On the mechanism of ethanol-induced fatty liver and its reversibility by adenosine☆
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Involvement of cell oxidant status and redox state in the increased non-enzymatic ethanol oxidation by the regenerating rat liver
2019, Biochemical PharmacologyCitation Excerpt :Mitochondrial and cytosolic activities of aspartate aminotransferase (AST; EC 2.6.1.1), as well as that of malate dehydrogenase (MDH; EC 1.1.1.27), were determined as described elsewhere [28]. In the same acid extracts, neutralized with 4 mol • L−1 K2CO3, the redox-pair metabolites: lactate, pyruvate, α-glycerophosphate, dihydroxyacetone phosphate, β-hydroxybutyrate, and acetoacetate, were enzymatically determined, as described before [29,30]. The amount of aldehydic products generated by lipid peroxidation was quantified in the cytosolic fraction through the technique using the thiobarbituric acid reaction (TBARS), as previously modified [31].
Catalase increases ethanol oxidation through the purine catabolism in rat liver
2017, Biochemical PharmacologyCitation Excerpt :However, it becomes evident that given the appropriate stimulation, catalase can compete with and even overtake the NAD-dependent metabolism of ethanol. Even though we determined the mechanism through which adenosine stimulates the oxidation of ethanol, the results from this study have no resemblance to those previously reported [7,8]. It was found that adenosine was able to maintain the normal cytoplasmic redox state (NAD/NADH ratio) in the presence of ethanol, which was accompanied by an increased activity of both the malate-aspartate and the α-glycerophosphate shuttles.
An Adenosine Derivative Compound as a Hepatoprotective Agent
2017, Liver Pathophysiology: Therapies and Antioxidants<sup>31</sup>P-NMR spectroscopy of perifused rat hepatocytes immobilized in agarose threads: application to chemical-induced hepatotoxicity
1992, BBA - Molecular Basis of Disease
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This research was partially supported by Grant PNCB 0044 from the Consejo Nacional de Ciencia y Tecnología.