Inactivation of cytosolic aldehyde dehydrogenase via S-nitrosylation in ethanol-exposed rat liver

被引：42

作者：

Moon, Kwan-Hoon ^{[1
]}

Abdelmegeed, Mohamed A. ^{[1
]}

Song, Byoung-Joon ^{[1
]}

机构：

[1] NIAAA, NIH, Lab Membrane Biochem & Biophys, Bethesda, MD 20892 USA

来源：

FEBS LETTERS | 2007年 / 581卷 / 21期

关键词：

cytosolic aldehyde dehydrogenase (ALDH1); ethanol; s-nitrosylation; reversible inhibition; acetaldehyde metabolism;

D O I：

10.1016/j.febslet.2007.07.037

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Aldehyde dehydrogenase (ALDH) isozymes are critically important in the metabolism of acetaldehyde, thus preventing its accumulation after ethanol-exposure. We previously reported that mitochondrial ALDH2 could be inactivated via S-nitrosylation in ethanol-exposed rats. This study was aimed at investigating whether cytosolic ALDH1, with a relatively-low-K-m value (11-18 mu M) for acetaldehyde, could be also inhibited in ethanol-exposed rats. Chronic or binge ethanol-exposure significantly decreased ALDH1 activity, which was restored by addition of dithiothreitol. Immunoblot analysis with the anti-S-nitroso-Cys antibody showed one immunoreactive band in the immunoprecipitated ALDH1 only from ethanol-exposed rats, but not from pair-fed controls, suggesting S-nitrosylation of ALDH1. Therefore inactivation of ALDH1 via S-nitrosylation can result in accumulation of acetaldehyde upon ethanol-exposure. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：3967 / 3972

页数：6

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