RGD Reference Report - Inactivation of cytosolic aldehyde dehydrogenase via S-nitrosylation in ethanol-exposed rat liver. - Rat Genome Database

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

Authors: Moon, KH  Abdelmegeed, MA  Song, BJ 
Citation: Moon KH, etal., FEBS Lett. 2007 Aug 21;581(21):3967-72. Epub 2007 Jul 25.
RGD ID: 2306319
Pubmed: PMID:17673211   (View Abstract at PubMed)
PMCID: PMC2693367   (View Article at PubMed Central)
DOI: DOI:10.1016/j.febslet.2007.07.037   (Journal Full-text)

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-Km value (11-18 microM) 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.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
response to ethanol  IDA 2306319 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Aldh1a1  (aldehyde dehydrogenase 1 family, member A1)


Additional Information