TY - JOUR
T1 - Aldehyde dehydrogenase (ALDH) 2 associates with oxidation of methoxyacetaldehyde; in vitro analysis with liver subcellular fraction derived from human and Aldh2 gene targeting mouse
AU - Kitagawa, Kyoko
AU - Kawamoto, Toshihiro
AU - Kunugita, Naoki
AU - Tsukiyama, Tadasuke
AU - Okamoto, Kohji
AU - Yoshida, Akira
AU - Nakayama, Keiko
AU - Nakayama, Kei Ichi
N1 - Funding Information:
We are very grateful to Dr. Gary L. Foreman (Hazardous Pollutant Assessment Group, National Center for Environmental Assessment, U.S. Environmental Protection Agency) for his useful discussion and editorial advice and Yukari Yamada, Ai Hori, Tomohiro Uehara and Kayo Honda for their technical assistance. This work was supported by a Grant-in-Aid for Encouragement of Young Scientists from The Ministry of Education, Science, Sports and Culture of Japan.
PY - 2000/7/7
Y1 - 2000/7/7
N2 - 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 ALDH2 genotypes and Aldh2 knockout mice, which were generated in this study. The activity was distributed in mitochondrial fractions of ALDH2*1/*1 and wild type (Aldh2+/+) mice but not ALDH2*1/*2, *2/*2 subjects or Aldh2 homozygous mutant (Aldh2-/-) mice. These data suggest that ALDH2 is a key enzyme for MALD oxidation and ME susceptibility may be influenced by the ALDH2 genotype. Copyright (C) 2000 Federation of European Biochemical Societies.
AB - 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 ALDH2 genotypes and Aldh2 knockout mice, which were generated in this study. The activity was distributed in mitochondrial fractions of ALDH2*1/*1 and wild type (Aldh2+/+) mice but not ALDH2*1/*2, *2/*2 subjects or Aldh2 homozygous mutant (Aldh2-/-) mice. These data suggest that ALDH2 is a key enzyme for MALD oxidation and ME susceptibility may be influenced by the ALDH2 genotype. Copyright (C) 2000 Federation of European Biochemical Societies.
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U2 - 10.1016/S0014-5793(00)01710-5
DO - 10.1016/S0014-5793(00)01710-5
M3 - Article
C2 - 10913633
AN - SCOPUS:0034617452
SN - 0014-5793
VL - 476
SP - 306
EP - 311
JO - FEBS Letters
JF - FEBS Letters
IS - 3
ER -