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

Kyoko Kitagawa; Toshihiro Kawamoto; Naoki Kunugita; Tadasuke Tsukiyama; Kohji Okamoto; Akira Yoshida; Keiko Nakayama; Kei Ichi Nakayama

doi:10.1016/S0014-5793(00)01710-5

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

Kyoko Kitagawa, Toshihiro Kawamoto, Naoki Kunugita, Tadasuke Tsukiyama, Kohji Okamoto, Akira Yoshida, Keiko Nakayama, Kei Ichi Nakayama

Research output: Contribution to journal › Article › peer-review

117 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	306-311
Number of pages	6
Journal	FEBS Letters
Volume	476
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(00)01710-5
Publication status	Published - 2000 Jul 7
Externally published	Yes

Keywords

2-Methoxyethanol
Aldehyde dehydrogenase 2
Gene targeting mouse
Methoxyacetaldehyde

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(00)01710-5

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Kitagawa, K., Kawamoto, T., Kunugita, N., Tsukiyama, T., Okamoto, K., Yoshida, A., Nakayama, K., & Nakayama, K. I. (2000). Aldehyde dehydrogenase (ALDH) 2 associates with oxidation of methoxyacetaldehyde; in vitro analysis with liver subcellular fraction derived from human and Aldh2 gene targeting mouse. FEBS Letters, 476(3), 306-311. https://doi.org/10.1016/S0014-5793(00)01710-5

Aldehyde dehydrogenase (ALDH) 2 associates with oxidation of methoxyacetaldehyde; in vitro analysis with liver subcellular fraction derived from human and Aldh2 gene targeting mouse. / Kitagawa, Kyoko; Kawamoto, Toshihiro; Kunugita, Naoki; Tsukiyama, Tadasuke; Okamoto, Kohji; Yoshida, Akira; Nakayama, Keiko; Nakayama, Kei Ichi.

In: FEBS Letters, Vol. 476, No. 3, 07.07.2000, p. 306-311.

Research output: Contribution to journal › Article › peer-review

Kitagawa, K, Kawamoto, T, Kunugita, N, Tsukiyama, T, Okamoto, K, Yoshida, A, Nakayama, K & Nakayama, KI 2000, 'Aldehyde dehydrogenase (ALDH) 2 associates with oxidation of methoxyacetaldehyde; in vitro analysis with liver subcellular fraction derived from human and Aldh2 gene targeting mouse', FEBS Letters, vol. 476, no. 3, pp. 306-311. https://doi.org/10.1016/S0014-5793(00)01710-5

Kitagawa, Kyoko ; Kawamoto, Toshihiro ; Kunugita, Naoki ; Tsukiyama, Tadasuke ; Okamoto, Kohji ; Yoshida, Akira ; Nakayama, Keiko ; Nakayama, Kei Ichi. / Aldehyde dehydrogenase (ALDH) 2 associates with oxidation of methoxyacetaldehyde; in vitro analysis with liver subcellular fraction derived from human and Aldh2 gene targeting mouse. In: FEBS Letters. 2000 ; Vol. 476, No. 3. pp. 306-311.

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abstract = "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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