Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of leptin on liver alcohol dehydrogenase (ADH) was determined in male rats. Administration of one or three daily doses of leptin (1microg/g of body weight intraperitoneally) increased ADH activity. Leptin enhanced ADH synthesis without an effect on ADH degradation. Leptin did not change ADH mRNA, indicating that the effect of leptin in enhancing ADH occurs at the post-transcriptional level. Leptin increased eukaryotic initiation factor (eIF) 2alpha, eIF2B activity, and the eIF4E-eIF4G complex, while it decreased the inhibitory complex of eIF4E with the eIF4E-binding protein-1 (4E-BP1). Leptin increased mammalian target of rapamycin (mTor) that phosphorylates 4E-BP1. In conclusion, leptin increases liver ADH activity and ADH protein due to an increase in synthesis which occurs at the post-transcriptional level. The effect of leptin in enhancing translational initiating factors may be of significance in the regulation not only of ADH but also of many other proteins.
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PMID:Effect of leptin on liver alcohol dehydrogenase. 1623 69

Acute alcohol intoxication leads to an inhibition of protein synthesis in heart that results in part through altered phosphorylation of protein factors controlling mRNA translation initiation. The purpose of the present set of experiments was designed to examine the effects of inhibitors of ethanol metabolism on the phosphorylation of 4E-binding protein (4EBP1) and S6k1(Thr(389)), two factors regulating mRNA translation initiation. Phosphorylation of 4E-BP1, S6k1(Thr(389)), and Erk 1/2 was reduced 2 h following IP injection of alcohol. Pretreatment with 4-methylpyrazole (4-MP), an inhibitor of alcohol dehydrogenase (ADH), did not attenuate the ethanol-induced decrease in phosphorylation of 4EBP1 and S6k1(Thr(389)). In contrast, 4-MP prevented the decrease in Erk 1/2 phosphorylation observed with acute ethanol intoxication. Pretreatment with cyanamide, an inhibitor of aldehyde dehydrogenase, did not attenuate the ethanol-induced decrease in phosphorylation S6k1(Thr(389)), but partially prevented the ethanol-induced lowering of 4EBP1 phosphorylation. The studies indicate that modulation of ethanol metabolism through inhibition of ADH or aldehyde dehydrogenase leads to preferential modulation of the phosphorylation of distinct myocardial signaling systems involved in regulating protein synthesis.
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PMID:Differential phosphorylation of translation initiation regulators 4EBP1, S6k1, and Erk 1/2 following inhibition of alcohol metabolism in mouse heart. 1831 50