Tissue-specific expression and preliminary functional analysis of the 5' flanking regions of the human mitochondrial aldehyde dehydrogenase (ALDH2) gene.
Tissue-specific expression and preliminary functional analysis of the 5' flanking regions of the human mitochondrial aldehyde dehydrogenase (ALDH2) gene.
复制标题
人线粒体乙醛脱氢酶 (ALDH2) 基因 5 侧翼区域的组织特异性表达和初步功能分析。
DOI：
10.1007/978-1-4615-1965-2_16
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发表时间：
1995
影响因子：
--
通讯作者：
Crabb,DW
中科院分区：
文献类型：
--
作者：
Dipple,KM;Stewart,MJ;Crabb,DW
Mitochondrial aldehyde dehydrogenase (ALDH2) is a member of a large group of enzymes that catalyze the irreversible oxidation of aldehydes to carboxylic acids. The ALDH2 enzyme has a very low Km(<1 μM) for short aliphatic aldehydes such as acetaldehyde and propionaldehyde. In human beings, this isozyme appears to play a major role in the removal of acetaldehyde generated from the oxidation of ethanol. This conclusion is based on the study of individuals with a genetically determined deficiency in ALDH2 activity. Liver or hair root extracts from these individuals show the absence of the ALDH2 activity band on starch gels or isoelectric focusing gels (also known in the literature as the ALDH I or E2 band) (Haradaet al., 1980). The deficiency results from a point mutation that substitutes a lysine for glutamate at position 487 (Yoshidaet al., 1984; Crabbet al., 1989). Individuals with the deficient phenotype experience alcohol-induced flushing that is secondary to high levels of circulating acetaldehyde (Haradaet al., 1981; Enomotoet al., 1991b). This is commonly referred to as the Oriental alcohol flush reaction. Assays of liver extracts from individuals carrying a deficient allele have about half the aldehyde dehydrogenase activity of extracts from subjects without the deficiency (S.-J. Yin, personal communication). Thus, ALDH2 activity makes a major contribution to the total aldehyde oxidizing capacity of the liver.
