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Inactivation of cytosolic aldehyde dehydrogenase via S ‐nitrosylation in ethanol‐exposed rat liver
Author(s) -
Moon Kwan-Hoon,
Abdelmegeed Mohamed A.,
Song Byoung-Joon
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.037
Subject(s) - acetaldehyde , aldehyde dehydrogenase , aldh2 , ethanol , chemistry , dithiothreitol , biochemistry , s nitrosylation , alcohol dehydrogenase , cytosol , ethanol metabolism , nitrosylation , catalase , microbiology and biotechnology , enzyme , nitric oxide , biology , cysteine , organic chemistry
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 μM) 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.