Aldehyde dehydrogenase (ALDH) 2 associates with oxidation of methoxyacetaldehyde; in vitro analysis with liver subcellular fraction derived from human and <i>Aldh2</i> gene targeting mouse

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公開日
2000-07-03
権利情報
  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1016/s0014-5793(00)01710-5
公開者
Wiley

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説明

<jats:p>A principal pathway of 2‐methoxyethanol (ME) metabolism is to the toxic oxidative product, methoxyacetaldehyde (MALD). To assess the role of aldehyde dehydrogenase (ALDH) in MALD metabolism, in vitro MALD oxidation was examined with liver subcellular fractions from Japanese subjects who carried three different <jats:italic>ALDH2</jats:italic> genotypes and <jats:italic>Aldh2</jats:italic> knockout mice, which were generated in this study. The activity was distributed in mitochondrial fractions of <jats:italic>ALDH2*1/*1</jats:italic> and wild type (<jats:italic>Aldh2</jats:italic>+/+) mice but not <jats:italic>ALDH2*1/*2</jats:italic>, <jats:italic>*2/*2</jats:italic> subjects or <jats:italic>Aldh2</jats:italic> homozygous mutant (<jats:italic>Aldh2</jats:italic>−/−) mice. These data suggest that ALDH2 is a key enzyme for MALD oxidation and ME susceptibility may be influenced by the <jats:italic>ALDH2</jats:italic> genotype.</jats:p>

収録刊行物

  • FEBS Letters

    FEBS Letters 476 (3), 306-311, 2000-07-03

    Wiley

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