Ethanol feeding can produce secondary alterations in aldehyde dehydrogenase isozymes

7Citations
Citations of this article
2Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Depressed hepatic aldehyde dehydrogenase (ALDH) activity levels have been observed in alcoholics, but whether the deficit is primary or secondary in nature remains controversial. In this study, we examined liver ALDH in rodent (rat) and primate (baboon) animal models pair-fed nutritionally adequate ethanol or isocaloric carbohydrate containing liquid diets. Both species show qualitative changes in ALDH isozymes after ethanol consumption. The changes include alterations in isozyme patterns seen upon electrofocusing and decreased responsiveness to the ALDH inhibitor, disulfiram. The subcellular locus of most of the changes is cytosolic in the baboon and mitochondrial in the rat. Study of partially purified (enriched) baboon cytosolic ALDH confirmed changes seen in the original cytosols and kinetic characterization of the enriched enzyme revealed a 9-fold higher Kmfor acetaldehyde in ALDH from an ethanol treated animal. We note that qualitative and quantitative changes secondary to ethanol treatment in the primate model closely parallel those described in human alcoholics. © 1985.

Cite

CITATION STYLE

APA

Alderman, J. A., Sanny, C., Gordon, E., & Lieber, C. S. (1985). Ethanol feeding can produce secondary alterations in aldehyde dehydrogenase isozymes. Alcohol, 2(1), 91–95. https://doi.org/10.1016/0741-8329(85)90022-9

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free