Alcohol induced histone acetylation mediated by histone acetyl transferase GCN5 in liver

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Alcohol induced histone acetylation mediated by histone acetyl transferase GCN5 in liver

Please use this identifier to cite or link to this item: http://hdl.handle.net/10355/6866

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dc.contributor.advisor Shukla, Shivendra D. en_US
dc.contributor.author Choudhury, Mahua, 1977- en_US
dc.date.accessioned 2010-04-19T14:39:22Z
dc.date.available 2010-04-19T14:39:22Z
dc.date.issued 2008 en_US
dc.date.submitted 2008 Summer en_US
dc.identifier.other ChoudhuryM-110509-D11715 en_US
dc.identifier.uri http://hdl.handle.net/10355/6866
dc.description The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. en_US
dc.description Title from PDF of title page (University of Missouri--Columbia, viewed on April 6, 2010). en_US
dc.description Includes bibliographical references en_US
dc.description Vita. en_US
dc.description Thesis advisor: Shivendra D. Shukla. en_US
dc.description "August 2008" en_US
dc.description Ph. D. University of Missouri-Columbia 2008. en_US
dc.description Dissertations, Academic -- University of Missouri--Columbia -- physiology (Medicine). en_US
dc.description.abstract Although several mechanisms have identified for alcoholic liver disease, at present there are no precise mechanisms for liver injury. We have observed that surrogate alcohols increases histone H3 acetylation selectively at Lys 9 (H3AcK9) via metabolites in primary rat hepatocytes. Alcohols and metabolites both increased the HAT activity. However, propionate and butyrate also decreased HDAC activity. In addition, oxidative stress also mediates ethanol induced histone acetylation and ADH1 gene expression. It is likely that both NADPH oxidase and mitochondria derived ROS are involved. The study presented here also identifies for the first time the specific HAT, GCN5, responsible for ethanol induced H3AcK9 in human hepatoma cell overexpressing ADH1 (VA-13). siRNA knock down of GCN5 decreased both ethanol induced H3AcK9 and HAT activity. In summery, we conclude that ethanol increases H3AcK9 via modulation of GCN5 in the liver. These original findings may contribute to a better understanding of the mechanism underlying the pathogenesis of alcoholic liver disease. en_US
dc.format.extent xv, 181 pages en_US
dc.language.iso en_US en_US
dc.publisher University of Missouri--Columbia en_US
dc.relation.ispartof 2008 Freely available dissertations (MU) en_US
dc.subject.lcsh Alcoholic liver diseases en_US
dc.subject.lcsh Histones -- Metabolism en_US
dc.subject.lcsh Histones -- Effect of drugs on en_US
dc.subject.lcsh Acetyltransferases en_US
dc.subject.lcsh Alcohols -- Receptors -- Effect of drugs on en_US
dc.subject.lcsh Histone deacetylase -- Metabolism en_US
dc.subject.mesh Liver Diseases, Alcoholic -- etiology en_US
dc.subject.mesh Histones -- metabolism en_US
dc.subject.mesh Histones -- drug effects en_US
dc.subject.mesh Histone Acetyltransferases en_US
dc.subject.mesh Alcohols -- pharmacology en_US
dc.subject.mesh Histone Deacetylases -- metabolism en_US
dc.title Alcohol induced histone acetylation mediated by histone acetyl transferase GCN5 in liver en_US
dc.type Thesis en_US
thesis.degree.discipline Physiology (Medicine) en_US
thesis.degree.grantor University of Missouri--Columbia en_US
thesis.degree.name Ph. D. en_US
thesis.degree.level Doctoral en_US
dc.identifier.oclc 603557930 en_US
dc.relation.ispartofcommunity University of Missouri-Columbia. Graduate School. Theses and Dissertations. Dissertations. 2008 Dissertations


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