Ethanol feeding can produce secondary alterations in aldehyde dehydrogenase isozymes

Jeffrey A. Alderman, Charles Sanny, Ellen Gordon, Charles S. Lieber

Research output: Contribution to journalArticle

7 Citations (Scopus)

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 Km for 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.

Original languageEnglish
Pages (from-to)91-95
Number of pages5
JournalAlcohol
Volume2
Issue number1
DOIs
StatePublished - 1 Jan 1985

Fingerprint

Aldehyde Dehydrogenase
alcoholism
Isoenzymes
Ethanol
animal
Papio
deficit
Alcoholics
Primates
Rats
Animals
Disulfiram
Acetaldehyde
Liver
Isoelectric Focusing
Nutrition
Cytosol
Rodentia
Animal Models
Carbohydrates

Keywords

  • Aldehyde dehydrogenase (ALDH)
  • Isozymes
  • Primary
  • Secondary

Cite this

Alderman, Jeffrey A. ; Sanny, Charles ; Gordon, Ellen ; Lieber, Charles S. / Ethanol feeding can produce secondary alterations in aldehyde dehydrogenase isozymes. In: Alcohol. 1985 ; Vol. 2, No. 1. pp. 91-95.
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Ethanol feeding can produce secondary alterations in aldehyde dehydrogenase isozymes. / Alderman, Jeffrey A.; Sanny, Charles; Gordon, Ellen; Lieber, Charles S.

In: Alcohol, Vol. 2, No. 1, 01.01.1985, p. 91-95.

Research output: Contribution to journalArticle

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AB - 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 Km for 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.

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