Human hepatic alcohol and aldehyde dehydrogenases: genetic polymorphism and activities.

C T Yao, C S Liao, S J Yin
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Abstract

Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are the major enzymes responsible for the metabolism of ethanol in the body. Both exhibit genetic polymorphism in racial populations. To determine hepatic ethanol metabolizing activities in relation to genetic polymorphism, a total of 23 surgical specimens were investigated. The expression patterns of ADH and ALDH isoenzymes were identified by means of agarose isoelectric focusing, and the activities were assayed spectrophotometrically. At 33 mM ethanol, pH 7.5, the activities in the liver with the homozygous phenotype ADH2 1-1 and ADH2 2-2 and the heterozygous phenotype ADH2 1-2 were determined to be 2.9 +/- 0.7, 16.0 +/- 2.5, and 13.6 +/- 1.0 U/g tissue, respectively. The activities of the ALDH2-active and ALDH2-inactive phenotypes at 200 microM acetaldehyde were determined to be 1.06 +/- 0.13 and 0.71 +/- 0.07 U/g tissue, respectively. These findings indicate that human hepatic ethanol-metabolizing activities differ significantly with respect to polymorphism at both the ADH2 and ALDH2 loci. The results suggest that this genetically determined differential hepatic activity may influence drinking behavior and the development of alcoholism among Orientals.

人肝酒精和醛脱氢酶:基因多态性和活性。
醇脱氢酶(ADH)和醛脱氢酶(ALDH)是体内乙醇代谢的主要酶。两者在种族群体中都表现出基因多态性。为了确定肝脏乙醇代谢活性与遗传多态性的关系,共研究了23例手术标本。琼脂糖等电聚焦法鉴定ADH和ALDH同工酶的表达规律,分光光度法测定其活性。在33 mM乙醇、pH 7.5条件下,纯合型ADH2 1-1、ADH2 2-2和杂合型ADH2 1-2的肝脏组织活性分别为2.9 +/- 0.7、16.0 +/- 2.5和13.6 +/- 1.0 U/g。在200 μ m乙醛条件下,aldh2活性型和aldh2无活性型的组织活性分别为1.06 +/- 0.13和0.71 +/- 0.07 U/g。这些发现表明,人肝脏乙醇代谢活性在ADH2和ALDH2位点的多态性方面存在显著差异。结果表明,这种由基因决定的肝脏活动差异可能影响东方人的饮酒行为和酒精中毒的发展。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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