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

• Published in: FEBS letters Vol. 476; no. 3; pp. 306 - 311
• Main Authors: Kitagawa, Kyoko, Kawamoto, Toshihiro, Kunugita, Naoki, Tsukiyama, Tadasuke, Okamoto, Kohji, Yoshida, Akira, Nakayama, Keiko, Nakayama, Kei-ichi
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 07.07.2000
• Subjects: 2-Methoxyethanol; Acetaldehyde - analogs & derivatives; Acetaldehyde - metabolism; Aldehyde Dehydrogenase - genetics; Aldehyde Dehydrogenase - metabolism; Aldehyde dehydrogenase 2; Aldehyde Dehydrogenase, Mitochondrial; Alleles; Animals; Base Sequence; DNA Primers - genetics; Female; Gene targeting mouse; Genotype; Humans; In Vitro Techniques; Liver - enzymology; Liver - metabolism; Male; Methoxyacetaldehyde; Mice; Mice, Inbred C57BL; Mice, Knockout; Oxidation-Reduction; Polymorphism, Genetic; Subcellular Fractions - enzymology; Subcellular Fractions - metabolism; Aldehyde dehydrogenase 2; Gene targeting mouse; 2-Methoxyethanol; Methoxyacetaldehyde

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 thre...