related pathological changes for which they are used as indicators. The biochemical pathways involved in isoprostane formation, their pathogenetic relevance to adult disease states, and their biological function are addressed. Developmentally, plasma and tissue content data show that isoprostan...</description>
            <author>Free Radical Biology and Medicine</author>
            <type>journals</type>
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            <pubDate>Thu, 22 Oct 2009 00:00:00 +0100</pubDate>
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