title: Cellular glutathione peroxidase as a predominant scavenger of hydroperoxyeicosatetraenoic acids in rabbit alveolar macrophages.
abstract: The cytosol of rabbit lung alveolar macrophages contains a high amount of peroxidase, which reduces 5-hydroperoxyeicosatetraenoic acid (5-HPETE) to 5-hydroxyeicosatetraenoic acid (5-HETE) in the presence of glutathione. This peroxidase was purified 69-fold to homogeneity with overall recovery of activity of 18.5%. The molecular mass of the enzyme was approximately 80 kDa by gel filtration, and emerged as a single band at 23.1 kDa under reducing condition by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The amino-terminal sequence of the purified peroxidase was completely identical to the sequence deduced from cellular glutathione peroxidase (cGPx) gene of rabbit liver. No other activity that reduces 5-HPETE to 5-HETE was observed during purification. These results suggest that cGPx plays an important role in metabolism of lipid hydroperoxides, especially HPETE, in lung alveolar macrophages.
authors.affiliation: Japan Energy Research Center Co., Ltd., Tokyo.
authors.forename: N
authors.initials: N
authors.lastname: Chiba
authors.forename: H
authors.initials: H
authors.lastname: Imai
authors.forename: K
authors.initials: K
authors.lastname: Narashima
authors.forename: M
authors.initials: M
authors.lastname: Arai
authors.forename: G
authors.initials: G
authors.lastname: Oshima
authors.forename: M
authors.initials: M
authors.lastname: Kunimoto
authors.forename: Y
authors.initials: Y
authors.lastname: Nakagawa
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D005979:Glutathione Peroxidase / Q000378:metabolism*; D066298:In Vitro Techniques; D015289:Leukotrienes / Q000378:metabolism*; D016676:Macrophages, Alveolar / Q000201:enzymology* / Q000378:metabolism; D008969:Molecular Sequence Data; D011817:Rabbits; D017421:Sequence Analysis
chemical_list: D015289:Leukotrienes; C047629:8-hydroperoxyeicosatetraenoic acid; D005979:Glutathione Peroxidase