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        <title>Chemico-Biological Interactions 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 'Chemico-Biological Interactions' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Chemico-Biological+Interactions&t=Chemico-Biological+Interactions&s=Search&f=source]]></link>
        <lastBuildDate>Thu, 09 Feb 2012 16:56:39 +0100</lastBuildDate>
        <item>
            <title>The naphthol selective estrogen receptor modulator (SERM), LY2066948, is oxidized to an o-quinone analogous to the naphthol equine estrogen, equilenin.</title>
            <link>http://www.medworm.com/index.php?rid=5658659&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22290292%26dopt%3DAbstract</link>
            <description>Authors: Gherezghiher TB, Michalsen B, Chandrasena RE, Qin Z, Sohn J, Thatcher GR, Bolton JL
    Abstract
    o-Quinone forming estrogens and selective estrogen receptor modulators (SERMs) have been associated with carcinogenesis. LY2066948, a novel SERM in development by Eli Lilly for the treatment of uterine fibroids and myomas, has structural similarity to the equine estrogen equilenin present in hormone replacement formulations; both contain a naphthol group susceptible to oxidative metabolism to o-quinones. LY2066948 was synthesized and assayed for antiestrogenic activity, and in cell culture was confirmed to be a more potent antiestrogen than the prototypical SERM, 4-hydroxytamoxifen. Oxidation of LY2066948 with 2-iodoxybenzoic acid gave an o-quinone (t(1/2)=3.9±0.1h) which like 4-h...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658659</comments>
            <pubDate>Fri, 27 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>The dietary phytochemical 3,3'-diindolylmethane induces G2/M arrest and apoptosis in oral squamous cell carcinoma by modulating Akt-NF-κB, MAPK, and p53 signaling.</title>
            <link>http://www.medworm.com/index.php?rid=5658660&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22290291%26dopt%3DAbstract</link>
            <description>Authors: Weng JR, Bai LY, Chiu CF, Wang YC, Tsai MH
    Abstract
    In light of the growing incidence of oral cancer in Taiwan, this study is aimed at investigating the antitumor activity of 3,3'-diindolylmetha, an active metabolite of the phytochemical indole-3-carbinol (I3C), in oral squamous cell carcinoma (OSCC). DIM exhibited substantially higher antiproliferative potency than I3C in three OSCC cell lines with IC(50) values in SCC2095, SCC9, and SCC15 cells, respectively, of 22 versus 168μM, 25 versus 176μM, and 29versus 300μM. Flow cytometric analysis and Comet assay indicated that DIM suppressed the viability of SCC2095 cells by inducing apoptosis and G2/M arrest. Western blot analysis of various signaling markers revealed the ability of DIM to target pathways mediated by Akt, m...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658660</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5658660</guid>        </item>
        <item>
            <title>Amelioration of cyclophosphamide induced myelosuppression and oxidative stress by cinnamic acid.</title>
            <link>http://www.medworm.com/index.php?rid=5658662&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285266%26dopt%3DAbstract</link>
            <description>Authors: Patra K, Bose S, Sarkar S, Rakshit J, Jana S, Mukherjee A, Roy A, Mandal DP, Bhattacharjee S
    Abstract
    Cinnamic acid (C(9)H(8)O(2)), is a major constituent of the oriental Ayurvedic plant Cinnamomum cassia (Family: Lauraceae). This phenolic acid has been reported to possess various pharmacological properties of which its antioxidant activity is a prime one. Therefore it is rational to hypothesize that it may ameliorate myelosuppression and oxidative stress induced by cyclophosphamide, a widely used chemotherapeutic agent. Commercial cyclophosphamide, Endoxan, was administered intraperitoneally to Swiss albino mice (50mg/kg) pretreated with 15, 30 and 60mg/kg doses of cinnamic acid orally at alternate days for 15days. Cinnamic acid pre-treatment was found to reduce cyclophos...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658662</comments>
            <pubDate>Sat, 21 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5658662</guid>        </item>
        <item>
            <title>The anti-fibrotic effect of betulinic acid is mediated through the inhibition of NF-κB nuclear protein translocation.</title>
            <link>http://www.medworm.com/index.php?rid=5658661&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285267%26dopt%3DAbstract</link>
            <description>This study provides evidence that BA exerts a significant anti-fibrosis effect by modulating the TLR4/MyD88/NF-κB signaling pathway.
    PMID: 22285267 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658661</comments>
            <pubDate>Sat, 21 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5658661</guid>        </item>
        <item>
            <title>Hepatic expression of cytochrome P450 in type 2 diabetic Goto-Kakizaki rats.</title>
            <link>http://www.medworm.com/index.php?rid=5599195&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22244987%26dopt%3DAbstract</link>
            <description>Authors: Oh SJ, Choi JM, Yun KU, Oh JM, Kwak HC, Oh JG, Lee KS, Kim BH, Heo TH, Kim SK
    Abstract
    Although hepatic expression of cytochrome P450 (CYP) changes markedly in diabetes, the role of ketone bodies in the regulation of CYP in diabetes is controversial. The present study was performed to determine the expression and activity of CYP in non-obese type II diabetic Goto-Kakizaki (GK) rats with normal levels of ketone bodies. In the present study, basal serum glucose levels increased 1.95-fold in GK rats, but acetoacetate and β-hydroxybutyrate levels were not significantly different. Hepatic expression of CYP reductase and CYP3A2 was up-regulated in the GK rats, and consequently, activities of CYP reductase and midazolam 4-hydroxylase, mainly catalyzed by CYP3A2, increased. In co...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5599195</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5599195</guid>        </item>
        <item>
            <title>Differential protective effects of quercetin, resveratrol, rutin and epigallocatechin gallate against mitochondrial dysfunction induced by indomethacin in Caco-2 cells.</title>
            <link>http://www.medworm.com/index.php?rid=5577985&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22214982%26dopt%3DAbstract</link>
            <description>Authors: Carrasco-Pozo C, Mizgier ML, Speisky H, Gotteland M
    Abstract
    The beneficial effects of dietary polyphenols on health are due not only to their antioxidant properties but also to their antibacterial, anti-inflammatory and/or anti-tumoral activities. It has recently been proposed that protection of mitochondrial function (which is altered in several diseases such as Alzheimer, Parkinson, obesity and diabetes) by these compounds, may be important in explaining the beneficial effects of polyphenols on health. The aim of this study was to evaluate the protective effects of dietary polyphenols quercetin, rutin, resveratrol and epigallocatechin gallate against the alterations of mitochondrial function induced by indomethacin (INDO) in intestinal epithelial Caco-2 cells, and to ad...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577985</comments>
            <pubDate>Tue, 27 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577985</guid>        </item>
        <item>
            <title>Effects of phthalates on 3β-hydroxysteroid dehydrogenase and 17β-hydroxysteroid dehydrogenase 3 activities in human and rat testes.</title>
            <link>http://www.medworm.com/index.php?rid=5577984&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22214983%26dopt%3DAbstract</link>
            <description>Authors: Yuan K, Zhao B, Li XW, Hu GX, Su Y, Chu Y, Akingbemi BT, Lian QQ, Ge RS
    Abstract
    The 3β-hydroxysteroid dehydrogenase (3β-HSD) and 17β-hydroxysteroid dehydrogenase 3 (17β-HSD3) are involved in the reactions that culminate in androgen biosynthesis in Leydig cells. Human and rat testis microsomes were used to investigate the inhibitory potencies on 3β-HSD and 17β-HSD3 activities of 14 different phthalates with various carbon numbers in the ethanol moiety. The results demonstrated that the half-maximal inhibitory concentrations (IC(50)s) of dipropyl (DPrP), dibutyl (DBP), dipentyl (DPP), bis(2-butoxyethyl) (BBOP) and dicyclohexyl (DCHP) phthalate were 123.0, 24.1, 25.5, 50.3 and 25.5μM for human 3β-HSD activity, and 62.7, 30.3, 33.8, 82.6 and 24.7μM for rat 3β-HSD ac...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577984</comments>
            <pubDate>Tue, 27 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577984</guid>        </item>
        <item>
            <title>Additional analysis of dendrochemical data of Fallon, Nevada.</title>
            <link>http://www.medworm.com/index.php?rid=5577983&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22227064%26dopt%3DAbstract</link>
            <description>Authors: Sheppard PR, Helsel DR, Speakman RJ, Ridenour G, Witten ML
    Abstract
    Previously reported dendrochemical data showed temporal variability in concentration of tungsten (W) and cobalt (Co) in tree rings of Fallon, Nevada, US. Criticism of this work questioned the use of the Mann-Whitney test for determining change in element concentrations. Here, we demonstrate that Mann-Whitney is appropriate for comparing background element concentrations to possibly elevated concentrations in environmental media. Given that Mann-Whitney tests for differences in shapes of distributions, inter-tree variability (e.g., &quot;coefficient of median variation&quot;) was calculated for each measured element across trees within subsites and time periods. For W and Co, the metals of highest interest in Fallon,...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577983</comments>
            <pubDate>Tue, 27 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577983</guid>        </item>
        <item>
            <title>Differential sensitivity of plasma carboxylesterase-null mice to parathion, chlorpyrifos and chlorpyrifos oxon, but not to diazinon, dichlorvos, diisopropylfluorophosphate, cresyl saligenin phosphate, cyclosarin thiocholine, tabun thiocholine, and carbofuran.</title>
            <link>http://www.medworm.com/index.php?rid=5577986&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22209767%26dopt%3DAbstract</link>
            <description>Authors: Duysen EG, Cashman JR, Schopfer LM, Nachon F, Masson P, Lockridge O
    Abstract
    Mouse blood contains four esterases that detoxify organophosphorus compounds: carboxylesterase, butyrylcholinesterase, acetylcholinesterase, and paraoxonase-1. In contrast human blood contains the latter three enzymes but not carboxylesterase. Organophosphorus compound toxicity is due to inhibition of acetylcholinesterase. Symptoms of intoxication appear after approximately 50% of the acetylcholinesterase is inhibited. However, complete inhibition of carboxylesterase and butyrylcholinesterase has no known effect on an animal's well being. Paraoxonase hydrolyzes organophosphorus compounds and is not inhibited by them. Our goal was to determine the effect of plasma carboxylesterase deficiency on res...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577986</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577986</guid>        </item>
        <item>
            <title>Nanocapsulated curcumin: Oral chemopreventive formulation against diethylnitrosamine induced hepatocellular carcinoma in rat.</title>
            <link>http://www.medworm.com/index.php?rid=5548917&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22197969%26dopt%3DAbstract</link>
            <description>Authors: Ghosh D, Choudhury ST, Ghosh S, Mandal AK, Sarkar S, Ghosh A, Saha KD, Das N
    Abstract
    Toxic outcome of chemical therapeutics as well as multidrug resistance are two serious phenomena for their inacceptance in cancer chemotherapy. Antioxidants like curcumin (Cur) have gained immense importance for their excellent anticarcinogenic activities and minimum toxic manifestations in biological system. However, Cur is lipophilic and thus following oral administration hardly appears in blood indicating its potential therapeutic challenge in cancer therapy. Nanocapsulated Cur has been used as a drug delivery vector to focus the effectiveness of these vesicles against hepatocellular carcinoma. The theme of work was to evaluate effectiveness in oral route of polylactide co-glycolide (P...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548917</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5548917</guid>        </item>
        <item>
            <title>Quercetin modulates Nrf2 and glutathione-related defenses in HepG2 cells: Involvement of p38.</title>
            <link>http://www.medworm.com/index.php?rid=5548916&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22197970%26dopt%3DAbstract</link>
            <description>In conclusion, p38-MAPK is involved in the mechanisms of the cell response to quercetin through the modulation of Nrf2 and glutathione-related enzymes in HepG2 cells.
    PMID: 22197970 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548916</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5548916</guid>        </item>
        <item>
            <title>Tungsten toxicity.</title>
            <link>http://www.medworm.com/index.php?rid=5548919&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22182474%26dopt%3DAbstract</link>
            <description>Authors: Witten ML, Sheppard PR, Witten BL
    Abstract
    There is emerging evidence that tungsten has toxic health effects. We summarize the recent tungsten toxicity research in this short review. Tungsten is widely used in many commercial and military applications because it has the second highest melting temperature of any element. Consequently, it is important to elucidate the potential health effects of tungsten.
    PMID: 22182474 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548919</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5548919</guid>        </item>
        <item>
            <title>Antiproliferative and iron chelating efficiency of the new bis-8-hydroxyquinoline benzylamine chelator S1 in hepatocyte cultures.</title>
            <link>http://www.medworm.com/index.php?rid=5548918&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22197641%26dopt%3DAbstract</link>
            <description>Authors: Lescoat G, Léonce S, Pierré A, Gouffier L, Gaboriau F
    Abstract
    If a new generation of iron chelators specifically devoted for cancer chemotherapy emerged these last years, any of them has not yet been approved at this time. Accordingly, there is a need to optimize new chelating molecules for iron chelation therapy and cancer treatment. So, the objective of the present investigation was to characterize the antiproliferative activity and the iron chelating capacity of the iron chelator S1 [bis-N-(8-hydroxyquinoline-5-ylmethyl)benzylamine]. Its effects were compared to O-trensox which binds ferric iron with a very high affinity (pFe(3+)=29.5). For this purpose, primary rat hepatocyte stimulated by EGF and human hepatoma HepaRG cell cultures were used. In these models, the a...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548918</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5548918</guid>        </item>
        <item>
            <title>Induction of cytochrome P450 3A by Shexiang Baoxin Pill and its main components.</title>
            <link>http://www.medworm.com/index.php?rid=5548921&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22178124%26dopt%3DAbstract</link>
            <description>Authors: Jiang B, Cai F, Gao S, Meng L, Liang F, Dai X, Xu W, Chen W
    Abstract
    The expression of cytochrome P450 is regulated by both endogenous factors and xenobiotics including chemical drugs and natural medicines. Induction on cytochrome P450 can reduce the therapeutic efficacy from drugs inactivated by this enzyme system, but may increase the efficacy or lead to intoxication for prodrugs. Shexiang Baoxin Pill (SBP) is a traditional Chinese medicine widely used for the treatment of angina pectoris and myocardial infarction in China and other oriental countries. To assess the potential of SBP to alter the activity and expression of cytochrome P450 3A (CYP3A) extensively involved in drug metabolism, we investigated the enzyme-inducing effects of SBP in HepG2 cells and in rats. The ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548921</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5548921</guid>        </item>
        <item>
            <title>The inhibitory effects of perfluoroalkyl substances on human and rat 11β-hydroxysteroid dehydrogenase 1.</title>
            <link>http://www.medworm.com/index.php?rid=5548922&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22178014%26dopt%3DAbstract</link>
            <description>In conclusion, the present study shows that PFOS and PFOA are the inhibitors of 11βHSD1.
    PMID: 22178014 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548922</comments>
            <pubDate>Thu, 08 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5548922</guid>        </item>
        <item>
            <title>Gastroprotective activity and mechanism of novel dichlorido-zinc(II)-4-(2-(5-methoxybenzylideneamino)ethyl)piperazin-1-iumphenolate complex on ethanol-induced gastric ulceration.</title>
            <link>http://www.medworm.com/index.php?rid=5548920&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22178775%26dopt%3DAbstract</link>
            <description>Authors: Salga MS, Ali HM, Abdulla MA, Abdelwahab SI
    Abstract
    Zinc complexes were reported to have anti-ulcer activity and used as drug for the treatment of gastrointestinal disorders. A novel compound dichlorido-zinc(II)-4-(2-(5-methoxybenzylidene amino)ethyl)piperazin-1-iumphenolate (ZnHMS) was synthesized, characterized and evaluated for its gastroprotective activity against ethanol-induced ulcer in rats. Gross and microscopic lesions, histochemical staining of glycogen storage, biochemical and immunological parameters were taken into consideration. Oral administration of ZnHMS (30 and 60mg/kg; 14days) dose-dependently inhibited gastric lesions. It significantly increased the mucus content and total acidity compared to the control group (P&amp;lt;0.01). Serum levels of aspartate (AS...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548920</comments>
            <pubDate>Thu, 08 Dec 2011 05:00:00 +0100</pubDate>
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        <item>
            <title>Induction of apoptosis and cell cycle arrest by Bis (2-ethylhexyl) phthalate produced by marine Bacillus pumilus MB 40.</title>
            <link>http://www.medworm.com/index.php?rid=5548923&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155658%26dopt%3DAbstract</link>
            <description>Authors: Moushumi Priya A, Jayachandran S
    Abstract
    Marine microorganisms represent a potential source for the production of biomedically useful compounds active against inflammation, cancer, diabetes, etc. Marine Bacillus pumilus MB 40 (GenBank accession no. HQ705771) isolated from deep sea water column (1000m depth) near Andaman and Nicobar islands produced a bioactive lead, Bis (2-ethylhexyl) phthalate (BEHP) with a molecular formula of C(6)H(4)(CO(2)C(8)H(17))(2) and a molecular ion at m/z 391 (M(+)). Anti proliferative effect of the isolated compound was examined by MTT assay in human erythroleukemic K562 cells and the IC(50) of BEHP was found to be 21μM. BEHP was able to induce apoptosis involving caspases pathway, besides regulating mitochondrial enzymes. Further, western bl...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548923</comments>
            <pubDate>Sat, 03 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5548923</guid>        </item>
        <item>
            <title>Metabolic effects of silibinin in the rat liver.</title>
            <link>http://www.medworm.com/index.php?rid=5548924&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22137898%26dopt%3DAbstract</link>
            <description>Authors: Colturato CP, Constantin RP, Maeda AS, Constantin RP, Yamamoto NS, Bracht A, Ishii-Iwamoto EL, Constantin J
    Abstract
    The flavonolignan silibinin, which is a mixture of two diastereoisomers, silybin A and silybin B, is a component of the extract obtained from the fruit and seeds of the variegated milk thistle (Silybum marianum (L.) Gaertn. (Asteraceae)), known as silymarin. Among the therapeutic properties credited to silibinin, its antihyperglycaemic action has been extensively explored. Silibinin is structurally related to the flavonoids quercetin and fisetin, which have been previously demonstrated to be very active on liver metabolic processes related to glycaemic regulation. The aim of the present work was to investigate the effects of silibinin on metabolic pathways r...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548924</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5548924</guid>        </item>
        <item>
            <title>Effect of zinc supplementation on glutathione peroxidase activity and selenium concentration in the serum, liver and kidney of rats chronically exposed to cadmium.</title>
            <link>http://www.medworm.com/index.php?rid=5474462&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22100499%26dopt%3DAbstract</link>
            <description>Authors: Galażyn-Sidorczuk M, Brzóska MM, Rogalska J, Roszczenko A, Jurczuk M
    Abstract
    It was investigated whether the ability of zinc (Zn) to prevent cadmium (Cd)-induced lipid peroxidation may be connected with its impact on glutathione peroxidase (GPx) activity and selenium (Se) concentration. GPx and Se were determined in the serum, liver and kidney of the rats that received Cd (5 or 50mg/L) or/and Zn (30mg/L) in drinking water for 6 months in whose the protective Zn impact was noted (Rogalska J, Brzóska MM, Roszczenko A, Moniuszko-Jakoniuk J. Enhanced zinc consumption prevents cadmium-induced alterations in lipid metabolism in male rats. Chem Biol Interact 2009;177:142-52). Moreover, dependences between these parameters, and indices of lipid peroxidation (F(2)-isoprostane, ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5474462</comments>
            <pubDate>Thu, 17 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5474462</guid>        </item>
        <item>
            <title>Suppression of TNBS-induced colitis in rats by 4-methylesculetin, a natural coumarin: Comparison with prednisolone and sulphasalazine.</title>
            <link>http://www.medworm.com/index.php?rid=5474458&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22119283%26dopt%3DAbstract</link>
            <description>In conclusion, 4-methylesculetin showed similar efficacy to that obtained with either prednisolone or sulphasalazine, both in the acute phase of colitis as well as following a curative protocol. The intestinal anti-inflammatory activity by 4-methylesculetin is likely related to its ability in reduce colonic oxidative stress and inhibit pro-inflammatory cytokine production.
    PMID: 22119283 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5474458</comments>
            <pubDate>Wed, 16 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5474458</guid>        </item>
        <item>
            <title>Epigallocatechin gallate suppresses peritoneal fibrosis in mice.</title>
            <link>http://www.medworm.com/index.php?rid=5474460&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22101032%26dopt%3DAbstract</link>
            <description>Authors: Kitamura M, Nishino T, Obata Y, Furusu A, Hishikawa Y, Koji T, Kohno S
    Abstract
    Long-term peritoneal dialysis (PD) leads to histological changes in the peritoneal membrane. Angiogenesis and inflammation caused by glucose degradation products (GDPs) play crucial roles in peritoneal fibrosis. One such GDP is methylglyoxal (MGO), which enhances the formation of advanced glycation end products (AGEs). AGEs bind to their receptor (RAGE) and activate nuclear factor-κB (NF-κB), which is a key regulator of angiogenesis and inflammation. Recent studies have indicated that (-)-epigallocatechin gallate (EGCG), a tea polyphenol, inhibits angiogenesis and inflammation. Here, we examined whether EGCG suppresses peritoneal fibrosis in mice. Based on preliminary examination, 2mL of 40mM...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5474460</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5474460</guid>        </item>
        <item>
            <title>Photodynamic anticancer activities of water-soluble C(60) derivatives and their biological consequences in a HeLa cell line.</title>
            <link>http://www.medworm.com/index.php?rid=5474459&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22108244%26dopt%3DAbstract</link>
            <description>Authors: Hu Z, Zhang C, Huang Y, Sun S, Guan W, Yao Y
    Abstract
    Photodynamic therapy is an emerging, externally activatable, treatment modality for various diseases, especially for cancer therapy. The photodynamic activities of tumor targeting water-soluble C(60) derivatives (WSFD) were evaluated on HeLa cells. To overcome the poor solubility, biocompatibility and selectivity of C(60), we modified C(60) with l-phenylalanine, folic acid and l-arginine. Consistent with their photodynamic abilities, WSFD generated the reactive oxygen species after irradiation both in water and in vitro. No dark cytotoxicity was observed using 5μg/mL WSFD during long incubation time. Furthermore, the uptake of WSFD into HeLa cells was much more than normal cells, which indicated the WSFD had selectivit...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5474459</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5474459</guid>        </item>
        <item>
            <title>Inheritable stimulatory effects of caffeine on steroidogenic acute regulatory protein expression and cortisol production in human adrenocortical cells.</title>
            <link>http://www.medworm.com/index.php?rid=5474461&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22100783%26dopt%3DAbstract</link>
            <description>This study was designed to investigate the direct effects and inheritable epigenetic mechanisms of caffeine on cortisol production and StAR expression in human adrenocortical cells. The human adrenocortical cell line NCI-H295A was cultured with 0.4-40μM caffeine. There was a significant increase of the cortisol production in cells. In both acutely and chronically caffeine-treated cell groups, mRNA and protein expressions of StAR were stimulated in a dose-dependent manner. DNA methylation detection via bisulfite-sequencing PCR (BSP) uncovered a single site CpG demethylation at nt -682 within the StAR promoter region. Then we investigated how long the increased StAR expression and the single CpG demethylation could last. The caffeine was withdrawn after 48h of treatment and then the cells w...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5474461</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5474461</guid>        </item>
        <item>
            <title>The enzymatic activity of human aldehyde dehydrogenases 1A2 and 2 (ALDH1A2 and ALDH2) is detected by Aldefluor, inhibited by diethylaminobenzaldehyde and has significant effects on cell proliferation and drug resistance.</title>
            <link>http://www.medworm.com/index.php?rid=5419095&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22079344%26dopt%3DAbstract</link>
            <description>In this study, we explore the effects of human ALDH isoenzymes, ALDH1A2 and ALDH2, on drug resistance and proliferation, and the specificity of DEAB as an inhibitor. We also screened for the expression of 19 ALDH isoenzymes in K562 cells using TaqMan Low Density Array (TLDA). We used lentiviral vectors containing the full cDNA length of either ALDH2 or ALDH1A2 to over express the enzymes in K562 leukemia and H1299 lung cancer cell lines. Successful expression was measured by activity assay, Western blot, RT-PCR, and Aldefluor assay. Both cell lines, with either ALDH1A2 or ALDH2, exhibited higher cell proliferation rates, higher clonal efficiency, and increased drug resistance to 4-hydroperoxycyclophosphamide and doxorubicin. In order to study the specificity of known ALDH activity inhibito...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419095</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419095</guid>        </item>
        <item>
            <title>Ginsenoside Rg2 induces orphan nuclear receptor SHP gene expression and inactivates GSK3β via AMP-activated protein kinase to inhibit hepatic glucose production in HepG2 cells.</title>
            <link>http://www.medworm.com/index.php?rid=5419098&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22062806%26dopt%3DAbstract</link>
            <description>In conclusion, our results propose that ginsenoside Rg2 suppresses the hepatic glucose production via AMPK-induced phosphorylation of GSK3β and induction of SHP gene expression. Further studies are warranted to elucidate a therapeutic potential of Rg2 for type 2 diabetic patients.
    PMID: 22062806 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419098</comments>
            <pubDate>Mon, 31 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419098</guid>        </item>
        <item>
            <title>A novel fused 1,2,4-triazine aryl derivative as antioxidant and nonselective antagonist of adenosine A(2A) receptors in ethanol-activated liver stellate cells.</title>
            <link>http://www.medworm.com/index.php?rid=5419097&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22063920%26dopt%3DAbstract</link>
            <description>Authors: Szuster-Ciesielska A, Sztanke K, Kandefer-Szerszeń M
    Abstract
    It has been detected that hepatic adenosine A(2A) receptors play an active role in the pathogenesis of hepatic fibrosis and suggest a novel therapeutic target in the treatment and prevention of hepatic cirrhosis. In this paper we examined if our new triazine derivative (IMT) can inhibit ethanol-induced activation of HSCs measured as increased α-SMA, collagen synthesis and enhanced oxidative stress in rat liver stellate cells. We also investigated its influence on cytokines (TGF-β, TNF-α) synthesis, MMP-2 and TIMP-1 production and ethanol-induced intracellular signal transduction. Moreover, with using of known adenosine A(2A) receptor agonist (CGS 21680), and antagonist (SCH 58261) we examined if this triazin...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419097</comments>
            <pubDate>Sat, 29 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419097</guid>        </item>
        <item>
            <title>Effect of vicanicin and protolichesterinic acid on human prostate cancer cells: Role of Hsp70 protein.</title>
            <link>http://www.medworm.com/index.php?rid=5419096&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22063921%26dopt%3DAbstract</link>
            <description>Authors: Russo A, Caggia S, Piovano M, Garbarino J, Cardile V
    Abstract
    With the aim of identifying novel agents with antigrowth and pro-apoptotic activity on prostate cancer cells, in the present study, we evaluated the effect of five lichen secondary metabolites the depsides atranorin (1), diffrattaic (2) and divaricatic (3) acids, the depsidone vicanicin (4) and the protolichesterinic acid (5) on cell growth in androgen-sensitive (LNCaP) and androgen-insensitive (DU-145) human prostate cancer cells. The cell viability was measured using MTT assay. LDH release, a marker of membrane breakdown, was also measured. For the detection of apoptosis, the evaluation of DNA fragmentation (COMET assay) and caspase-3 activity assay were employed. The expression of Bcl-2, Bax, TRAIL, COX-2, NO...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419096</comments>
            <pubDate>Sat, 29 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419096</guid>        </item>
        <item>
            <title>Ameliorative effect of diosmin, a citrus flavonoid against streptozotocin-nicotinamide generated oxidative stress induced diabetic rats.</title>
            <link>http://www.medworm.com/index.php?rid=5419099&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22056647%26dopt%3DAbstract</link>
            <description>Authors: Srinivasan S, Pari L
    Abstract
    Oxidative stress has been suggested as a contributory factor in development and complication of diabetes. The aim of the study was to evaluate the effect of diosmin (DS) in oxidative stress in streptozotocin-nicotinamide (STZ-NA)-induced diabetic rats by measuring the lipid peroxidation (LPO) as well as the ameliorative properties. Experimental diabetes was induced by a single intraperitoneal (i.p) injection of STZ (45mg/kg body weight (b.w.)) dissolved in 0.1mol/L citrate buffer (pH 4.5), 15min after the i.p administration of NA (110mg/kg b.w.). Diabetic rats exhibited increased plasma glucose with significant decrease in plasma insulin levels. The activities of antioxidant enzymes superoxide dismutase (SOD), catalase (CAT), glutathione perox...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419099</comments>
            <pubDate>Fri, 28 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419099</guid>        </item>
        <item>
            <title>Antimetastatic effect and mechanism of ovatodiolide in MDA-MB-231 human breast cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=5360990&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22033475%26dopt%3DAbstract</link>
            <description>In this study, we first noted that ovatodiolide inhibited MDA-MB-231 cell migration and invasion by wound-healing assay and Boyden chamber assay. Western blot, gelatin zymography and reversed transcription-PCR analysis showed that ovatodiolide significantly and selectively suppressed the expression, activation, and mRNA of matrix metalloproteinase-9 (MMP-9) in a concentration-dependent manner. Ovatodiolide significantly decreased the nuclear level of nuclear factor kappaB (NF-κB), increased inhibitor of kappaBα (IκBα) through preventing phosphorylation of upstream signal IκB kinase (IKK). Pretreatment with a specific NF-κB inhibitor (PDTC) and an IκB protease inhibitor (TPCK) also reduced MMP-9 activity, cell migration and cell invasion. Moreover, ovatodiolide can suppress activatio...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5360990</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5360990</guid>        </item>
        <item>
            <title>Characterization of inhibitory effects of perfluorooctane sulfonate on human hepatic cytochrome P450 isoenzymes: Focusing on CYP2A6.</title>
            <link>http://www.medworm.com/index.php?rid=5296313&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21964418%26dopt%3DAbstract</link>
            <description>Authors: Narimatsu S, Nakanishi R, Hanioka N, Saito K, Kataoka H
    Abstract
    Perfluorooctane sulfonate (PFOS) is a chemically stable compound extensively used as oil and water repellent, surface active agents in our daily life. Accumulative research evidence gradually appears the toxicity of PFOS against mammals, but the whole figure remains to be elucidated. The present study was conducted to know the effects of PFOS on human hepatic drug metabolizing-type cytochrome P450 (CYP) isoenzymes such as CYP1A2 (7-ethoxyresorufin as a substrate), CYP2A6 (coumarin), CYP2B6 (7-ethoxy-4-trifluoromethylcoumarin), CYP2C8 (paclitaxel), CYP2C9 (diclofenac), CYP2C19 (S-mephenytoin), CYP2D6 (bufuralol), CYP2E1 (chlorzoxazone) and CYP3A4 (testosterone) in human livers employing their typical substrate...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5296313</comments>
            <pubDate>Mon, 19 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5296313</guid>        </item>
        <item>
            <title>Anthraquinone compounds from Morinda officinalis inhibit osteoclastic bone resorption in vitro.</title>
            <link>http://www.medworm.com/index.php?rid=5277667&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21945525%26dopt%3DAbstract</link>
            <description>Authors: Bao L, Qin L, Liu L, Wu Y, Han T, Xue L, Zhang Q
    Abstract
    The root of Morinda officinalis has been claimed to have a protective effect against bone loss in sciatic neurectomized and ovariectomized osteoporotic rats, and this protective effect is supposed to be attributed to anthraquinone compounds in the plant. In the present study, we investigated the effects of three anthraquinones isolated from M. officinalis, including 1, 3, 8-trihydroxy-2-methoxy-anthraquinone (1), 2-hydroxy-1-methoxy-anthraquinone (2) and rubiadin (3) on bone resorption activity in vitro and the mechanism on osteoclasts derived from rat bone marrow cells. Compound 1, 2 and 3 decreased the formation of bone resorption pits, the number of multinucleated osteoclasts, and the activity of tartrate resista...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5277667</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5277667</guid>        </item>
        <item>
            <title>Impact of genetic polymorphisms of cytochrome P450 2 C (CYP2C) enzymes on the drug metabolism and design of antidiabetics.</title>
            <link>http://www.medworm.com/index.php?rid=5259685&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21939641%26dopt%3DAbstract</link>
            <description>Authors: Sun H, Scott DO
    Abstract
    CYP2C enzymes are responsible for the oxidative metabolism of a diverse number of drugs for the treatment of type 2 diabetes mellitus, a severe metabolic disorder with high prevalence. Various clinical studies found the close association between CYP2C polymorphisms and altered pharmacokinetics, toxicological profiles, and drug-drug interactions of antidiabetic drugs. In this brief review, we discussed the impact of CYP2C polymorphisms on the metabolic fate of small-molecule antidiabetics including sulfonylureas, meglitinides, thiazolidinediones, gliptins, and gliflozins, with the key drug-protein molecular interactions highlighted.
    PMID: 21939641 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5259685</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5259685</guid>        </item>
        <item>
            <title>Reactivation of organophosphate-inhibited human acetylcholinesterase by isonitrosoacetone (MINA): A kinetic analysis.</title>
            <link>http://www.medworm.com/index.php?rid=5246323&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21930118%26dopt%3DAbstract</link>
            <description>Authors: Worek F, Thiermann H
    Abstract
    Treatment of poisoning by highly toxic organophosphorus compounds (OP) with atropine and an acetylcholinesterase (AChE) reactivator (oxime) is of limited effectiveness in case of different nerve agents and pesticides. One challenge is the reactivation of OP-inhibited brain AChE which shows inadequate success with charged pyridinium oximes. Recent studies with high doses of the tertiary oxime isonitrosoacetone (MINA) indicated a beneficial effect on central and peripheral AChE and on survival in nerve agent poisoned guinea pigs. Now, an in vitro study was performed to determine the reactivation kinetics of MINA with tabun-, sarin-, cyclosarin-, VX- and paraoxon-inhibited human AChE. MINA showed an exceptionally low affinity to inhibited AChE bu...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5246323</comments>
            <pubDate>Fri, 09 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5246323</guid>        </item>
        <item>
            <title>Enhanced glutathione depletion, protein adduct formation, and cytotoxicity following exposure to 4-hydroxy-2-nonenal (HNE) in cells expressing human multidrug resistance protein-1 (MRP1) together with human glutathione S-transferase-M1 (GSTM1).</title>
            <link>http://www.medworm.com/index.php?rid=5246324&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21925487%26dopt%3DAbstract</link>
            <description>Authors: Rudd LP, Kabler SL, Morrow CS, Townsend AJ
    Abstract
    4-Hydroxy-2-nonenal (HNE) is one of the most reactive products of lipid peroxidation and has both cytotoxic and genotoxic effects in cells. Several enzymatic pathways have been reported to detoxify HNE, including conjugation by glutathione-S-transferases (GSTs). Removal of the resulting HNE-glutathione conjugate (HNE-SG) by an efflux transporter may be required for complete detoxification. We investigated the effect of expression of GSTM1 and/or the ABC efflux transporter protein, multidrug-resistance protein-1 (MRP1), on HNE-induced cellular toxicity. Stably transfected MCF7 cell lines were used to examine the effect of GSTM1 and/or MRP1 expression on HNE-induced cytotoxicity, GSH depletion, and HNE-protein adduct format...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5246324</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5246324</guid>        </item>
        <item>
            <title>25-OCH(3)-PPD induces the apoptosis of activated t-HSC/Cl-6 cells via c-FLIP-mediated NF-κB activation.</title>
            <link>http://www.medworm.com/index.php?rid=5246325&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21924252%26dopt%3DAbstract</link>
            <description>In this study, we evaluated the effects of 25-OCH(3)-PPD on apoptosis of activated t-HSC/Cl-6 cells induced by tumor necrosis factor-α (TNF-α). The inhibitory effects of eleven compounds isolated from Panax ginseng and P. notoginseng were detected in activated t-HSC/Cl-6 cells. 25-OCH(3)-PPD produced a significant inhibitory effect on activated t-HSC/Cl-6 cells. However, 25-OCH(3)-PPD showed almost no effect on the cell viability of Chang liver cells, a type of normal human hepatic cell line. Therefore, we aimed to determine the anti-fibrotic potential of 25-OCH(3)-PPD and to characterize the signal transduction pathways involved in activated HSCs. 25-OCH(3)-PPD decreased the fibrosis markers, including α-smooth muscle actin (α-SMA), transforming growth factor β-1 (TGF-β1) and tissue...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5246325</comments>
            <pubDate>Wed, 07 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5246325</guid>        </item>
        <item>
            <title>Hypolipidemic effect of Smallanthus sonchifolius (yacon) roots on diabetic rats: Biochemical approach.</title>
            <link>http://www.medworm.com/index.php?rid=5218681&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21907189%26dopt%3DAbstract</link>
            <description>In conclusion, yacon root flour is a natural product rich in FOS that could be well positioned as a nutraceutical product since the present results demonstrate its beneficial effects on diabetes-associated hyperlipidemia.
    PMID: 21907189 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218681</comments>
            <pubDate>Sun, 28 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218681</guid>        </item>
        <item>
            <title>Ginsenoside metabolite compound K differentially antagonizing tumor necrosis factor-α-induced monocyte-endothelial trafficking.</title>
            <link>http://www.medworm.com/index.php?rid=5218683&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21875580%26dopt%3DAbstract</link>
            <description>This study examined the potential of compound K to inhibit the pro-inflammatory cytokine TNF-α induction of monocyte adhesion onto TNF-α-activated human umbilical vein endothelial cells (HUVEC). HUVEC were cultured with 10ng/ml TNF-α with individual ginsenosides of Rb1, Rc, Re, Rh1 and compound K (CK). Ginsenosides at doses of ⩽50μM did not show any cytotoxicity. TNF-α induced THP-1 monocyte adhesion to HUVEC, and such induction was attenuated by Rh1 and CK. Consistently, CK suppressed TNF-α-induced expression of HUVEC adhesion molecules of VCAM-1, ICAM-1 and E-selectin, and also Rh1 showed a substantial inhibition. Rh1 and CK dampened induction of counter-receptors, α4/β1 integrin VLA-4 and αL/β2 integrin LFA-1 in TNF-α-treated THP-1 cells. Additionally, CK diminished THP-1 s...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218683</comments>
            <pubDate>Mon, 22 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218683</guid>        </item>
        <item>
            <title>Catabolism of 4-hydroxy-2-trans-nonenal by THP1 monocytes/macrophages and inactivation of carboxylesterases by this lipid electrophile.</title>
            <link>http://www.medworm.com/index.php?rid=5218682&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21878322%26dopt%3DAbstract</link>
            <description>Authors: Borazjani A, Edelmann MJ, Hardin KL, Herring KL, Allen Crow J, Ross MK
    Abstract
    Oxidative stress in cells and tissues leads to the formation of an assortment of lipid electrophiles, such as the quantitatively important 4-hydroxy-2-trans-nonenal (HNE). Although this cytotoxic aldehyde is atherogenic the mechanisms involved are unclear. We hypothesize that elevated HNE levels can directly inactivate esterase and lipase activities in macrophages via protein adduction, thus generating a biochemical lesion that accelerates foam cell formation and subsequent atherosclerosis. In the present study we examined the effects of HNE treatment on esterase and lipase activities in human THP1 monocytes/macrophages at various physiological scales (i.e., pure recombinant enzymes, cell lysat...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218682</comments>
            <pubDate>Mon, 22 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218682</guid>        </item>
        <item>
            <title>Cell cycle arrest and apoptosis induced by methyl 3,5-dicaffeoyl quinate in human colon cancer cells: Involvement of the PI3K/Akt and MAP kinase pathways.</title>
            <link>http://www.medworm.com/index.php?rid=5175043&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21872580%26dopt%3DAbstract</link>
            <description>In this study, MDQ inhibited proliferation and induced apoptosis in HT-29 cells in a dose-dependent manner as detected by 1-(4,5-dimethylthiazol-2-yl)-3,5-diphenylformazan (MTT), trypan blue exclusion, and flow cytometric assays. Western blot analysis showed that apoptosis was dependent on caspase-3 activity. PARP cleavage and the cytosolic release of cytochrome c from mitochondria increased significantly. In addition, these events were accompanied by a collapse in the mitochondrial membrane potential and a decreased Bcl-2/Bax ratio. Furthermore, the MDQ-induced G(0)/G(1) arrest was correlated with an increase in p27 and a decrease in cyclin D1 and p53. MDQ also inhibited the phosphorylation of PI3K/Akt and ERK; significantly reduced NF-κB; and in general displayed a significant anti-prol...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175043</comments>
            <pubDate>Sun, 21 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175043</guid>        </item>
        <item>
            <title>Bisphenol-A suppresses neurite extension due to inhibition of phosphorylation of mitogen-activated protein kinase in PC12 cells.</title>
            <link>http://www.medworm.com/index.php?rid=5175044&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21871873%26dopt%3DAbstract</link>
            <description>In this study, the morphological changes in nerve growth factor (NFG)-induced differentiation caused by bisphenol-A were confirmed using a PC12 cell system. When a low concentration of bisphenol-A was added to medium containing NGF, it inhibited neurite extension. In addition, to clarify whether bisphenol-A affects the early and late stages of the NGF-signaling pathway in cell differentiation, changes of phosphorylation of MAP kinases and cAMP-response element binding protein (CREB) in PC12 cells treated with and without BPA in medium containing NGF were investigated using western blot analysis. As results, bisphenol-A significantly inhibited phosphorylation of CREB and ERK1/2 MAPK.
    PMID: 21871873 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175044</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175044</guid>        </item>
        <item>
            <title>Propiconazole increases reactive oxygen species levels in mouse hepatic cells in culture and in mouse liver by a cytochrome P450 enzyme mediated process.</title>
            <link>http://www.medworm.com/index.php?rid=5175048&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864511%26dopt%3DAbstract</link>
            <description>Authors: Nesnow S, Grindstaff R, Lambert G, Padgett WT, Bruno M, Ge Y, Chen PJ, Wood CE, Murphy L
    Abstract
    Propiconazole induces hepatocellular carcinomas and hepatocellular adenomas in mice and promotes liver tumors in rats. Transcriptional, proteomic, metabolomic and biochemical studies of hepatic tissues from mice treated with propiconazole under the conditions of the chronic bioassay indicated that propiconazole induced oxidative stress. Here we sought to identify the source of the reactive oxygen species (ROS) induced by propiconazole using both AML12 immortalized mouse hepatocytes in culture and liver tissues from mice. We also sought to further characterize the nature and effects of ROS formation induced by propiconazole treatment in mouse liver. ROS was induced in AML12 cel...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175048</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175048</guid>        </item>
        <item>
            <title>Specific and prolonged proteasome inhibition dictates apoptosis induction by marizomib and its analogs.</title>
            <link>http://www.medworm.com/index.php?rid=5175047&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864512%26dopt%3DAbstract</link>
            <description>Authors: Miller CP, Manton C, Hale R, Debose L, Macherla VR, Potts BC, Palladino MA, Chandra J
    Abstract
    Marizomib (NPI-0052) is a naturally derived irreversible proteasome inhibitor that potently induces apoptosis via a caspase-8 and ROS-dependent mechanism in leukemia cells. We aim to understand the relationship between the irreversible inhibition of the proteasome and induction of cell death in leukemia cells by using analogs of marizomib that display reversible and irreversible properties. We highlight the importance of sustained inhibition of at least two proteasome activities as being key permissive events for the induction of the apoptotic process in leukemia cells. These data provide the basis for the development of new approaches to generate more effective anti-proteasome t...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175047</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175047</guid>        </item>
        <item>
            <title>Protective role of sinapic acid against arsenic - Induced toxicity in rats.</title>
            <link>http://www.medworm.com/index.php?rid=5175046&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864513%26dopt%3DAbstract</link>
            <description>Authors: Pari L, Mohamed Jalaludeen A
    Abstract
    Arsenic compounds are classified as toxicants and human carcinogens. Environmental exposure to arsenic imposes a big health issue worldwide. Sinapic acid is a phenylpropanoid compound and is found in various herbal materials and high-bran cereals. It has been reported that sinapic acid has antioxidant efficacy as metal chelators due to the orientation of functional groups. However, it has not yet been examined in experimental animals. In light of this fact, the purpose of this study was to characterize the protective role of sinapic acid against arsenic induced toxicity in rats. Rats were orally treated with arsenic alone (5mg/kg body weight (bw)/day) plus sinapic acid at different doses (10, 20 and 40mg/kg bw/day) for 30days. Hepatoto...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175046</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175046</guid>        </item>
        <item>
            <title>d-Ribose glycates β(2)-microglobulin to form aggregates with high cytotoxicity through a ROS-mediated pathway.</title>
            <link>http://www.medworm.com/index.php?rid=5175045&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864514%26dopt%3DAbstract</link>
            <description>Authors: Kong FL, Cheng W, Chen J, Liang Y
    Abstract
    β(2)-Microglobulin (β(2)M) modified with advanced glycation end products (AGEs) is a major component of the amyloid deposits in hemodialysis-associated amyloidosis (HAA). However, the effect of glycation on the misfolding and aggregation of β(2)M has not been studied so far. Here we examine the molecular mechanism of aggregate formation of HAA-related ribosylated β(2)M in vitro. We find that the glycating agent d-ribose interacts with human β(2)M to generate AGEs that form aggregates in a time-dependent manner. Ribosylated β(2)M molecules are highly oligomerized compared with unglycated β(2)M, and have granular morphology. Furthermore, such ribosylated β(2)M aggregates show significant cytotoxicity to both human SH-SY5Y ne...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175045</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175045</guid>        </item>
        <item>
            <title>The interactive effect of elevated temperature on deltamethrin-induced biochemical stress responses in Channa punctata Bloch.</title>
            <link>http://www.medworm.com/index.php?rid=5097737&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21801715%26dopt%3DAbstract</link>
            <description>Authors: Kaur M, Atif F, Ansari RA, Ahmad F, Raisuddin S
    There are reports showing interactive effect of environmental factors with the toxic outcome of chemicals. We studied the interactive effect of elevated temperature as an abiotic stressor on deltamethrin-induced biochemical stress responses in a freshwater fish, Channa punctata Bloch. Heat stress (∼12°C above ambient temperature for 3h) and pesticide exposure (deltamethrin 0.75ppb for 48h) showed significant induction of heat shock protein-70 (HSP70) in liver, kidney and gills of fishes. Elevated temperature when followed by deltamethrin exposure showed synergistic effect showing a high level of HSP70 in liver and gills whereas response in the kidney was opposite. On the contrary, when deltamethrin exposure followed the heat s...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097737</comments>
            <pubDate>Fri, 22 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097737</guid>        </item>
        <item>
            <title>Molecular pathogenesis of hepatic fibrosis and current therapeutic approaches.</title>
            <link>http://www.medworm.com/index.php?rid=5097736&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21803030%26dopt%3DAbstract</link>
            <description>Authors: Mormone E, George J, Nieto N
    The pathogenesis of hepatic fibrosis involves significant deposition of fibrilar collagen and other extracellular matrix proteins. It is a rather dynamic process of wound healing in response to a variety of persistent liver injury caused by factors such as ethanol intake, viral infection, drugs, toxins, cholestasis, and metabolic disorders. Liver fibrosis distorts the hepatic architecture, decreases the number of endothelial cell fenestrations and causes portal hypertension. Key events are the activation and transformation of quiescent hepatic stellate cells into myofibroblast-like cells with the subsequent up-regulation of proteins such as α-smooth muscle actin, interstitial collagens, matrix metalloproteinases, tissue inhibitor of metalloprotein...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097736</comments>
            <pubDate>Thu, 21 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097736</guid>        </item>
        <item>
            <title>Hydroxytyrosol glucuronides protect renal tubular epithelial cells against H(2)O(2) induced oxidative damage.</title>
            <link>http://www.medworm.com/index.php?rid=5097738&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21798251%26dopt%3DAbstract</link>
            <description>Authors: Deiana M, Incani A, Rosa A, Atzeri A, Loru D, Cabboi B, Paola Melis M, Lucas R, Morales JC, Assunta Dessì M
    Hydroxytyrosol (2-(3',4'-dihydroxyphenyl)ethanol; HT), the most active ortho-diphenolic compound, present either in free or esterified form in extravirgin olive oil, is extensively metabolized in vivo mainly to O-methylated, O-sulfated and glucuronide metabolites. We investigated the capacity of three glucuronide metabolites of HT, 3'-O-β-d-glucuronide and 4'-O-β-d-glucuronide derivatives and 2-(3',4'-dihydroxyphenyl)ethanol-1-O-β-d-glucuronide, in comparison with the parent compound, to inhibit H(2)O(2) induced oxidative damage and cell death in LLC-PK1 cells, a porcine kidney epithelial cell line. H(2)O(2) treatment exerted a toxic effect inducing cell death, inter...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097738</comments>
            <pubDate>Wed, 20 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097738</guid>        </item>
        <item>
            <title>The metabolic bioactivation of caffeic acid phenethyl ester (CAPE) mediated by tyrosinase selectively inhibits glutathione S-transferase.</title>
            <link>http://www.medworm.com/index.php?rid=5097739&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21458432%26dopt%3DAbstract</link>
            <description>In conclusion, both CAPE and caffeic acid selectively inhibited GST in the presence of tyrosinase. Our results suggest that intracellularly formed quinones and glutathione conjugates of caffeic acid and CAPE may play major roles in the selective inhibition of GST in SK-MEL-28 melanoma cells. Moreover, the inhibition of MRP enhances CAPE-induced toxicity in the SK-MEL-28 melanoma cells.
    PMID: 21458432 [PubMed - indexed for MEDLINE] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097739</comments>
            <pubDate>Thu, 14 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097739</guid>        </item>
        <item>
            <title>Pharmacodynamics of ellagic acid on cardiac troponin-T, lyosomal enzymes and membrane bound ATPases: Mechanistic clues from biochemical, cytokine and in vitro studies.</title>
            <link>http://www.medworm.com/index.php?rid=5051711&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21762681%26dopt%3DAbstract</link>
            <description>This study was designed to evaluate the protective effects of ellagic acid on the levels of cardiac troponin-T, lysosomal enzymes, and membrane bound ATPases along with the role of pro inflammatory cytokine. Male albino Wistar rats were pretreated with ellagic acid (7.5 and 15mg/kg body weight) daily for a period of 10days. After the pretreatment period isoproterenol (100mg/kg) was subcutaneously injected to rats twice at an interval of 24h. The protective effects of pretreatment with ellagic acid were measured by biochemical analysis and reverse transcriptase polymerase chain reaction. Evidence of myocardial infarction in isoproterenol induced rats included significant increase in the serum level of cardiac troponin-T and decreased levels of creatine kinase and lactate dehydrogenase in he...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051711</comments>
            <pubDate>Mon, 04 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051711</guid>        </item>
        <item>
            <title>Involvement of catalase in the apoptotic mechanism induced by apigenin in HepG2 human hepatoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=5051713&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21756884%26dopt%3DAbstract</link>
            <description>Authors: Valdameri G, Trombetta-Lima M, Worfel PR, Pires AR, Martinez GR, Noleto GR, Cadena SM, Sogayar MC, Winnischofer SM, Rocha ME
    Apigenin has been reported to inhibit proliferation of cancer cells; however, the mechanism underlying its action is not completely understood. Here, we evaluated the effects of apigenin on the levels of expression and activity of antioxidant enzymes, and the involvement of ROS in the mechanism of cell death induced by apigenin in HepG2 human hepatoma cells. Upon treatment with apigenin, HepG2 cells displayed a reduction in cell viability in a dose- and time-dependent manner, and some morphological changes. In addition, apigenin treatment induced ROS generation and significantly decreased the mRNA levels and activity of catalase and levels of intracellul...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051713</comments>
            <pubDate>Sat, 02 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051713</guid>        </item>
        <item>
            <title>Cadmium-induced ovarian pathophysiology is mediated by change in gene expression pattern of zinc transporters in zebrafish (Danio rerio).</title>
            <link>http://www.medworm.com/index.php?rid=5051712&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21756885%26dopt%3DAbstract</link>
            <description>This study explored the potential for expression pattern of genes encoding zinc (Zn) transporters to be involved in the cadmium (Cd)-induced reproductive toxicity in female of zebrafish. For this purpose, oocytes maturity and ovarian histology as well as Cd, Zn and metallothioneins (MTs) accumulation and expression of genes encoding Zrt-,Irt-related protein 10 (ZIP10), Zn transporter 1 (ZnT1 and ZIP10) and zebrafish metallothionein (zMT) were examined in ovaries of adult zebrafish exposed to 0.4mg/L Cd in water and supplemented with Zn (5mgkg(-1)) in their diet for 21days. Cd-exposure decreased the expression of ZnT1 and caused up-regulation of ZIP10 and zMT gene expression. These changes were accompanied by increased Cd and MTs accumulation, decreased Zn contents as well as by histopathol...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051712</comments>
            <pubDate>Sat, 02 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051712</guid>        </item>
        <item>
            <title>Arsenic trioxide and radiation enhance apoptotic effects in HL-60 cells through increased ROS generation and regulation of JNK and p38 MAPK signaling pathways.</title>
            <link>http://www.medworm.com/index.php?rid=5051715&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21741957%26dopt%3DAbstract</link>
            <description>Authors: Ho SY, Wu WJ, Chiu HW, Chen YA, Ho YS, Guo HR, Wang YJ
    The induction of apoptotic cell death is a significant mechanism of tumor cells under the influence of radio-/chemotherapy, and resistance to these treatments has been linked to some cancer cell lines with a low propensity for apoptosis. The present study aimed to investigate the enhanced effects and mechanisms in apoptosis and the cycle distribution of HL-60 cells, a human leukemia cell line lacking a functional p53 protein, after combination treatment with arsenic trioxide (ATO) and irradiation (IR). Our results indicated that combined treatment led to increased cytotoxicity and apoptotic cell death in HL-60 cells, which was correlated with the activation of cdc-2 and increased expression of cyclin B, the induction of in...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051715</comments>
            <pubDate>Thu, 30 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051715</guid>        </item>
        <item>
            <title>Effects of CYP inhibitors on precocene I metabolism and toxicity in rat liver slices.</title>
            <link>http://www.medworm.com/index.php?rid=5051714&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21741958%26dopt%3DAbstract</link>
            <description>We present a comprehensive in vitro approach to assessing metabolism-mediated hepatotoxicity using male Sprague-Dawley rat liver slices incubated with the well characterized hepatotoxicant, precocene I, and inhibitors of cytochrome P450 (CYP) enzymes. This approach combines liquid chromatography mass spectrometry (LC MS) detection methods with multiple toxicity endpoints to enable identification of critical metabolic pathways for hepatotoxicity. The incubations were performed in the absence and presence of the non-specific CYP inhibitor, 1-aminobenzotriazole (ABT) and isoform-specific inhibitors. The metabolite profile of precocene I in rat liver slices shares some features of the in vivo profile, but also had a major difference in that epoxide dihydrodiol hydrolysis products were not obse...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051714</comments>
            <pubDate>Thu, 30 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051714</guid>        </item>
        <item>
            <title>A novel parthenin analog exhibits anti-cancer activity: Activation of apoptotic signaling events through robust NO formation in human leukemia HL-60 cells.</title>
            <link>http://www.medworm.com/index.php?rid=5051716&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21741372%26dopt%3DAbstract</link>
            <description>This study describes the anti-cancer activity of P19, an analog of parthenin. P19 induced apoptosis in HL-60 cells and inhibited cell proliferation with 48h IC50 of 3.5μM. At 10mg/kg dose, it doubled the median survival time of L1210 leukemic mice and at 25mg/kg it inhibited Ehrlich ascites tumor growth by 60%. Investigation of the mechanism of P19 induced apoptosis in HL-60 cells revealed that N-acetyl-l-cysteine (NAC) and s-methylisothiourea (sMIT) could reverse several molecular events that lead to cell death by inhibiting nitric oxide (NO) formation. It selectively produced massive NO in cells while quenching the basal ROS levels with concurrent elevation of GSH. P19 disrupted mitochondrial integrity leading to cytochrome c release and caspase-9 activation. P19 also caused caspase-8 a...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051716</comments>
            <pubDate>Tue, 28 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051716</guid>        </item>
        <item>
            <title>Amelioration of glucose induced hemolysis of human erythrocytes by vitamin E.</title>
            <link>http://www.medworm.com/index.php?rid=5051717&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21736874%26dopt%3DAbstract</link>
            <description>Authors: Marar T
    Cells under aerobic condition are always threatened with the insult of reactive oxygen species, which are efficiently taken care of by the highly powerful antioxidant systems of the cell. The erythrocytes (RBCs) are constantly exposed to oxygen and oxidative stress but their metabolic activity is capable of reversing the injury under normal conditions. In vitro hemolysis of RBCs induced by 5, 10 and 20mM glucose was used as a model to study the free radical induced damage of biological membranes in hyperglycemic conditions and the protection rendered by vitamin E on the same. RBCs are susceptible to oxidative damage, peroxidation of the membrane lipids, release of hemoglobin (hemolysis) and alteration in activity of antioxidant enzymes catalase and superoxide dismutase...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051717</comments>
            <pubDate>Sat, 25 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051717</guid>        </item>
        <item>
            <title>Effect of galangin supplementation on oxidative damage and inflammatory changes in fructose-fed rat liver.</title>
            <link>http://www.medworm.com/index.php?rid=5004252&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21708140%26dopt%3DAbstract</link>
            <description>Authors: Sivakumar AS, Anuradha CV
    The study examined the effects of galangin (GA) on oxidative stress, inflammatory cytokine levels and nuclear factor-kappa B (NF-κB) activation in fructose-fed rat liver. Adult male albino Wistar rats were divided into 4 groups. Groups 1 and 4 received the control diet containing starch as the source of carbohydrate while groups 2 and 3 were fed a diet containing fructose. Groups 3 and 4 additionally received GA (100μg/kg, p.o) from the 15th day. At the end of 60 days, the levels of plasma glucose, insulin and triglycerides, insulin sensitivity indices and oxidative stress markers in the liver were determined. Cytokines of interest were assayed by ELISA and RT-PCR and NF-κB p65 nuclear translocation by Western blot and RT-PCR. Compared to control d...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5004252</comments>
            <pubDate>Fri, 24 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5004252</guid>        </item>
        <item>
            <title>Discovery and biological characterization of 1-(1H-indol-3-yl)-9H-pyrido[3,4-b]indole as an aryl hydrocarbon receptor activator generated by photoactivation of tryptophan by sunlight.</title>
            <link>http://www.medworm.com/index.php?rid=5004213&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21722628%26dopt%3DAbstract</link>
            <description>We report here the isolation from aTRP and chemical characterization and synthesis of 1-(1H-indol-3-yl)-9H-pyrido[3,4-b]indole (IPI), a compound previously identified as a natural product of marine ascidia and now shown to be a TRP photoproduct with AHR-inducing properties. IPI, FICZ and TCDD produced equieffective induction of CYP1A-mediated 7-ethoxyresorufin deethylase (EROD) activity in chick embryo primary hepatocytes and mammalian Hepa1c1c7 cells. EROD induction by IPI was markedly curtailed in AHR-defective c35 cells, supporting the AHR dependence of the IPI response. Although IPI had a higher EC(50) for EROD induction than FICZ, the much larger amount of IPI than FICZ in aTRP makes IPI a prominent contributor to EROD induction in aTRP. IPI was detected in TRP-containing culture medi...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5004213</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5004213</guid>        </item>
        <item>
            <title>Mangiferin attenuates methylmercury induced cytotoxicity against IMR-32, human neuroblastoma cells by the inhibition of oxidative stress and free radical scavenging potential.</title>
            <link>http://www.medworm.com/index.php?rid=5004290&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21703249%26dopt%3DAbstract</link>
            <description>Authors: Das S, Nageshwar Rao B, Satish Rao BS
    Mangiferin (MGN), a C-glucosylxanthone was investigated for its ability to protect against methylmercury (MeHg) induced neurotoxicity by employing IMR-32 (human neuroblastoma) cell line. MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] and clonogenic cell survival assays confirmed the efficacy of MGN supplementation in attenuating MeHg-induced cytotoxicity. Pre-treatment with MGN significantly (p&amp;lt;0.01) inhibited MeHg-induced DNA damage (micronuclei, olive tail moment and % tail DNA) thereby demonstrating MGN's antigenotoxic potential. Also, pre-treatment with MGN significantly reduced MeHg-induced oxidative stress, intra-cellular Ca(2+) influx and inhibited depolarization of mitochondrial membrane. MGN pre-treated cell...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5004290</comments>
            <pubDate>Mon, 13 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5004290</guid>        </item>
        <item>
            <title>CBI Editorial 2011.</title>
            <link>http://www.medworm.com/index.php?rid=4958507&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21672531%26dopt%3DAbstract</link>
            <description>Authors: Bond JA
    
    PMID: 21672531 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4958507</comments>
            <pubDate>Sun, 12 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4958507</guid>        </item>
        <item>
            <title>Effect of thymol on peripheral blood mononuclear cell PBMC and acute promyelotic cancer cell line HL-60.</title>
            <link>http://www.medworm.com/index.php?rid=4910416&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21640085%26dopt%3DAbstract</link>
            <description>Authors: Deb DD, Parimala G, Sarvana Devi S, Chakraborty T
    Thymol, a naturally occurring phenolic compound, has been known for its antioxidant, anti microbial, and anti inflammatory activity. Thymol has also been reported as anti-cancer agent, but its anti-cancer mechanism has not yet been fully elucidated. Thus, we aimed to investigate anticancer activity of thymol on HL-60 (acute promyelotic leukemia) cells. In our study, thymol demonstrated dose dependent cytotoxic effects on HL-60 cells after 24h of exposure. However, thymol did not show any cytotoxic effect in normal human PBMC. The cytotoxic effect of thymol on HL-60 cells appears to be associated with induction of cell cycle arrest at sub G0/G1 phase, and apoptotic cell death based on genomic DNA fragmentation pattern. Thymol al...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4910416</comments>
            <pubDate>Thu, 26 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4910416</guid>        </item>
        <item>
            <title>Protective effect of zinc against cadmium hepatotoxicity depends on this bioelement intake and level of cadmium exposure: A study in a rat model.</title>
            <link>http://www.medworm.com/index.php?rid=4910417&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21627960%26dopt%3DAbstract</link>
            <description>Authors: Rogalska J, Pilat-Marcinkiewicz B, Brzóska MM
    It was estimated, in a rat model of moderate and relatively high chronic human exposure to cadmium (Cd), whether enhanced zinc (Zn) consumption may prevent Cd-induced liver injury and if the possible protective effect of this bioelement depends on its intake. For this purpose, the structure and function of the liver of the rats that received Zn (30 and 60mg/l) or/and Cd (5 and 50mg/l) for 6months were evaluated. The treatment with Cd led to, dependent on the exposure level, pathological changes in the liver, including enhanced apoptosis and induction of inflammatory and necrotic processes. Moreover, the serum activities of hepatic marker enzymes (alanine transaminase and aspartate transaminase) and the concentration of proinflamma...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4910417</comments>
            <pubDate>Mon, 23 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4910417</guid>        </item>
        <item>
            <title>Glabridin protects osteoblastic MC3T3-E1 cells against antimycin A induced cytotoxicity.</title>
            <link>http://www.medworm.com/index.php?rid=4910420&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21621525%26dopt%3DAbstract</link>
            <description>In this study, the protective effects of glabridin, an isoflavan isolated from licorice root, against pharmacological inhibition of the respiratory chain were studied using osteoblastic MC3T3-E1 cells treated with antimycin A, which inhibits complex III of the electron transport system. Glabridin restored mitochondrial membrane potential dissipation, ATP loss, inactivation of complex IV, intracellular calcium elevation, and cytochrome c release that was induced by antimycin A treatment. This compound also prevented cell death. These results imply that glabridin protects osteoblasts from antimycin A-induced cell death via improved mitochondrial function. Glabridin scavenged ROS and mitochondrial superoxide anions generated by antimycin A. In addition, glabridin prevented antimycin A-induced...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4910420</comments>
            <pubDate>Thu, 19 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4910420</guid>        </item>
        <item>
            <title>Nitric oxide donor, V-PROLI/NO, provides protection against arsenical induced toxicity in rat liver cells: Requirement for Cyp1a1.</title>
            <link>http://www.medworm.com/index.php?rid=4910419&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21621526%26dopt%3DAbstract</link>
            <description>Authors: Qu W, Cheng L, Dill AL, Saavedra JE, Hong SY, Keefer LK, Waalkes MP
    Arsenic is a cancer chemotherapeutic but hepatotoxicity can be a limiting side effect. O(2)-vinyl 1-[2-(carboxylato)pyrrolidin-1-yl]diazen-1-ium-1,2-diolate (V-PROLI/NO) is a nitric oxide (NO) donor prodrug and metabolized by liver cytochromes P450 (CYP450) to release NO. The effects of V-PROLI/NO pretreatment on the toxicity of arsenic (as NaAsO(2)) were studied in a rat liver cell line (TRL 1215). The cells acted upon the prodrug to release NO, as assessed by nitrite levels, in a time-dependent fashion to maximal levels of 8-fold above basal levels. Pretreatment with V-PROLI/NO markedly reduced arsenic cytolethality which was directly related to the level of NO produced by V-PROLI/NO treatment. Cyp1a1 expres...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4910419</comments>
            <pubDate>Thu, 19 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4910419</guid>        </item>
        <item>
            <title>Dietary astaxanthin inhibits colitis and colitis-associated colon carcinogenesis in mice via modulation of the inflammatory cytokines.</title>
            <link>http://www.medworm.com/index.php?rid=4910418&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21621527%26dopt%3DAbstract</link>
            <description>Authors: Yasui Y, Hosokawa M, Mikami N, Miyashita K, Tanaka T
    Astaxanthin (AX) is one of the marine carotenoid pigments, which possess powerful biological antioxidant, anti-inflammatory and anti-cancer properties. The purpose of this study is to investigate possible inhibitory effect of AX against inflammation-related mouse colon carcinogenesis and dextran sulfate sodium (DSS)-induced colitis in male ICR mice. We conducted two different experiments. In the first experiment, we evaluated the effects of AX at three dose levels, 50, 100 and 200ppm in diet, on colitis-associated colon carcinogenesis induced by azoxymethane (AOM)/DSS in mice. In the second, the effects of the AX (100 and 200ppm) in diet on DSS-induced colitis were determined. We found that dietary AX significantly inhibited...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4910418</comments>
            <pubDate>Thu, 19 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4910418</guid>        </item>
        <item>
            <title>The role of the glutathione system in seizures induced by diphenyl diselenide in rat pups.</title>
            <link>http://www.medworm.com/index.php?rid=4910421&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21620807%26dopt%3DAbstract</link>
            <description>In conclusion, administration of GSH protected against seizure episodes induced by (PhSe)(2) in rat pups by reducing oxidative stress and, at least in part, by acting as an antagonist of glutamate and glycine modulatory sites in the NMDA receptor.
    PMID: 21620807 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4910421</comments>
            <pubDate>Mon, 16 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4910421</guid>        </item>
        <item>
            <title>Antitumor effects of a novel benzonaphthofurandione derivative (8e) on the human colon cancer cells in vitro and in vivo through cell cycle arrest accompanied with the modulation of EGFR and mTOR signaling.</title>
            <link>http://www.medworm.com/index.php?rid=4859180&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21600193%26dopt%3DAbstract</link>
            <description>In this study, we evaluated the antitumor effects of 3-[2-(dimethylamino)isopropoxy]-1-hydroxybenzo[b]naphtho[2,3-d]furan-6,11-dione (8e), a novel benzonaphthofurandione derivative, on the growth of colorectal cancer HCT 116 cells both in vitro culture and an in vivo animal model. Compound 8e exhibited the potential growth inhibition of the colon cancer cells in a concentration-dependent manner. The anti-proliferative activity of 8e was also associated with the induction of cell cycle arrest in the G(0)/G(1) phase. The 8e-induced cell cycle arrest was well correlated with the suppression of cyclin-dependent kinase 2 (CDK2), CDK4, cyclin D1, cyclin E, c-Myc, and phosphorylated retinoblastoma protein (pRb). The tumor growth in xenograft nude mice bearing HCT 116 cells by compound 8e (10mg/kg...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859180</comments>
            <pubDate>Mon, 09 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859180</guid>        </item>
        <item>
            <title>The effects of nitrogen-heme-iron coordination on substrate affinities for cytochrome P450 2E1.</title>
            <link>http://www.medworm.com/index.php?rid=4859175&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21600194%26dopt%3DAbstract</link>
            <description>Authors: Jones JP, Joswig-Jones CA, Hebner M, Chu Y, Koop DR
    A descriptor based computational model was developed for cytochrome P450 2E1 (CYP2E1) based on inhibition constants determined for inhibition of chlorzoxazone, or 4-nitrophenol, metabolism. An empirical descriptor for type II binding was developed and tested for a series of CYP2E1 inhibitors. Inhibition constants where measured for 51 different compounds. A fast 2-dimensional predictive model was developed based on 40 compounds, and tested on 8 compounds of diverse structure. The trained model (n=40) had an r(2) value of 0.76 and an RMSE of 0.48. The correlation between the predicted and actual pK(i) values of the test set of compounds not included in the model gives an r(2) value of 0.78. The features that described binding ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859175</comments>
            <pubDate>Mon, 09 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859175</guid>        </item>
        <item>
            <title>Beneficial role of naringin, a flavanoid on nickel induced nephrotoxicity in rats.</title>
            <link>http://www.medworm.com/index.php?rid=4859174&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21600195%26dopt%3DAbstract</link>
            <description>This study was conducted to investigate the beneficial role of naringin on nickel induced nephrotoxicity. Nickel (Ni) (20mg/kg body weight (b.w.) was administered intraperitoneally (i.p.) for 20days. Naringin was administered orally (20, 40 and 80mg/kg b.w.) with i.p. administration of Ni. Ni administration increased the levels of serum urea, uric acid and creatinine with a significant decrease in creatinine clearance and decreased levels of urea, uric acid and creatinine in urine. The levels of lipid peroxidation markers and nickel concentration in blood and kidney were also increased. While, the activities of enzymic and non-enzymic antioxidants were decreased. Treatment with naringin attenuated the alterations in the renal and urine markers, decreasing lipid peroxidation markers, increa...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859174</comments>
            <pubDate>Mon, 09 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859174</guid>        </item>
        <item>
            <title>Influence of tamoxifen on gluconeogenesis and glycolysis in the perfused rat liver.</title>
            <link>http://www.medworm.com/index.php?rid=4859188&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21570382%26dopt%3DAbstract</link>
            <description>Authors: Marek CB, Peralta RM, Itinose AM, Bracht A
    The actions of tamoxifen, a selective estrogen receptor modulator used in chemotherapy and chemo-prevention of breast cancer, on glycolysis and gluconeogenesis were investigated in the isolated perfused rat liver. Tamoxifen inhibited gluconeogenesis from both lactate and fructose at very low concentrations (e.g., 5μM). The opposite, i.e., stimulation, was found for glycolysis from both endogenous glycogen and fructose. Oxygen uptake was unaffected, inhibited or stimulated, depending on the conditions. Stimulation occurred in both microsomes and mitochondria. Tamoxifen did not affect the most important key-enzymes of gluconeogenesis, namely, phosphoenolpyruvate carboxykinase, pyruvate carboxylase, fructose 1,6-bisphosphatase and gluco...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859188</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859188</guid>        </item>
        <item>
            <title>Radiosensitization by celastrol is mediated by modification of antioxidant thiol molecules.</title>
            <link>http://www.medworm.com/index.php?rid=4859182&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21570383%26dopt%3DAbstract</link>
            <description>Authors: Seo HR, Seo WD, Pyun BJ, Lee BW, Jin YB, Park KH, Seo EK, Lee YJ, Lee YS
    The radiosensitizing effects of naturally occurring triterpenes were investigated in human lung cancer cells. Several quinone methide-containing triterpenes (QMTs) enhanced the cytotoxic effect of ionizing radiation (IR) and of these QMTs, celastrol (CE) had the greatest enhancing effect on IR-induced cell death in vitro. Additionally, the quinone methide moiety of CE was shown to be essential for CE-mediated radiosensitization; in contrast, dihydrocelastrol (DHCE), does not contain this moiety. Reactive oxygen species (ROS) production by IR was augmented in combination with CE, which was responsible for CE-mediated radiosensitization. CE induced the thiol reactivity and inhibited the activities of antiox...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859182</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859182</guid>        </item>
        <item>
            <title>Exposure to sodium tungstate and Respiratory Syncytial Virus results in hematological/immunological disease in C57BL/6J mice.</title>
            <link>http://www.medworm.com/index.php?rid=4859189&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21565177%26dopt%3DAbstract</link>
            <description>This study reports the results of exposing C57BL/6J mice to Na(2)WO(4)in utero via water (15ppm, ad libetum) and inhalation (mean concentration PM(5) 3.33mg/m(3)) and to Respiratory Syncytial Virus (RSV) within 2weeks of weaning. Inoculation of C57BL/6J mice with RSV was associated with a neutrophil shift in 56% of 5-month old mice. When the RSV inoculation was combined with Na(2)WO(4)-exposure, significant splenomegaly resulted (p=0.0406, 0.0184, 0.0108 for control, Na(2)WO(4)-only and RSV-only, respectively) in addition to other hematological pathologies which were not significant. Exposure to Na(2)WO(4) and RSV resulted in hematological/immunological disease, the nature of which is currently inconclusive. Further research is needed to characterize this potential leukemia mouse model.
  ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859189</comments>
            <pubDate>Sat, 30 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859189</guid>        </item>
        <item>
            <title>Review of the Churchill County, NV ALL cluster, 1997-2004.</title>
            <link>http://www.medworm.com/index.php?rid=4859191&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21554862%26dopt%3DAbstract</link>
            <description>Authors: Walker M, Pritsos C, Seiler R
    Between 1997 and 2002, 16 cases of acute childhood leukemia were diagnosed in children who either lived in Churchill County, Nevada at the time of diagnosis or had lived in the county before their diagnosis. The cases were characterized as a cluster of like illnesses and the probability of having such a cluster occur by chance was estimated to be very small (approximately one in 2.33×10(8)). This suggested that the cluster could be linked to one or more physical, limnological, chemical, or biological agents. This review discusses the setting in which the cluster took place, the epidemiological investigations carried out by the Nevada Bureau of Health Protection Services, the National Center for Environmental Health Centers for Disease Control and...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859191</comments>
            <pubDate>Fri, 29 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859191</guid>        </item>
        <item>
            <title>Methylated chrysin induces co-ordinated attenuation of the canonical Wnt and NF-kB signaling pathway and upregulates apoptotic gene expression in the early hepatocarcinogenesis rat model.</title>
            <link>http://www.medworm.com/index.php?rid=4859190&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21554863%26dopt%3DAbstract</link>
            <description>Authors: Khan MS, Halagowder D, Devaraj SN
    Hepatocellular carcinoma (HCC), a highly aggressive form of solid tumor, has been increasing in South East Asia. The lack of effective therapy necessitates the introduction of novel chemopreventive strategies to counter the substantial morbidity and mortality associated with the disease. Recently, we reported that dimethoxy flavone (DMF), a methylated flavone derived from chrysin, significantly suppressed the development of preneoplastic lesions induced by N-nitrosodiethylamine (DEN) in rats, although the mechanism of action was not known. In the present study, we have investigated the effects of DMF administration on gene expression changes related to the inflammation-mediated NF-kB pathway, Wnt pathway and apoptotic mediators in DEN-induced ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859190</comments>
            <pubDate>Fri, 29 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859190</guid>        </item>
        <item>
            <title>Physical setting and natural sources of exposure to carcinogenic trace elements and radionuclides in Lahontan Valley, Nevada.</title>
            <link>http://www.medworm.com/index.php?rid=4804555&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21536017%26dopt%3DAbstract</link>
            <description>Authors: Seiler R
    In Lahontan Valley, Nevada, arsenic, cobalt, tungsten, uranium, radon, and polonium-210 are carcinogens that occur naturally in sediments and groundwater. Arsenic and cobalt are principally derived from erosion of volcanic rocks in the local mountains and tungsten and uranium are derived from erosion of granitic rocks in headwater reaches of the Carson River. Radon and (210)Po originate from radioactive decay of uranium in the sediments. Arsenic, aluminum, cobalt, iron, and manganese concentrations in household dust suggest it is derived from the local soils. Excess zinc and chromium in the dust are probably derived from the vacuum cleaner used to collect the dust, or household sources such as the furnace. Some samples have more than 5 times more cobalt in the dust th...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804555</comments>
            <pubDate>Thu, 21 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804555</guid>        </item>
        <item>
            <title>Tert-butyl-2(4,5-dihydrogen-4,4,5,5-tetramethyl-3-O-1H-imidazole-3-cationic-1-oxyl-2-pyrrolidine-1-carboxylic ester displays novel cytotoxicity through reactive oxygen species-mediated oxidative damage in MCF-7 and MDA-MB-231 cells.</title>
            <link>http://www.medworm.com/index.php?rid=4804556&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21536016%26dopt%3DAbstract</link>
            <description>Authors: Zhang Y, Guo J, Zeng L, Zhang J, Hui Y, Liu J, Qing X, Sun X, Guo G
    The cytotoxicity of a new nitroxyl nitroxide radical, tert-butyl-2 (4,5-dihydrogen-4,4,5,5-tetramethyl-3-O-1H-imidazole-3-cationic-1-oxyl-2-pyrrolidine-1-carboxylic ester (L-NNP) was examined in MCF-7 and MDA-MB-231 cells. L-NNP treatment resulted in a significant growth inhibition in MCF-7 and MDA-MB-231 cells. Compared with control, 10, 30, and 50μg/ml L-NNP treatments for 48h induced significant cell and nuclei swelling, and organelle distension. The marked cell death was seen in a concentration- and time-dependant manner in L-NNP treated groups. The L-NNP treated group displayed a concentration-dependant increase in DNA double strand damage compared to the control and the 1Gy γ-rays exposure groups. Thes...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804556</comments>
            <pubDate>Wed, 20 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804556</guid>        </item>
        <item>
            <title>Protein damage from electrophiles and oxidants in lungs of mice chronically exposed to the tumor promoter butylated hydroxytoluene.</title>
            <link>http://www.medworm.com/index.php?rid=4804554&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21536018%26dopt%3DAbstract</link>
            <description>Authors: Shearn CT, Fritz KS, Thompson JA
    The food additive butylated hydroxytoluene (BHT) promotes tumorigenesis in mouse lung. Chronic BHT exposure is accompanied by pulmonary inflammation and several studies indicate that elevated levels of reactive oxygen species (ROS) are involved in its promoting activity. The link between BHT and elevated ROS involves formation of quinone methide (QM) metabolites; these electrophiles form adducts with a variety of lung proteins including several enzymes that protect cells from oxidative stress. Studies in vitro demonstrated that QM alkylation of cytoprotective enzymes is accompanied by inactivation, so an objective of the present investigation was to determine if inactivation also occurs in vivo. Two groups of mice were exposed to BHT by intrape...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804554</comments>
            <pubDate>Wed, 20 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804554</guid>        </item>
        <item>
            <title>Inhibition of DNA binding activity of cAMP response element-binding protein by 1,2-naphthoquinone through chemical modification of Cys-286.</title>
            <link>http://www.medworm.com/index.php?rid=4804557&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21530497%26dopt%3DAbstract</link>
            <description>In this study, we identified the modification sites of CREB that are associated with the decreased transcriptional activity. Matrix-assisted laser desorption and ionization time-of-flight mass spectrometry (MALDI-TOF/MS) analysis indicated that three amino acids (Cys-286, Lys-290, and Lys-319) were irreversibly modified by 1,2-NQ. Mutational analysis revealed that electrophilic modification of Cys-286, but not the other two amino acids, at the DNA binding domain is essential for the reduced CREB activity. Substitution of Cys-286 with tryptophan (C286W), which mimics CREB modification by 1,2-NQ, supported this notion. These results suggest that the covalent interaction of CREB with 1,2-NQ through Cys-286 blocks the DNA binding activity of CREB, resulting in the repression of CREB-regulated ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804557</comments>
            <pubDate>Tue, 19 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804557</guid>        </item>
        <item>
            <title>Estrogen-related receptor ERRα-mediated downregulation of human hydroxysteroid sulfotransferase (SULT2A1) in Hep G2 cells.</title>
            <link>http://www.medworm.com/index.php?rid=4754006&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21513704%26dopt%3DAbstract</link>
            <description>Authors: Huang C, Zhou T, Chen Y, Sun T, Zhang S, Chen G
    Hydroxysteroid sulfotransferase SULT2A1 catalyzes the sulfation of hydroxysteroids and xenobiotics. It plays an important role in the detoxification of hydroxyl-containing xenobiotics and in the regulation of the biological activities of hydroxysteroids. ERRα is an orphan member of the nuclear receptor superfamily that is closely related to estrogen receptor alpha (ERα). Here we report that the mRNA expression of human SULT2A1 was suppressed by ERRα in Hep G2 cells. To investigate the mechanisms of this regulation, the effects of ERRα on human SULT2A1 promoter transcription in Hep G2 cells were investigated. Reporter luciferase assay results showed that ERRα significantly represses human SULT2A1 promoter transcription in Hep...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754006</comments>
            <pubDate>Tue, 12 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754006</guid>        </item>
        <item>
            <title>Carnosine and neocuproine as neutralizing agents for copper overload-induced damages in cultured human cells.</title>
            <link>http://www.medworm.com/index.php?rid=4754007&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21501601%26dopt%3DAbstract</link>
            <description>Authors: Arnal N, de Alaniz MJ, Marra CA
    Copper is dangerous when it is present in excess, mainly because it can participate in the Fenton reaction, which produces radical species. As a consequence of copper pollution, people are involuntarily exposed to a copper overload under sub-clinical and sub-symptomatological conditions, which may be very difficult to detect. Thus, we investigated (i) the possible use of the chelator molecules carnosine and neocuproine to prevent the Cu overload-induced damage on cellular lipids and proteins, as tested in human cell culture systems, and (ii) the differential response of these two chelating agents in relation to their protective action, and the type of copper ion involved in the process, by using two types of human cultured cells (HepG2 and A-549...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754007</comments>
            <pubDate>Thu, 07 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754007</guid>        </item>
        <item>
            <title>In vitro kinetic interactions of DEET, pyridostigmine and organophosphorus pesticides with human cholinesterases - Response to the letter to the editor.</title>
            <link>http://www.medworm.com/index.php?rid=4754008&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473858%26dopt%3DAbstract</link>
            <description>Authors: Wille T, Thiermann H, Worek F
    
    PMID: 21473858 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754008</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754008</guid>        </item>
        <item>
            <title>Chemical interactions and Gulf War Illnesses.</title>
            <link>http://www.medworm.com/index.php?rid=4754009&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473857%26dopt%3DAbstract</link>
            <description>Authors: Moss JI
    
    PMID: 21473857 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754009</comments>
            <pubDate>Sun, 03 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754009</guid>        </item>
        <item>
            <title>Herbal bioactivation, molecular targets and the toxicity relevance.</title>
            <link>http://www.medworm.com/index.php?rid=4754010&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21459083%26dopt%3DAbstract</link>
            <description>Authors: Chen XW, Serag ES, Sneed KB, Zhou SF
    There have been increasing reports on the adverse reactions associated with herbal consumption. For many of these adverse reactions, the underlying biochemical mechanisms are unknown, but bioactivation of herbal compounds to generate reactive intermediates have been implicated. This minireview updates our knowledge on metabolic activation of herbal compounds, molecular targets and the toxicity relevance. A number of studies have documented that some herbal compounds can be converted to toxic or even carcinogenic metabolites by Phase I [e.g. cytochrome P450s (CYPs)] and less frequently by Phase II enzymes. For example, aristolochic acids (AAs) in Aristolochia spp, which undergo reduction of the nitro group by hepatic CYP1A1/2 or peroxidases ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754010</comments>
            <pubDate>Thu, 31 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754010</guid>        </item>
        <item>
            <title>The metabolic bioactivation of caffeic acid phenethyl ester mediated by tyrosinase selectively inhibits glutathione S-transferase.</title>
            <link>http://www.medworm.com/index.php?rid=4754011&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21458432%26dopt%3DAbstract</link>
            <description>In conclusion, CAPE and caffeic acid selectively inhibited GST in the presence of tyrosinase. Our results suggest that intracellularly formed quinones and glutathione conjugates of caffeic acid and CAPE may play major roles in the selective inhibition of GST in SK-MEL-28 melanoma cells. Moreover, the inhibition of MRP enhances CAPE-induced toxicity in the SK-MEL-28 melanoma cells.
    PMID: 21458432 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754011</comments>
            <pubDate>Wed, 30 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754011</guid>        </item>
        <item>
            <title>Rhein inhibits angiogenesis and the viability of hormone-dependent and -independent cancer cells under normoxic or hypoxic conditions in vitro.</title>
            <link>http://www.medworm.com/index.php?rid=4754013&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21457705%26dopt%3DAbstract</link>
            <description>Authors: Fernand VE, Losso JN, Truax RE, Villar EE, Bwambok DK, Fakayode SO, Lowry M, Warner IM
    Hypoxia is a hallmark of solid tumors, including breast cancer, and the extent of tumor hypoxia is associated with treatment resistance and poor prognosis. Considering the limited treatment of hypoxic tumor cells and hence a poor prognosis of breast cancer, the investigation of natural products as potential chemopreventive anti-angiogenic agents is of paramount interest. Rhein (4,5-dihydroxyanthraquinone-2-carboxylic acid), the primary anthraquinone in the roots of Cassia alata L., is a naturally occurring quinone which exhibits a variety of biologic activities including anti-cancer activity. However, the effect of rhein on endothelial or cancer cells under hypoxic conditions has never been ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754013</comments>
            <pubDate>Tue, 29 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754013</guid>        </item>
        <item>
            <title>Metformin attenuates streptozotocin-induced diabetic nephropathy in rats through modulation of oxidative stress genes expression.</title>
            <link>http://www.medworm.com/index.php?rid=4754012&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21457706%26dopt%3DAbstract</link>
            <description>Authors: Alhaider AA, Korashy HM, Sayed-Ahmed MM, Mobark M, Kfoury H, Mansour MA
    Diabetes mellitus is a group of metabolic diseases characterized by hyperglycemia resulting from defects in insulin secretion and/or action. One of the most important complications of this metabolic disease is diabetic nephropathy. Hyperglycemia promotes oxidative stress and hence generation of reactive oxygen species (ROS), which is known to play a crucial role in the pathogenesis of diabetic nephropathy. Recent studies have established that metformin, an oral hypoglycemic drug, possesses antioxidant activity effects. However, whether metformin can protect against diabetic nephropathy has not been reported before. The overall objectives of the present study are to elucidate the potential nephroprotective ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754012</comments>
            <pubDate>Tue, 29 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754012</guid>        </item>
        <item>
            <title>Role of the interaction between puerarin and the erythrocyte membrane in puerarin-induced hemolysis.</title>
            <link>http://www.medworm.com/index.php?rid=4754019&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21453687%26dopt%3DAbstract</link>
            <description>This study investigated the underlying mechanisms of puerarin-induced hemolysis. Our results show that puerarin induced concentration-dependent and time-dependent hemolysis when human erythrocytes were incubated in saline solution with more than 2mM puerarin for over 2h. However, incubation in PBS or addition of 1mM of lidocaine to the saline solution completely abolished the hemolysis. Providing materials that could start ATP synthesis did not reverse the hemolysis, and puerarin did not affect Na(+)-K(+)-ATPase activity. In addition, puerarin (0.1-2mM) did not cause calcium influx or exhibited pro-oxidant activity in erythrocytes. Puerarin exhibited different influences on the membrane microviscosity of erythrocytes in saline and PBS. Moreover, 1mM lidocaine inhibited 8mM puerarin-induced...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754019</comments>
            <pubDate>Mon, 28 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754019</guid>        </item>
        <item>
            <title>Vitamin K3-2,3-epoxide induction of apoptosis with activation of ROS-dependent ERK and JNK protein phosphorylation in human glioma cells.</title>
            <link>http://www.medworm.com/index.php?rid=4754018&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21453688%26dopt%3DAbstract</link>
            <description>Authors: Wu J, Chien CC, Yang LY, Huang GC, Cheng MC, Shen SC, Chen YC
    2-Methyl-1,4-naphthoquinone (menadione or vitamin K3; EPO) and K3-2,3-epoxide (EPO1), but not vitamin K3-3-OH (EPO2), exhibited cytotoxicity that caused DNA fragmentation and chromatin condensation in U87 and C6 cells. EPO1 showed more-potent cytotoxicity than EPO, and the IC(50) values of EPO and EPO1 in U87 cells were 37.5 and 15.7μM, respectively. Activation of caspase 3 enzyme activity with cleavage of caspase 3 protein was detected in EPO1-treated U87 and C6 cells, and the addition of the caspase 3 peptidyl inhibitor, DEVD-FMK, reduced the cytotoxic effect of EPO1. An increase in the intracellular ROS level by EPO1 was observed in the DCHF-DA analysis, and EPO1-induced apoptosis and caspase 3 protein cleavage ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754018</comments>
            <pubDate>Mon, 28 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754018</guid>        </item>
        <item>
            <title>Farnesol attenuates 1,2-dimethylhydrazine induced oxidative stress, inflammation and apoptotic responses in the colon of Wistar rats.</title>
            <link>http://www.medworm.com/index.php?rid=4754017&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21453689%26dopt%3DAbstract</link>
            <description>Authors: Khan R, Sultana S
    Colon cancer is the major health hazard related with high mortality and it is a pathological consequence of persistent oxidative stress and inflammation. Farnesol, an isoprenoid alcohol, has been shown to possess antioxidant, anti-inflammatory and chemopreventive properties. The present study was performed to evaluate the protective efficacy of farnesol against 1,2-dimethylhydrazine (DMH) induced oxidative stress, inflammatory response and apoptotic tissue damage. Farnesol was administered once daily for seven consecutive days at the doses of 50 and 100mg/kg body weight in corn oil. On day 7, a single injection of DMH was given subcutaneously in the groin at the dose of 40mg/kg body weight. Protective effects of farnesol were assessed by using caspase-3 activ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754017</comments>
            <pubDate>Mon, 28 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754017</guid>        </item>
        <item>
            <title>Effect of several analogs of 2,4,6-triphenyldioxane-1,3 on constitutive androstane receptor activation.</title>
            <link>http://www.medworm.com/index.php?rid=4754016&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21453690%26dopt%3DAbstract</link>
            <description>Authors: Pustylnyak V, Yarushkin A, Kachaylo E, Slynko N, Lyakhovich V, Gulyaeva L
    2,4,6-Triphenyldioxane-1,3 (TPD) is a highly effective species-specific inducer of CYP2В in rats. Several analogs of TPD were synthesized to verify a hypothesis that minor changes in the inducer structure can cause changes in induction abilities (R=H, cisTPD and transTPD; R=N(CH(3))(2), transpDMA; R=NO(2), transpNO(2); R=F, transpF; R=OCH(3), transpMeO). Five of six compounds were able to activate CAR in rat liver. Results of Western-blot and ChIP showed that cisTPD and transTPD, transpDMA, transpNO(2), transpF treatment stimulated nuclear accumulation of CAR and evoked CAR receptor PBREM-binding activity in rat liver. cisTPD, transTPD, transpDMA, transpNO(2) and transpF administration significantly inc...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754016</comments>
            <pubDate>Mon, 28 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754016</guid>        </item>
        <item>
            <title>Sensitizing effect of 3-methyladenine on radiation-induced cytotoxicity in radio-resistant HepG2 cells in vitro and in tumor xenografts.</title>
            <link>http://www.medworm.com/index.php?rid=4754015&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21453691%26dopt%3DAbstract</link>
            <description>In this study, 3-methyladenine (3-MA), an autophagy inhibitor, was investigated for its potential to enhance radio-sensitivity under radio-resistant conditions both in vitro and in vivo. Hep3B and HepG2 cells were used to examine the radio-resistance of liver cancer cells. The results show that Hep3B cells respond to irradiation with increased apoptotic cell death and that HepG2 is radio-resistant due to the IR-induced autophagy, as verified by DNA fragmentation, electron microscopy, acidic vesicular organelle formation, and Western blot analysis. Application of IR with 3-MA to inhibit autophagy simultaneously suppressed the expression of LC3 and enhanced cell death. The tumor xenograft model in nude mice verified the synergistic cytotoxic effect of 3-MA and IR, which resulted in significa...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754015</comments>
            <pubDate>Mon, 28 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754015</guid>        </item>
        <item>
            <title>Aristolochic acid downregulates monocytic matrix metalloproteinase-9 by inhibiting nuclear factor-κB activation.</title>
            <link>http://www.medworm.com/index.php?rid=4754014&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21453692%26dopt%3DAbstract</link>
            <description>In this study, we found that AA showed concentration-dependent inhibition of tumor necrosis factor (TNF)-α-induced MMP-9 activation with an IC(50) value of 6.4±0.5μM in human monocytic THP-1 cells. A similar effect was also noted with different ratios of AAs (types I and II). However, AA had no inhibitory effect on the intact enzymatic activity of MMP-9 at a concentration of 20μM. On the other hand, the level of tissue inhibitor of metalloproteinase (TIMP)-1 was not induced by AA, but it suppressed TNF-α-induced MMP-9 protein and messenger RNA expressions. AA also significantly inhibited TNF-α-induced IκBα degradation. Furthermore, an electrophoretic mobility shift assay and a reported gene study, respectively, revealed that AA inhibited TNF-α-induced NF-κB translocation and acti...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4754014</comments>
            <pubDate>Mon, 28 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4754014</guid>        </item>
        <item>
            <title>Introduction.</title>
            <link>http://www.medworm.com/index.php?rid=4640246&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21402059%26dopt%3DAbstract</link>
            <description>Authors: Flynn TG, Kedishvili N, Maser E, O'Brien PJ, Plapp BV
    
    PMID: 21402059 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4640246</comments>
            <pubDate>Mon, 21 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4640246</guid>        </item>
        <item>
            <title>Introduction to the Proceedings of the 8th International Symposium on Biological Reactive Intermediates.</title>
            <link>http://www.medworm.com/index.php?rid=4640245&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21402060%26dopt%3DAbstract</link>
            <description>Authors: Monks TJ
    
    PMID: 21402060 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4640245</comments>
            <pubDate>Fri, 11 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4640245</guid>        </item>
        <item>
            <title>Strategies for evaluating the environment-public health interaction of long-term latency disease: the quandary of the inconclusive case-control study.</title>
            <link>http://www.medworm.com/index.php?rid=4580370&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21382361%26dopt%3DAbstract</link>
            <description>Authors: Pleil JD, Sobus JR, Sheppard PR, Ridenour G, Witten ML
    Environmental links to disease are difficult to uncover because environmental exposures are variable in time and space, contaminants occur in complex mixtures, and many diseases have a long time delay between exposure and onset. Furthermore, individuals in a population have different activity patterns (e.g., hobbies, jobs, interests), and different genetic susceptibilities to disease. As such, there are many potential confounding factors to obscure the reasons that one individual gets sick and another remains healthy. An important method for deducing environmental associations with disease outbreak is the retrospective case-control study wherein affected and control subject cohorts are studied to see what is different abou...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580370</comments>
            <pubDate>Fri, 04 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580370</guid>        </item>
        <item>
            <title>Antioxidant effect of vegetable oils containing conjugated linolenic acid isomers against induced tissue lipid peroxidation and inflammation in rat model.</title>
            <link>http://www.medworm.com/index.php?rid=4580369&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21382362%26dopt%3DAbstract</link>
            <description>Authors: Saha SS, Ghosh M
    The purpose of the present study was to examine the antioxidant activity of two typical oils obtained from two vegetables, bitter gourd seed and snake gourd seed, containing two different isomers of conjugated linolenic acid (CLnA) against oxidative stress induced by sodium arsenite in relation to tissue lipid peroxidation and inflammation. Male albino rats were taken as subject and divided into six groups: Group 1 was control and Group 2 was treated with sodium arsenite (Sa; 10mg/Kg BW); Group 3, 4, 5 and 6 were orally treated with different doses of seed oils maintaining definite concentration of CLnA isomers (0.5% and 1.0% of total lipid for each CLnA isomer) along with sodium arsenite. There was significant increase in lipid peroxidation, pro-oxidant enzym...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580369</comments>
            <pubDate>Fri, 04 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580369</guid>        </item>
        <item>
            <title>Thymoquinone ameliorates chemical induced oxidative stress and β-cell damage in experimental hyperglycemic rats.</title>
            <link>http://www.medworm.com/index.php?rid=4580368&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21382363%26dopt%3DAbstract</link>
            <description>Authors: Sankaranarayanan C, Pari L
    The present study was aimed to investigate the effect of thymoquinone (TQ) on pancreatic insulin levels, tissue antioxidant and lipid peroxidation (LPO) status in streptozotocin (STZ) nicotinamide (NA) induced diabetic rats. Diabetes was induced in experimental rats by a single intraperitoneal (i.p) injection of STZ (45mg/kg b.w) dissolved in 0.1mol/L citrate buffer (pH 4.5), 15minutes after the i.p administration of NA (110mg/kg b.w). Diabetic rats exhibited increased blood glucose with significant decrease in plasma insulin levels. The activities of antioxidant enzymes catalase (CAT), glutathione peroxidase (GPx), glutathione-S-transferase (GST) and the levels of low-molecular weight antioxidants Vitamin C, Vitamin E and reduced glutathione (GSH) w...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580368</comments>
            <pubDate>Fri, 04 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580368</guid>        </item>
        <item>
            <title>Induction of apoptosis in K562 cells by dicyclohexylammonium salt of hyperforin through a mitochondrial-related pathway.</title>
            <link>http://www.medworm.com/index.php?rid=4580376&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21376709%26dopt%3DAbstract</link>
            <description>Authors: Liu JY, Liu Z, Wang DM, Li MM, Wang SX, Wang R, Chen JP, Wang YF, Yang DP
    Hyperforin is an abundant phloroglucinol-type constituent isolated from the extract of the flowering upper portion of the plant Hypericum perforatum L. The dicyclohexylammonium salt of hyperforin (DCHA-HF) has exhibited antitumor and antiangiogenic activities in various cancer cells. Here, the antitumor effects of DCHA-HF on the chronic myeloid leukemia K562 cell line were investigated for the first time. DCHA-HF exhibited dose- and time-dependent inhibitory activities against K562 cells, with IC(50) values of 8.6 and 3.2μM for 48h and 72h of treatment, respectively, which was more effective than that of the hyperforin. In contrast, little cytotoxic activity was observed with DCHA-HF on HUVECs. DCHA-HF ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580376</comments>
            <pubDate>Wed, 02 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580376</guid>        </item>
        <item>
            <title>Aldose reductase deficiency protects sugar-induced lens opacification in rats.</title>
            <link>http://www.medworm.com/index.php?rid=4580375&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21376710%26dopt%3DAbstract</link>
            <description>Authors: Reddy AB, Tammali R, Mishra R, Srivastava S, Srivastava SK, Ramana KV
    Aldose reductase (AKR1B1), which catalyzes the reduction of glucose to sorbitol and lipid aldehydes to lipid alcohols, has been shown to be involved in secondary diabetic complications including cataractogenesis. Rats have high levels of AKR1B1 in lenses and readily develop diabetic cataracts, whereas mice have very low levels of AKR1B1 in their lenses and are not susceptible to hyperglycemic cataracts. Studies with transgenic mice that over-express AKR1B1 indicate that it is the key protein for the development of diabetic complications including diabetic cataract. However, no such studies were performed in genetically altered AKR1B1 rats. Hence, we developed siRNA-based AKR1B1 knockdown rats (ARKO) using th...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580375</comments>
            <pubDate>Wed, 02 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580375</guid>        </item>
        <item>
            <title>Cytotoxic molecular mechanisms and cytoprotection by enzymic metabolism for glyceraldehyde, hydroxypyruvate and glycolaldehyde.</title>
            <link>http://www.medworm.com/index.php?rid=4580374&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21376711%26dopt%3DAbstract</link>
            <description>Authors: Yang K, Feng C, Lip H, Bruce WR, O'Brien PJ
    Previously, we showed that dietary fructose or its carbonyl metabolites, glyceraldehyde and glycolaldehyde, could be oxidized by inflammatory reactive oxygen species (ROS), products of immune cells, to form highly toxic and genotoxic products, such as glyoxal. Glycolaldehyde-caused hepatocyte protein carbonylation likely resulted from glyoxal, an autoxidation product formed by ROS. Although hepatocyte protein carbonylation by glyoxal or D-glycolaldehyde was rapid, the product was unstable. Glyceraldehyde-induced protein carbonylation was slower and was also less cytotoxic. Non-toxic concentrations of H(2)O(2) were then used to mimic inflammation and oxidative stress associated with fructose-induced non-alcoholic steatohepatitis (NASH...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580374</comments>
            <pubDate>Wed, 02 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580374</guid>        </item>
        <item>
            <title>Effect of cryopreservation on the activity of OATP1B1/3 and OCT1 in isolated human hepatocytes.</title>
            <link>http://www.medworm.com/index.php?rid=4580378&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21356203%26dopt%3DAbstract</link>
            <description>In conclusion, the present study showed that cryopreserved human hepatocytes are useful tool to investigate hepatic uptake mediated by OATP1B1/3/SLCO1B1/3 or OCT1/SLC22A1, two of the most important hepatic uptake transporters.
    PMID: 21356203 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580378</comments>
            <pubDate>Sat, 26 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580378</guid>        </item>
        <item>
            <title>Reduced cytotoxicity of polyhexamethylene biguanide hydrochloride (PHMB) by egg phosphatidylcholine while maintaining antimicrobial efficacy.</title>
            <link>http://www.medworm.com/index.php?rid=4580377&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21356204%26dopt%3DAbstract</link>
            <description>Authors: Müller G, Kramer A, Schmitt J, Harden D, Koburger T
    Liposomes or oil-in-water emulsions containing egg yolk phosphatidylcholine (EPC) were combined with aqueous polyhexamethylene biguanide hydrochloride (PHMB). The bactericidal activity of these preparations against Pseudomonas aeruginosa and Staphylococcus aureus as well as their cytotoxicity on cultured murine fibroblasts (L929 cells) was then assayed for either 30min or 60min in the presence of cell culture medium containing 10% fetal bovine serum as surrogate for wound fluid. We used two assay designs: in the first bactericidal activity and cytotoxicity were determined in separate experiments; in the second both were determined in one experiment. Combining PHMB and EPC containing o/w emulsions or liposomes protects mammal...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580377</comments>
            <pubDate>Sat, 26 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580377</guid>        </item>
        <item>
            <title>In vitro kinetic interactions of DEET, pyridostigmine and organophosphorus pesticides with human cholinesterases.</title>
            <link>http://www.medworm.com/index.php?rid=4580380&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21354413%26dopt%3DAbstract</link>
            <description>In conclusion, the in vitro investigation of interactions between human cholinesterases, DEET, pyridostigmine, malaoxon and chlorpyrifos oxon showed a weak inhibition of hAChE and hBChE by DEET. The inhibitory potency of the tested cholinesterase inhibitors was not enhanced by DEET and it did not affect the regeneration velocity of pyridostigmine-inhibited AChE. Hence, this in vitro study does not give any evidence of a synergistic effect of the tested compounds on human cholinesterases.
    PMID: 21354413 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580380</comments>
            <pubDate>Fri, 25 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580380</guid>        </item>
        <item>
            <title>Effects of low molecular weight fungal compounds on inflammatory gene transcription and expression in mouse alveolar macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=4580379&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21356202%26dopt%3DAbstract</link>
            <description>In this study we evaluated the effect of pure fungal compounds on potentiating acute inflammatory response in primary mouse alveolar macrophages (AMs) and tested the hypothesis that AM responses to low molecular weight fungal compounds exhibit temporal and compound specificity that mimic that observed in the whole lung. Transcriptional responses of 13 inflammation/respiratory burst-associated genes (KC=Cxcl1, Cxcl2, Cxcl5, Cxcl10, Ccl3, Ccl112, Ccl20, IL-1β, Il-6, ifi27 Tnfα, iNOS and Blvrb) were evaluated in mouse AMs exposed to a 1ml (10(-8)mol) dose of either pure atranone C, brevianimide, cladosporin, curdlan, LPS, neoechinulin A &amp; B, sterigmatocystin or TMC-120A for 2h, 4h and 12h PE using customized reverse transcription (RT)-PCR based arrays. Multianalyte ELISA was used to mea...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580379</comments>
            <pubDate>Fri, 25 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580379</guid>        </item>
        <item>
            <title>Aldose reductase inhibition suppresses oxidative stress-induced inflammatory disorders.</title>
            <link>http://www.medworm.com/index.php?rid=4580382&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21354119%26dopt%3DAbstract</link>
            <description>Authors: Srivastava SK, Yadav UC, Reddy AB, Saxena A, Tammali R, Mohammad S, Ansari NH, Bhatnagar A, Petrash MJ, Srivastava S, Ramana KV
    Oxidative stress-induced inflammation is a major contributor to several disease conditions including sepsis, carcinogenesis and metastasis, diabetic complications, allergic asthma, uveitis and after cataract surgery posterior capsular opacification. Since reactive oxygen species (ROS)-mediated activation of redox-sensitive transcription factors and subsequent expression of inflammatory cytokines, chemokines and growth factors are characteristics of inflammatory disorders, we envisioned that by blocking the molecular signals of ROS that activate redox-sensitive transcription factors, various inflammatory diseases could be ameliorated. We have indeed de...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580382</comments>
            <pubDate>Thu, 24 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580382</guid>        </item>
        <item>
            <title>Overview of lipid peroxidation products and hepatic protein modification in alcoholic liver disease.</title>
            <link>http://www.medworm.com/index.php?rid=4580381&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21354120%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Inhibition of Hsp70, Hsp90 and PDI function could be involved in initiation of the early phases of ER stress contributing to stimulation and accumulation of hepatic lipids. Likewise, impairment of L-FABP activity could also disrupt lipid transport also contributing to steatosis. The modification and inhibition of Erk1/2 by 4-HNE may also contribute to the decreased hepatocellular proliferation associated with ALD. Collectively, these results provide new information concerning the mechanisms whereby the modification of hepatic proteins by 4-HNE contributes to ALD.
    PMID: 21354120 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580381</comments>
            <pubDate>Thu, 24 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580381</guid>        </item>
        <item>
            <title>Unusual space-time patterning of the fallon, Nevada leukemia cluster: Evidence of an infectious etiology.</title>
            <link>http://www.medworm.com/index.php?rid=4580383&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21352818%26dopt%3DAbstract</link>
            <description>We examined the temporal and spatial patterning of the leukemia case homes in comparison to the distribution of the general population at risk, other cancer incidence, and features of land use. Leukemia cases were predominantly diagnosed during the early to mid summer, exhibiting a seasonal bias. Leukemia cases lived outside of the &quot;developed/urban&quot; area of Fallon, predominantly in the &quot;agriculture/pasture&quot; region of Churchill County, circumscribing downtown Fallon. This pattern was different from the distribution of the underlying population (p-value&amp;lt;0.001) and different from the distribution of other cancers, which were evenly distributed when compared to the population (p-value=0.97). The unusual space-time patterning of childhood leukemia is consistent with the involvement of an inf...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580383</comments>
            <pubDate>Wed, 23 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580383</guid>        </item>
        <item>
            <title>Discovery of Novel Regulators of Aldehyde Dehydrogenase Isoenzymes.</title>
            <link>http://www.medworm.com/index.php?rid=4525714&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21349255%26dopt%3DAbstract</link>
            <description>Authors: Parajuli B, Kimble-Hill AC, Khanna M, Ivanova Y, Meroueh S, Hurley TD
    Over the past three years we have been involved in high-throughput screening in an effort to discover novel small molecular modulators of aldehyde dehydrogenase (ALDH) activity. In particular, we have been interested in both the activation and inhibitionof the three commonly studied isoenzymes, ALDH1A1, ALDH2 and ALDH3A1, as their distinct, yet overlapping substrate specificities, present a particularly difficult challenge for inhibitor discovery and design. Activation of ALDH2 has been shown to benefit cardiovascular outcome following periods of ischemia and renewed interest in specific inhibition of ALDH2 has application for alcohol aversion therapy, and more recently, in cocaine addiction. In contrast, in...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525714</comments>
            <pubDate>Mon, 21 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525714</guid>        </item>
        <item>
            <title>Alleviation of Iron Induced Oxidative Stress by the Grape Fruit Flavanone Naringin in Vitro.</title>
            <link>http://www.medworm.com/index.php?rid=4525715&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21345335%26dopt%3DAbstract</link>
            <description>Authors: Jagetia GC, Reddy TK
    Iron is an essential element that participates in several metabolic activities of cells, however excess iron is a major cause of iron-induced oxidative stress and several human diseases. The protective effect of naringin, a grape fruit flavanone was studied in iron overloaded isolated mouse liver mitochondria, where the isolated mitochondrial fraction was incubated with various concentrations of naringin before ferric ion loading. Iron overloading of mitochondrial fraction resulted in an increase in lipid peroxidation, protein oxidation, and DNA damage, whereas iron overload reduced the glutathione (GSH) concentration, glutathione-S-transferase (GST), glutathione peroxidase (GSHPx), catalase and superoxide dismutase (SOD) activities. Pretreatment of mitoch...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525715</comments>
            <pubDate>Sun, 20 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525715</guid>        </item>
        <item>
            <title>Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and oxidative stress induced cytotoxicity.</title>
            <link>http://www.medworm.com/index.php?rid=4525716&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21338592%26dopt%3DAbstract</link>
            <description>In conclusion, ALDH7A1 mechanistically appears to provide cells protection through multiple pathways including the removal of toxic LPO-derived aldehydes in addition to osmolyte generation.
    PMID: 21338592 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525716</comments>
            <pubDate>Fri, 18 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525716</guid>        </item>
        <item>
            <title>Gastroprotective potential of risperidone, an atypical antipsychotic, against stress and pyloric ligation induced gastric lesions.</title>
            <link>http://www.medworm.com/index.php?rid=4525728&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21315700%26dopt%3DAbstract</link>
            <description>Authors: Saxena B, Krishnamurthy S, Singh S
    Risperidone has been used in some stress disorders and may be potentially protective against stress-induced gastric lesions. Thus, the aim of the present study is to investigate, whether risperidone, a D(2) receptor and 5-HT(2A) receptor antagonist, would be able to result in gastroprotective effect in stress induced lesions and also explore the possible mechanism of action behind its gastroprotective activity. Gastroprotective activity of risperidone was evaluated both by single treatment and 21 days repeated (0.03, 0.1, 0.3 and 1mg/kg, p.o.) treatment in the cold restraint stress (CRS) model and 21 days repeated treatment in the pyloric ligation (PL) model and compared with that of sulpiride (D(2) receptor antagonist) and ketanserin (5-HT(2...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525728</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525728</guid>        </item>
        <item>
            <title>Involvement of P-glycoprotein and CYP 3A4 in the enhancement of etoposide bioavailability by a piperine analogue.</title>
            <link>http://www.medworm.com/index.php?rid=4525721&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21333639%26dopt%3DAbstract</link>
            <description>Authors: Najar IA, Sharma SC, Singh GD, Koul S, Gupta PN, Javed S, Johri RK
    Etoposide, a semi-synthetic derivative of podophyllotoxin, is widely used anticancer agent. Etoposide presents low bioavailability with wide inter-, and intra-patient variability after oral dosing. In an earlier study a piperine analogue, namely, 4-ethyl 5-(3, 4-methylenedioxyphenyl)-2E,4E-pentadienoic acid piperidide (PA-1), was shown to cause 2.32-fold enhancement of the absolute bioavailability of co-dosed etoposide in mice. In the present investigation a mechanistic evaluation was undertaken using various in vitro and animal-derived models. In everted rat gut sac studies PA-1 enhanced mucosal uptake of the drug while it inhibited efflux of Rh-123, a P-glycoprotein substrate from serosal-to-mucosal direction...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525721</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525721</guid>        </item>
        <item>
            <title>Aldose reductase inhibition suppresses airway inflammation.</title>
            <link>http://www.medworm.com/index.php?rid=4525719&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21334316%26dopt%3DAbstract</link>
            <description>Authors: Yadav UC, Ramana KV, Srivastava SK
    Airway inflammation induced by reactive oxygen species-mediated activation of redox-sensitive transcription factors is the hallmark of asthma, a prevalent chronic respiratory disease. In various cellular and animal models, we have recently demonstrated that, in response to multiple stimuli, aldose reductase (AKR1B1) regulates the inflammatory signals via NF-kappa B activation. Since NF-κB activation is implicated in asthma pathogenesis, we investigated whether AKR1B1 inhibition could prevent ovalbumin (Ova)- and ragweed pollen extract (RWE)-induced airway inflammation and hyper-responsiveness in mice models and tumor necrosis factor-alpha (TNF-α)-, lipopolysachharide (LPS)- and RWE-induced cytotoxic and inflammatory signals in primary human...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525719</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525719</guid>        </item>
        <item>
            <title>Differences in glyoxal and methylglyoxal metabolism determine cellular susceptibility to protein carbonylation and cytotoxicity.</title>
            <link>http://www.medworm.com/index.php?rid=4525718&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21334317%26dopt%3DAbstract</link>
            <description>Authors: Yang K, Qiang D, Delaney S, Mehta R, Bruce W, O'Brien PJ
    Chronic hyperglycemia in diabetic patients often leads to chronic side effects associated with protein glycation and the formation of reactive carbonyl species, such as methylglyoxal (MGO) and glyoxal (GO). We have shown that both MGO and GO carbonylated bovine serum albumin (BSA) in vitro to the same degree and similar stability. The carbonylated BSA formed initially could be a reversible Schiff base as the UV absorbance formed after the addition of 2,4-dinitrophenylhydrazine was decreased when sodium borohydride was added. MGO and GO also carbonylated hepatocyte protein rapidly with similar dose or time dependence. In contrast to BSA carbonylation, the amount of carbonylated proteins in hepatocytes decreased over time,...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525718</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525718</guid>        </item>
        <item>
            <title>Cafestol, a coffee-specific diterpene, induces apoptosis in renal carcinoma Caki cells through down-regulation of anti-apoptotic proteins and Akt phosphorylation.</title>
            <link>http://www.medworm.com/index.php?rid=4525717&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21334318%26dopt%3DAbstract</link>
            <description>Authors: Choi MJ, Park EJ, Oh JH, Min KJ, Yang ES, Kim YH, Lee TJ, Kim SH, Choi YH, Park JW, Kwon TK
    Cafestol, one of the major compounds in coffee beans, has been reported for its tumor cell growth inhibitory activity and anti-carcinogenic activity, although the mechanism of action is poorly understood. In the present study, we investigated the effect of cafestol on the apoptotic pathway in human renal Caki cells and other cancer cell lines. Cafestol treatment inhibited Caki cells viability a dose-dependent manner by inducing apoptosis, as evidenced by DNA fragmentation and the accumulation of sub-G1 phase. Cafestol-induced apoptosis is associated with the reduction of mitochondrial membrane potential (MMP), activation of caspase 3, cytochrome c release, and down-regulation of anti-ap...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525717</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525717</guid>        </item>
        <item>
            <title>Lipoic acid ameliorates arsenic trioxide-induced HO-1 expression and oxidative stress in THP-1 monocytes and macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=4525729&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21315065%26dopt%3DAbstract</link>
            <description>In conclusion, the cytotoxicity of arsenic trioxide is associated with an imbalance of the cellular redox state, and LA can protect cells from arsenic-induced malfunctions either through its reducing activity, direct interacting with arsenic or stimulating other unidentified signaling pathways.
    PMID: 21315065 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525729</comments>
            <pubDate>Wed, 16 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525729</guid>        </item>
        <item>
            <title>Benzene, the Exposome and Future Investigations of Leukemia Etiology.</title>
            <link>http://www.medworm.com/index.php?rid=4525720&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21333640%26dopt%3DAbstract</link>
            <description>Authors: Smith MT, Zhang L, McHale CM, Skibola CF, Rappaport SM
    Benzene exposure is associated with acute myeloid leukemia (AML), myelodysplastic syndromes (MDS), and probably lymphoma and childhood leukemia. Biological plausibility for a causal role of benzene in these diseases comes from its toxicity to hematopoietic stem cells (HSC) or progenitor cells, from which all leukemias and related disorders arise. The effect of this toxicity is manifest as lowered blood counts (hematotoxicity), even in individuals occupationally exposed to low levels of benzene. Benzene can induce AML/MDS via several well-characterized pathways associated with these diseases. Through its metabolites, benzene induces multiple alterations that likely contribute to the leukemogenic process, and appears to oper...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525720</comments>
            <pubDate>Wed, 16 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525720</guid>        </item>
        <item>
            <title>Human and rodent aldo-keto reductases from the AKR1B subfamily and their specificity with retinaldehyde.</title>
            <link>http://www.medworm.com/index.php?rid=4525727&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21329680%26dopt%3DAbstract</link>
            <description>Authors: Ruiz FX, Moro A, Gallego O, Ardèvol A, Rovira C, Petrash JM, Parés X, Farrés J
    NADP(H)-dependent cytosolic aldo-keto reductases (AKR) are mostly monomeric enzymes which fold into a typical (α/β)(8)-barrel structure. Substrate specificity and inhibitor selectivity are determined by interaction with residues located in three highly variable loops (A, B, and C). Based on sequence identity, AKR have been grouped into families, namely AKR1-AKR15, containing multiple subfamilies. Two human enzymes from the AKR1B subfamily (AKR1B1 and AKR1B10) are of special interest. AKR1B1 (aldose reductase) is related to secondary diabetic complications, while AKR1B10 is induced in cancer cells and is highly active with all-trans-retinaldehyde. Residues interacting with all-trans-retinaldehyd...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525727</comments>
            <pubDate>Tue, 15 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525727</guid>        </item>
        <item>
            <title>Aldose reductase-mediated induction of epithelium-to-mesenchymal transition (EMT) in lens.</title>
            <link>http://www.medworm.com/index.php?rid=4525725&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21329682%26dopt%3DAbstract</link>
            <description>Authors: Zablocki GJ, Ruzycki PA, Overturf MA, Palla S, Reddy GB, Petrash JM
    Cataract is a key factor in the morbidity associated with diabetes. While the pathogenesis of diabetic cataract formation is poorly understood, previous research has identified aldose reductase (ALR2) as a key player. To elucidate a potential role for this enzyme in diabetic cataract formation, we created a series of transgenic mice designed for expression of human ALR2 (AKR1B1) in epithelial and outer cortical fiber cells of the lens. One of the founder lines, designated PAR39, developed an early onset cataract that involved formation of a plaque of cells at the anterior aspect of the lens. These cells appear to separate from the anterior epithelium and undergo a dramatic change that is reminiscent of the epi...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525725</comments>
            <pubDate>Tue, 15 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525725</guid>        </item>
        <item>
            <title>Characterization of new medium-chain alcohol dehydrogenases adds resolution to duplications of the class I/III and the sub-class I genes.</title>
            <link>http://www.medworm.com/index.php?rid=4525724&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21329683%26dopt%3DAbstract</link>
            <description>Authors: Cederlund E, Hedlund J, Hjelmqvist L, Jonsson A, Shafqat J, Norin A, Keung WM, Persson B, Jörnvall H
    Four additional variants of alcohol and aldehyde dehydrogenases have been purified and functionally characterized, and their primary structures have been determined. The results allow conclusions about the structural and evolutionary relationships within the large family of MDR alcohol dehydrogenases from characterizations of the pigeon (Columba livia) and dogfish (Scyliorhinus canicula) major liver alcohol dehydrogenases. The pigeon enzyme turns out to be of class I type and the dogfish enzyme of class III type. This result gives a third type of evidence, based on purifications and enzyme characterization in lower vertebrates, that the classical liver alcohol dehydrogenase or...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525724</comments>
            <pubDate>Tue, 15 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525724</guid>        </item>
        <item>
            <title>Human aldo-keto reductases 1B1 and 1B10: A comparative study on their enzyme activity toward electrophilic carbonyl compounds.</title>
            <link>http://www.medworm.com/index.php?rid=4525723&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21329684%26dopt%3DAbstract</link>
            <description>This study evaluated in parallel the enzyme activity of 1B1 and 1B10 toward alpha, beta-unsaturated carbonyl compounds with cellular and dietary origins, including acrolein, crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, and trans-2,4-hexadienal. Our results showed that 1B10 had much better enzyme activity and turnover rates toward these chemicals than 1B1. By detecting the enzymatic products using high-performance liquid chromatography, we measured their activity to carbonyl compounds at low concentrations. Our data showed that 1B10 efficiently reduced the tested carbonyl compounds at physiological levels, but 1B1 was less effective. Ectopically expressed 1B10 in 293T cells effectively eliminated 4-hydroxynonenal at 5μM by reducing to 1,4-dihydroxynonene, whereas endogenously express...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525723</comments>
            <pubDate>Tue, 15 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525723</guid>        </item>
        <item>
            <title>The toxic effect of fluoride on MG-63 osteoblast cells is also dependent on the production of nitric oxide.</title>
            <link>http://www.medworm.com/index.php?rid=4525722&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21329685%26dopt%3DAbstract</link>
            <description>Authors: Bergandi L, Aina V, Malavasi G, Morterra C, Ghigo D
    Some soda-lime-phospho-silicate glasses, such as Hench's Bioglass(®) 45S5, form bone-like apatite on their surface when bound to living bone. To improve their osteointegration for clinical purposes, the fluoride insertion in their structure has been proposed, but we recently showed that fluoride causes oxidative damage in human MG-63 osteoblasts, via inhibition of pentose phosphate oxidative pathway (PPP) and its key enzyme glucose 6-phosphate dehydrogenase (G6PD). In the same cells we have now investigated the role of nitric oxide (NO) in these effects. Fluoride-containing bioactive glasses and NaF caused, as expected, release of lactate dehydrogenase in the extracellular medium, accumulation of intracellular malonyldialdeh...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525722</comments>
            <pubDate>Tue, 15 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525722</guid>        </item>
        <item>
            <title>Natural alcohol exposure: Is ethanol the main substrate for alcohol dehydrogenases in animals?</title>
            <link>http://www.medworm.com/index.php?rid=4525726&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21329681%26dopt%3DAbstract</link>
            <description>Authors: Hernández-Tobías A, Julián-Sánchez A, Piña E, Riveros-Rosas H
    Alcohol dehydrogenase (ADH) activity is widely distributed in all phyla. In animals, three non-homologous NAD(P)(+)-dependent ADH protein families are reported. These arose independently throughout evolution and possess different structures and mechanisms of reaction: type I (medium-chain) ADHs are zinc-containing enzymes and comprise the most studied group in vertebrates; type II (short-chain) ADHs lack metal cofactor and have been extensively studied in Drosophila, and type III ADHs are iron-dependent/-activated enzymes that were initially identified only in microorganisms. The presence of these different ADHs in animals has been assumed to be a consequence of chronic exposure to ethanol. By far the most comm...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525726</comments>
            <pubDate>Mon, 14 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525726</guid>        </item>
        <item>
            <title>Resveratrol ameliorates early diabetic nephropathy associated with suppression of augmented TGF-β/smad and ERK 1/2 signaling in streptozotocin-induced diabetic rats.</title>
            <link>http://www.medworm.com/index.php?rid=4471179&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21300041%26dopt%3DAbstract</link>
            <description>Authors: Chen KH, Hung CC, Hsu HH, Jing YH, Yang CW, Chen JK
    Diabetic nephropathy (DN) is the major cause of end-stage renal disease. The early changes in DN are characterized by an increased in kidney size, glomerular volume, and kidney function, followed by the accumulation of glomerular extracellular matrix, increased urinary albumin excretion (UAE), glomerular sclerosis, and tubular fibrosis. Resveratrol (RSV) has been shown to ameliorate hyperglycemia and hyperlipidemia in streptozotocin-induced diabetic rats. In the present study, we examined the beneficial effects of RSV on DN and explored the possible mechanism of RSV action. Male Sprague-Dawley rats were injected with streptozotocin at 65mg/kg body weight. The induction of diabetes mellitus (DM) was confirmed by a fasting plas...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471179</comments>
            <pubDate>Fri, 04 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471179</guid>        </item>
        <item>
            <title>Bioinformatic and Biochemical Characterization of DCXR and DHRS2/4 from Caenorhabditis elegans.</title>
            <link>http://www.medworm.com/index.php?rid=4471178&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21300042%26dopt%3DAbstract</link>
            <description>Authors: Kisiela M, El-Hawari Y, Martin HJ, Maser E
    Several reductases belonging to the large enzyme superfamily of the short-chain dehydrogenases/reductases (SDR) are involved in the reductive metabolism of carbonyl containing xenobiotics. In order to characterize the human enzymes dicarbonyl/L-xylulose reductase (DCXR), and dehydrogenase/reductase members 2 and 4 (DHRS2, DHRS4) in terms of metabolism of xenobiotics, orthologues from the model organism Caenorhabditis elegans (C. elegans) were identified by using hidden Markov models that were developed in the present study. Accordingly, we describe the characterization of proteins from C. elegans as orthologous to the human enzymes DCXR and DHRS2/4 using a combined approach of bioinformatic and biochemical methods. With the hidden Mar...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471178</comments>
            <pubDate>Fri, 04 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471178</guid>        </item>
        <item>
            <title>Catalytic reduction of carbonyl groups in oxidized PAPC by Kvβ2 (AKR6).</title>
            <link>http://www.medworm.com/index.php?rid=4471184&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21296056%26dopt%3DAbstract</link>
            <description>Authors: Xie Z, Barski OA, Cai J, Bhatnagar A, Tipparaju SM
    The β-subunits of the voltage-gated potassium channel (Kvβ) belong to the aldo-keto reductase superfamily. The Kvβ-subunits dock with the pore-forming Kv α-subunits and impart or accelerate the rate of inactivation in Kv channels. Inactivation of Kv currents by Kvβ is differentially regulated by oxidized and reduced pyridine nucleotides. In mammals, AKR6 family is comprised of 3 different genes Kvβ1-3. We have shown previously that Kvβ2 catalyzes the reduction of a broad range of carbonyls including aromatic carbonyls, electrophilic aldehydes and prostaglandins. However, the endogenous substrates for Kvβ have not been identified. To determine whether products of lipid oxidation are substrates of Kvβs, we tested the en...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471184</comments>
            <pubDate>Thu, 03 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471184</guid>        </item>
        <item>
            <title>Comparative studies of vertebrate aldehyde dehydrogenase 3: Sequences, structures, phylogeny and evolution. Evidence for a mammalian origin for the ALDH3A1 gene.</title>
            <link>http://www.medworm.com/index.php?rid=4471183&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21296057%26dopt%3DAbstract</link>
            <description>Authors: Holmes RS, Hempel J
    Mammalian ALDH3 genes (ALDH3A1, ALDH3A2, ALDH3B1 and ALDH3B2) encode enzymes of peroxidic and fatty aldehyde metabolism. ALDH3A1 also plays a major role in anterior eye tissue UV-filtration. BLAT and BLAST analyses were undertaken of several vertebrate genomes using rat, chicken and zebrafish ALDH3-like amino acid sequences. Predicted vertebrate ALDH3 sequences and structures were highly conserved, including residues involved in catalysis, coenzyme binding and enzyme structure as reported by Liu and coworkers (1997) for rat ALDH3A1. Phylogeny studies of human, rat, opossum, platypus, chicken, xenopus and zebrafish ALDH3-like sequences supported three hypotheses: (1) the mammalian ALDH3A1 gene was generated by a tandem duplication event of an ancestral verte...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471183</comments>
            <pubDate>Thu, 03 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471183</guid>        </item>
        <item>
            <title>Inactivation of porcine kidney betaine aldehyde dehydrogenase by hydrogen peroxide.</title>
            <link>http://www.medworm.com/index.php?rid=4471182&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21296058%26dopt%3DAbstract</link>
            <description>Authors: Rosas-Rodríguez JA, Valenzuela-Soto EM
    Concentrated urine formation in the kidney is accompanied by conditions that favor the accumulation of reactive oxygen species (ROS). Under hyperosmotic conditions, medulla cells accumulate glycine betaine, which is an osmolyte synthesized by betaine aldehyde dehydrogenase (BADH, EC 1.2.1.8). All BADHs identified to date have a highly reactive cysteine residue at the active site, and this cysteine is susceptible to oxidation by hydrogen peroxide. Porcine kidney BADH incubated with H(2)O(2) (0-500μM) lost 25% of its activity. However, pkBADH inactivation by hydrogen peroxide was limited, even after 120min of incubation. The presence of coenzyme NAD(+) (10-50μM) increased the extent of inactivation (60%) at 120min of reaction, but the li...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471182</comments>
            <pubDate>Thu, 03 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471182</guid>        </item>
        <item>
            <title>Optimizing preclinical study design in oncology research.</title>
            <link>http://www.medworm.com/index.php?rid=4471181&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21296059%26dopt%3DAbstract</link>
            <description>Authors: Wittenburg LA, Gustafson DL
    The current drug development pathway in oncology research has led to a large attrition rate for new drugs, in part due to a general lack of appropriate preclinical studies that are capable of accurately predicting efficacy and/or toxicity in the target population. Because of an obvious need for novel therapeutics in many types of cancer, new compounds are being investigated in human Phase I and Phase II clinical trials before a complete understanding of their toxicity and efficacy profiles is obtained. In fact, for newer targeted molecular agents that are often cytostatic in nature, the conventional preclinical evaluation used for traditional cytotoxic chemotherapies utilizing primary tumor shrinkage as an endpoint may not be appropriate. By utilizi...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471181</comments>
            <pubDate>Thu, 03 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471181</guid>        </item>
        <item>
            <title>Drosophila lacking a homologue of mammalian ALDH2 have multiple fitness defects.</title>
            <link>http://www.medworm.com/index.php?rid=4471180&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21296060%26dopt%3DAbstract</link>
            <description>Authors: Chakraborty M, Fry JD
    Little is known about the roles of aldehyde dehydrogenases in non-vertebrate animals. We recently showed that in Drosophila melanogaster, an enzyme with ∼70% amino acid identity to mammalian ALDH2 is necessary for detoxification of dietary ethanol. To investigate other functions of this enzyme, DmALDH, encoded by the gene Aldh, we compared two strains homozygous for Aldh-null mutations to two closely related wild type strains in measures of fitness and stress resistance in the absence of ethanol. Aldh-null strains have lower total reproductive rate, pre-adult viability, resistance to starvation, and possibly longevity than wild-type strains. When maintained under hyperoxia, Aldh nulls die more quickly and accumulate higher levels of protein carbonyls th...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471180</comments>
            <pubDate>Thu, 03 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471180</guid>        </item>
        <item>
            <title>Mammalian alcohol dehydrogenases - A comparative investigation at gene and protein levels.</title>
            <link>http://www.medworm.com/index.php?rid=4471185&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21291872%26dopt%3DAbstract</link>
            <description>Authors: Höög JO, Ostberg LJ
    Mammalian alcohol dehydrogenase (ADH) can be divided into six classes, ADH1-ADH6, according to primary structure and function, where the classes are further subdivided into isozymes and allelic forms. With the increasing amount of available genomic data a general pattern is possible to trace within the mammalian ADH gene and protein families. The transcriptional order for the ADH genes in all mammalian genomes is the same (ADH4-ADH1-ADH6-ADH5-ADH2-ADH3), but the cluster is found on different chromosomes in different species. However, in primates only ADH1-ADH5 are present, where the loss of ADH6 may have occurred simultaneously as the split into ADH1 isoforms. ADH3, also denoted glutathione-dependent formaldehyde dehydrogenase and S-nitrosoglutathione red...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471185</comments>
            <pubDate>Tue, 01 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471185</guid>        </item>
        <item>
            <title>Steroid degradation and two steroid-inducible enzymes in the marine bacterium H5.</title>
            <link>http://www.medworm.com/index.php?rid=4471186&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21281621%26dopt%3DAbstract</link>
            <description>Authors: Sang Y, Xiong G, Maser E
    Natural and synthetic steroid hormones excreted into the environment are potentially threatening the population dynamics of all kinds of animals and public health. We have previously isolated a steroid degrading bacterial strain (H5) from the Baltic Sea, at Kiel, Germany. 16S-rRNA analysis showed that bacterial strain H5 belongs to the genus Vibrio, family Vibrionaceae and class Gamma-Proteobacteria. Bacterial strain H5 can degrade steroids such as testosterone and estrogens, which was shown in this study by determining the (3)H labeled steroid retaining in the bacterial H5 culture medium at incubation times of 5h and 20h. Since 3α-hydroxysteroid dehydrogenase/carbonyl reductase (3α-HSD/CR) is a key enzyme in adaptive steroid degradation in Comamonas...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471186</comments>
            <pubDate>Mon, 31 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471186</guid>        </item>
        <item>
            <title>Regulation of aldo-keto reductase AKR1B10 gene expression: Involvement of transcription factor Nrf2.</title>
            <link>http://www.medworm.com/index.php?rid=4471187&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21277289%26dopt%3DAbstract</link>
            <description>In this study, we investigated the regulation of AKR1B10 expression. A -3282bp of the 5'-flanking fragment of AKR1B10 gene was isolated from A549 lung carcinoma cells. This region contains several putative regulatory motifs such as AP-1, NF-κB and antioxidant response element. In addition, a complex polymorphic microsatellite with repetitive sequences enriched with C and T was found. However, luciferase reporter assay revealed that the microsatellite polymorphism did not influence the basal promoter activity. We found that an antioxidant ethoxyquin induced the AKR1B10 expression based on RT-PCR analysis and luciferase reporter assay. Since ethoxyquin is known to activate the gene expression mediated through transcription factor Nrf2, the involvement of Nrf2 was examined. Forced expression...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471187</comments>
            <pubDate>Fri, 28 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471187</guid>        </item>
        <item>
            <title>Aldose reductase (AKR1B3) regulates the accumulation of advanced glycosylation end products (AGEs) and the expression of AGE receptor (RAGE).</title>
            <link>http://www.medworm.com/index.php?rid=4471194&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21276777%26dopt%3DAbstract</link>
            <description>Authors: Baba SP, Hellman J, Srivastava S, Bhatnagar A
    Diabetes results in enhanced chemical modification of proteins by advanced lipoxidation end products (ALEs) and advanced glycation end products (AGEs) precursors. These modifications have been linked to the development of several secondary diabetic complications. Our previous studies showed that aldose reductase (AR; AKR1B3) catalyzes the reduction of ALEs and AGEs precursors; however, the in vivo significance of this metabolic pathway during diabetes and obesity has not been fully assessed. Therefore we examined the role of AR in regulating ALEs and AGEs formation in murine models of diet-induced obesity and streptozotocin-induced diabetes. In comparison with wild-type and AR-null mice fed normal chow, mice fed a high-fat (HF) die...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471194</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471194</guid>        </item>
        <item>
            <title>Novel alkenal/one reductase activity of yeast NADPH:quinone reductase zta1p. Prospect of the functional role for the ζ-crystallin family.</title>
            <link>http://www.medworm.com/index.php?rid=4471193&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21276778%26dopt%3DAbstract</link>
            <description>Authors: Crosas E, Porté S, Moeini A, Farrés J, Biosca JA, Parés X, Fernández MR
    ζ-Crystallins are a Zn(2+)-lacking enzyme group with quinone reductase activity, which belongs to the medium-chain dehydrogenase/reductase superfamily. It has been recently observed that human ζ-crystallin is capable of reducing the α,β-double bond of alkenals and alkenones. Here we report that this activity is also shared by the homologous Zta1p enzyme from Saccharomyces cerevisiae. While the two enzymes show similar substrate specificity, human ζ-crystallin exhibits higher activity with lipid peroxidation products and Zta1p is more active with cinnamaldehyde. The presence of Zta1p has an in vivo protective effect on yeast strains exposed to the toxic substrate 3-penten-2-one. Analysis of ZTA1 ge...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471193</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471193</guid>        </item>
        <item>
            <title>Water-restraint stress enhances methamphetamine-induced cardiotoxicity.</title>
            <link>http://www.medworm.com/index.php?rid=4471192&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21276779%26dopt%3DAbstract</link>
            <description>Authors: Tomita M, Katsuyama H, Watanabe Y, Hidaka K, Yoshitome K, Miyaishi S, Ishikawa T, Shinone K, Nata M
    Methamphetamine (MAP) and stress both cause a variety of cardiovascular problems. Stress also increases stimulant drug-seeking or drug-taking behavior by both humans and animals. In addition to the physiological effects on circulation, metabolism, and excretion, stress affects subject's responses to stimulant drugs such as MAP. However, the mechanisms underlying the drug-stress interactions remain unknown. In the present study, we assessed the effects of stress on myocardial responses to MAP in mice. Mice were injected with MAP (30mg/kg) immediately before exposure to water-restraint stress (WRS), which has often been used as a stressor in animal experiments. The combination of ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471192</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471192</guid>        </item>
        <item>
            <title>NADH fluorescence lifetime analysis of the effect of magnesium ions on ALDH2.</title>
            <link>http://www.medworm.com/index.php?rid=4471191&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21276780%26dopt%3DAbstract</link>
            <description>Authors: Gonnella TP, Leedahl TS, Karlstad JP, Picklo MJ
    Aldehyde dehydrogenase 2 (ALDH2) catalyzes oxidation of toxic aldehydes to carboxylic acids. Physiologic levels of Mg(2+) ions influence ALDH2 activity in part by increasing NADH binding affinity. Traditional fluorescence measurements monitor the blue shift of the NADH fluorescence spectrum to study ALDH2-NADH interactions. By using time-resolved fluorescence spectroscopy, we have resolved the fluorescent lifetimes (τ) of free NADH (τ=0.4ns) and bound NADH (τ=6.0ns). We used this technique to investigate the effects of Mg(2+) on the ALDH2-NADH binding characteristics and enzyme catalysis. From the resolved free and bound NADH fluorescence signatures, the K(D) for NADH with ALDH2 ranged from 468μM to 12μM for Mg(2+) ion conce...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471191</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471191</guid>        </item>
        <item>
            <title>In vitro effects of active constituents and extracts of Orthosiphon stamineus on the activities of three major human cDNA-expressed cytochrome P450 enzymes.</title>
            <link>http://www.medworm.com/index.php?rid=4471190&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21276781%26dopt%3DAbstract</link>
            <description>Authors: Pan Y, Abd-Rashid BA, Ismail Z, Ismail R, Mak JW, Pook PC, Er HM, Ong CE
    Orthosiphon stamineus (OS) has been traditionally used to treat diabetes, kidney and urinary disorders, high blood pressure and bone or muscular pain. To assess the possibility of drug-herb interaction via interference of metabolism, effects of four OS extracts of different polarity and three active constituents (sinensetin, eupatorin and rosmarinic acid) on major human cDNA-expressed cytochrome P450 (CYP) enzymes were investigated. Three substrate-probe based high-performance liquid chromatography (HPLC) assays were established to serve as activity markers for CYP2C9, CYP2D6 and CYP3A4. Our results indicate that OS extracts and constituents exhibited differential modulatory effects on different CYPs. Whi...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471190</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471190</guid>        </item>
        <item>
            <title>Functional expression of novel human and murine AKR1B genes.</title>
            <link>http://www.medworm.com/index.php?rid=4471189&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21276782%26dopt%3DAbstract</link>
            <description>Authors: Salabei JK, Li XP, Petrash JM, Bhatnagar A, Barski OA
    The Aldo Keto Reductases (AKRs) are a superfamily of enzymes that catalyze the reduction of biogenic and xenobiotic aldehydes and ketones. AKR1B family has 2 known members in humans and 3 in rodents. Two novel gene loci, hereafter referred to as AKR1B15 in human and Akr1b16 in mouse have been predicted to exist within the AKR1B clusters. AKR1B15 displays 91% and 67% sequence identity with human genes AKR1B10 and AKR1B1, respectively while Akr1b16 shares 82-84% identity with murine Akr1b8 and Akr1b7. We tested the hypothesis that AKR1B15 and Akr1b16 genes are expressed as functional proteins in human and murine tissues, respectively. Using whole tissue mRNA, we were able to clone the full-length open reading frames for AKR1B...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471189</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471189</guid>        </item>
        <item>
            <title>Activities of aldo-keto reductase 1 enzymes on two inhaled corticosteroids: Implications for the pharmacological effects of inhaled corticosteroids.</title>
            <link>http://www.medworm.com/index.php?rid=4471188&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21276783%26dopt%3DAbstract</link>
            <description>In this study, the activities of these AKR1 enzymes on cortisol and two ICS compounds budesonide (BUD) and flunisolide (FLU) were investigated. It was found that the catalytic efficiency of AKR1D1 for the reduction of the double bond in cortisol was 4- and 10-fold higher than the catalytic efficiencies of AKR1D1 with FLU and BUD, respectively. This suggests that compared to cortisol, for which the 5β-reduction is a major metabolic pathway, a lower degree of systemic (hepatic) metabolism of BUD and FLU via AKR1D1 takes place. In addition, BUD potently inhibited AKR1D1 and AKR1C4, the key steroid metabolizing enzymes in liver, which may disrupt endogenous steroid hormone metabolism and thus contribute to BUD-induced systemic effects. Activities of AKR1C1-3 on cortisol and the two ICS compou...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471188</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471188</guid>        </item>
        <item>
            <title>The role of aldehyde reductase AKR1A1 in the metabolism of gamma-hydroxybutyrate in 1321N1 human astrocytoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=4471196&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21276435%26dopt%3DAbstract</link>
            <description>Authors: Alzeer S, Ellis EM
    The role of the aldehyde reductase AKR1A1 in the biosynthesis of gamma-hydroxybutyrate (GHB) has been investigated in cell lines using a specific double stranded siRNA designed to knock down expression of the enzyme. This enzyme, along with the aldo-keto reductase AKR7A2, has been proposed previously to be one of the major succinic semialdehyde reductases in brain. The AKR1A1 siRNA was introduced into the human astrocytoma cell line (1321N1) and AKR1A1 expression was monitored using quantitative reverse-transcriptase PCR and Western blots. Results show an 88% reduction in mRNA levels and a 94% reduction in AKR1A1 protein expression 72h after transfection with the siRNA. Aldehyde reductase activity was examined in silenced cells by following the aldehyde-depe...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471196</comments>
            <pubDate>Wed, 26 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471196</guid>        </item>
        <item>
            <title>Metabolic mechanisms of methanol/formaldehyde in isolated rat hepatocytes: Carbonyl-metabolizing enzymes versus oxidative stress.</title>
            <link>http://www.medworm.com/index.php?rid=4471195&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21276436%26dopt%3DAbstract</link>
            <description>Authors: Macallister SL, Choi J, Dedina L, O'Brien PJ
    Methanol (CH(3)OH), a common industrial solvent, is metabolized to toxic compounds by several enzymatic as well as free radical pathways. Identifying which process best enhances or prevents CH(3)OH-induced cytotoxicity could provide insight into the molecular basis for acute CH(3)OH-induced hepatoxicity. Metabolic pathways studied include those found in 1) an isolated hepatocyte system and 2) cell-free systems. Accelerated Cytotoxicity Mechanism Screening (ACMS) techniques demonstrated that CH(3)OH had little toxicity towards rat hepatocytes in 95% O(2), even at 2M concentration, whereas 50mM was the estimated LC(50) (2h) in 1% O(2), estimated to be the physiological concentration in the centrilobular region of the liver and also th...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471195</comments>
            <pubDate>Wed, 26 Jan 2011 00:00:00 +0100</pubDate>
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        <item>
            <title>Studies on reduction of s-nitrosoglutathione by human carbonyl reductases 1 and 3.</title>
            <link>http://www.medworm.com/index.php?rid=4402442&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21256830%26dopt%3DAbstract</link>
            <description>STUDIES ON REDUCTION OF S-NITROSOGLUTATHIONE BY HUMAN CARBONYL REDUCTASES 1 AND 3.
    Chem Biol Interact. 2011 Jan 20;
    Authors: Staab CA, Hartmanová T, El-Hawari Y, Ebert B, Kisiela M, Wsol V, Martin HJ, Maser E
    Human carbonyl reductases 1 and 3 (CBR1 and CBR3) are monomeric NADPH-dependent enzymes of the short-chain dehydrogenase/reductase superfamily. Despite 72% identity in primary structure they exhibit substantial differences in substrate specificity. Recently, the endogenous low molecular weight S-nitrosothiol S-nitrosoglutathione (GSNO) has been added to the broad substrate spectrum of CBR1. The current study initially addressed whether CBR3 could equally reduce GSNO which was not the case. Neither the introduction of residues which contribute to glutathione binding in CBR...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402442</comments>
            <pubDate>Thu, 20 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402442</guid>        </item>
        <item>
            <title>Hydroxyl containing seleno-imine compound exhibits improved anti-oxidant potential and does not inhibit thiol-containing enzymes.</title>
            <link>http://www.medworm.com/index.php?rid=4402441&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21256831%26dopt%3DAbstract</link>
            <description>This study reveals that an imine group close to selenium atom drastically enhances the catalytic activities in the aromatic thiol (PhSH) assay systems. The oxidation of biologically significant thiols reflects the toxicity of the compounds. However the present data showed that treatment with Compound A at 0, 10, 25 or 50mg/kg) was not associated with mortality or body weight loss. Similarly it did not inhibit α-ALA-D and Na(+1)/K(+1) ATPase (sulfhydryl group containing enzymes) activities after acute oral treatment; rather it enhanced non-protein thiols (NPSH) concentration. The Compound A did not cause any oxidative stress as measured by TBARS production in rat's tissue preparation. Our data also indicate that exposure to Compound A did not affect plasma transaminase activities or levels...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402441</comments>
            <pubDate>Thu, 20 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402441</guid>        </item>
        <item>
            <title>Withaferin A enhances radiation-induced apoptosis in Caki cells through induction of reactive oxygen species, Bcl-2 downregulation and Akt inhibition.</title>
            <link>http://www.medworm.com/index.php?rid=4402440&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21256832%26dopt%3DAbstract</link>
            <description>In this study, we investigated the effect of Wit A on radiation-induced apoptosis in human renal cancer cells (Caki cells). Our results showed that, compared with Wit A or radiation alone, the combination of both resulted in a significant enhancement of apoptosis, showing the increase in the cleavage of caspase-3 and PARP as well as sub-G1 cell population. In addition, reactive oxygen species (ROS) generation was correlated with the enhancement of radiation-induced apoptosis by Wit A. Wit A downregulated Bcl-2 protein levels and ectopic expression of Bcl-2 in Caki cells attenuated the apoptosis induced by Wit A plus radiation. Taken together, these results indicate that Wit A enhanced radiation-induced apoptosis in Caki cells through ROS generation, down-regulation of Bcl-2 and Akt dephosp...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402440</comments>
            <pubDate>Thu, 20 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402440</guid>        </item>
        <item>
            <title>Murine hepatic aldehyde dehydrogenase 1a1 is a major contributor to oxidation of aldehydes formed by lipid peroxidation.</title>
            <link>http://www.medworm.com/index.php?rid=4402443&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21256123%26dopt%3DAbstract</link>
            <description>Authors: Makia NL, Bojang P, Falkner KC, Conklin DJ, Prough RA
    Reactive lipid aldehydes are implicated in the pathogenesis of various oxidative stress-mediated diseases, including non-alcoholic steatohepatitis, atherosclerosis, Alzheimer's and cataract. In the present study, we sought to define which hepatic Aldh isoform plays a major role in detoxification of lipid-derived aldehydes, such as acrolein and HNE by enzyme kinetic and gene expression studies. The catalytic efficiencies for metabolism of acrolein by Aldh1a1 was comparable to that of Aldh3a1 (V(max)/K(m)=23). However, Aldh1a1 exhibits far higher affinity for acrolein (K(m)=23.2μM) compared to Aldh3a1 (K(m)=464μM). Aldh1a1 displays a 3-fold higher catalytic efficiency for HNE than Aldh3a1 (218 vs 69ml/min/mg). The endogenou...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402443</comments>
            <pubDate>Wed, 19 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402443</guid>        </item>
        <item>
            <title>Importance of Inverse Correlation Between ALDH3A1 and PPARγ in Tumor Cells and Tissue Regeneration.</title>
            <link>http://www.medworm.com/index.php?rid=4402444&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21251908%26dopt%3DAbstract</link>
            <description>In conclusion, through modulation of PPARγ or ALDH3A1, it may be possible to reduce cell proliferation in tumor cells or stimulate cell proliferation in normal cells during tissue regeneration.
    PMID: 21251908 [PubMed - as supplied by publisher] (Source: Chemico-Biological Interactions)</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402444</comments>
            <pubDate>Mon, 17 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402444</guid>        </item>
        <item>
            <title>ROS-Ca(2+) is associated with mitochondria permeability transition pore involved in surfactin-induced MCF-7 cells apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=4402446&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21241685%26dopt%3DAbstract</link>
            <description>Authors: Cao XH, Zhao SS, Liu DY, Wang Z, Niu LL, Hou LH, Wang CL
    The surfactin can inhibit proliferation and induce apoptosis in cancer cells. Moreover, surfactin can induce cell death in human breast cancer MCF-7 cells through mitochondrial pathway. However, the molecular mechanism involved in this pathway remains to be elucidated. Here, the reactive oxygen species (ROS) and Ca(2+) on mitochondria permeability transition pore (MPTP) activity, and MCF-7 cell apoptosis which induced by surfactin were investigated. It is found that surfactin evoked mitochondrial ROS generation, and the surfactin-induced cell death was prevented by N-acetylcysteine (NAC, an inhibitor of ROS). An increasing cytoplasmic Ca(2+) concentration was detected in surfactin-induced MCF-7 apoptosis, which was inhib...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402446</comments>
            <pubDate>Sat, 15 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402446</guid>        </item>
        <item>
            <title>Differentiation of human embryonic stem cells along a hepatic lineage.</title>
            <link>http://www.medworm.com/index.php?rid=4402445&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21241686%26dopt%3DAbstract</link>
            <description>Authors: Zamule SM, Coslo DM, Chen F, Omiecinski CJ
    The limited availability of hepatic tissue suitable for the treatment of liver disease and drug discovery research advances the generation of hepatic-like cells from alternative sources as a valuable approach. In this investigation we exploited a unique hepatic differentiation approach to generate hepatocyte-like cells from human embryonic stem cells (hESCs). hESCs were cultured for only 10 days on collagen substrate in highly defined and serum free hepatocyte media. The resulting cell populations exhibited hepatic cell-like morphology and were characterized with a variety of biological endpoint analyses. Real-time PCR analysis demonstrated that mRNA expression of the 'stemness' marker genes NANOG and alkaline phosphatase in the diffe...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402445</comments>
            <pubDate>Sat, 15 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402445</guid>        </item>
        <item>
            <title>Enzymatic properties of ALDH1L2, a mitochondrial 10-formyltetrahydrofolate dehydrogenase.</title>
            <link>http://www.medworm.com/index.php?rid=4402449&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21238436%26dopt%3DAbstract</link>
            <description>Authors: Strickland KC, Krupenko NI, Dubard ME, Hu CJ, Tsybovsky Y, Krupenko SA
    10-Formyltetrahydrofolate dehydrogenase (FDH, ALDH1L1), an abundant cytosolic enzyme of folate metabolism, shares significant sequence similarity with enzymes of the aldehyde dehydrogenase (ALDH) family. The enzyme converts 10-formyltetrahydrofolate (10-fTHF) to tetrahydrofolate and CO(2) in an NADP(+)-dependent manner. The mechanism of this reaction includes three consecutive steps with the final occurring in an ALDH-homologous domain. We have recently identified a mitochondrial isoform of FDH (mtFDH), which is the product of a separate gene, ALDH1L2. Its overall identity to cytosolic FDH is about 74%, and the identity between the ALDH domains rises up to 79%. In the present study, human mtFDH was expresse...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402449</comments>
            <pubDate>Fri, 14 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402449</guid>        </item>
        <item>
            <title>Advanced lipoxidation end-products.</title>
            <link>http://www.medworm.com/index.php?rid=4402448&amp;cid=s_34407_67_f&amp;fid=34407&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21238437%26dopt%3DAbstract</link>
            <description>Authors: Pamplona R
    Chemical and nonenzymatic molecular modifications induced by reactive carbonyl species (RCS) generated by peroxidation of membrane phospholipids acyl chains play a dual role as signaling molecules and as mediators of the aging process. Cytotoxic effects of RCS are due to their capacity to react with cellular constituents, forming advanced lipoxidation end-products (ALEs). Reactive carbonyl compounds are stable and can diffuse within or even escape from the cell and attack targets far from the site of formation. The consequent loss of function and structural integrity of modified biomolecules can have a wide range of downstream functional consequences and may be the cause of subsequent cellular dysfunctions and tissue damage.
    PMID: 21238437 [PubMed - as supplied ...</description>
            <author>Chemico-Biological Interactions</author>
            <type>journals</type>
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            <pubDate>Fri, 14 Jan 2011 00:00:00 +0100</pubDate>
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