A proteomic analysis of liver after ethanol binge in chronically ethanol treated rats
العنوان: | A proteomic analysis of liver after ethanol binge in chronically ethanol treated rats |
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المؤلفون: | Lowery J Roy, Annayya R. Aroor, Shivendra D. Shukla, Brian P. Mooney, Ricardo J. Restrepo |
المصدر: | Proteome Science, Vol 10, Iss 1, p 29 (2012) Proteome Science |
بيانات النشر: | BMC, 2012. |
سنة النشر: | 2012 |
مصطلحات موضوعية: | medicine.medical_specialty, medicine.disease_cause, Biochemistry, chemistry.chemical_compound, Western blot, Internal medicine, Glutamine synthetase, medicine, Binge ethanol, Liver proteomics, lcsh:QH573-671, Molecular Biology, Liver injury, Ethanol, medicine.diagnostic_test, business.industry, lcsh:Cytology, Research, Chronic ethanol, CYP2E1, medicine.disease, Biotechnology, Endocrinology, chemistry, Steatosis, business, Carbonic anhydrase 3, Oxidative stress |
الوصف: | Background Binge ethanol in rats after chronic ethanol exposure augments necrosis and steatosis in the liver. In this study, two-dimensional gel electrophoresis proteomic profiles of liver of control, chronic ethanol, control-binge, and chronic ethanol- binge were compared. Results The proteomic analysis identified changes in protein abundance among the groups. The levels of carbonic anhydrase 3 (CA3) were decreased after chronic ethanol and decreased further after chronic ethanol-binge. Ethanol binge alone in control rats had no effect on this protein suggesting its possible role in increased susceptibility to injury by binge after chonic ethanol treatment. A protein spot, in which both cytosolic isocitrate dehydrogenase (IDH1) and glutamine synthetase (GS) were identified, showed a small decrease after chronic ethanol binge but western blot demonstrated significant decrease only for glutamine synthetase in chronic ethanol treated rats. The level of gluathione S-transferase mu isoform (GSTM1) increased after chronic ethanol but was lower after chronic ethanol-binge compared to chronic ethanol treatment. The protein levels of the basic form of protein disulfide isomerase associated protein 3 (PDIA3) were significantly decreased and the acidic forms were increased after chronic ethanol- binge but not in chronic ethanol treated rats or ethanol binge in control rats. The significant changes in proteome profile in chronic ethanol binge were accompanied by a marked increase in liver injury as evidenced by enhanced steatosis, necrosis, increased 4-hydroxynonenal labeled proteins, CYP2E1 expression, and decreased histone H2AX phosphorylation. Conclusions Given the role of CA3, IDH1 and GST in oxidative stress; PDIA3 in protein quality control, apoptosis and DNA repair and decreased glutamine synthetase as a sensitive marker of pericentral liver injury this proteome study of chronic ethanol-binge rat model identifies these proteins for the first time as molecular targets with potential role in progression of liver injury by binge ethanol drinking. |
اللغة: | English |
تدمد: | 1477-5956 |
الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c3b31d0074d6ceaf8a2c3b1773d3bf9Test https://doaj.org/article/a3d99570e5a7445cbe8df5d422dbf9dfTest |
حقوق: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....3c3b31d0074d6ceaf8a2c3b1773d3bf9 |
قاعدة البيانات: | OpenAIRE |
تدمد: | 14775956 |
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