Tissue distribution, molecular cloning, and gene expression of cytosolic glutathione peroxidase in Japanese monkey.
Cytosolic glutathione peroxidase (GPX-1) is an important antioxidant enzyme that scavange hydrogen peroxide in mammalian cells. The level of GPX-1 activity in Japanese monkey (Macaca fuscata) tissues was determined and it was found to be high in the liver, kidney, and adrenal gland followed by the small intestine. We also cloned the GPX-1 cDNA that included the whole protein-coding region. The active-site selenocysteine was assumed to be encoded by a TGA codon. Compared to the GPX-1s of other mammalian species, essential residues in catalysis were well conserved in monkey GPX-1. Amino acid substitutions were frequent in the N- and C-terminal regions which are less essential in catalysis. Expression of GPX-1 mRNA was found to be high in the liver, kidney, and adrenal gland, in consistence with the tissue distribution of GPX-1 activity.
Fukuhara
Ryoji
R
Center for Human Evolution Modeling Research, Primate Research Institute, Kyoto University, Japan. fukuhara@pri.kyoto-u.ac.jp
Kageyama
Takashi
T
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D003600:Cytosol / Q000201:enzymology*; D017931:DNA Primers; D015870:Gene Expression; D005979:Glutathione Peroxidase / Q000235:genetics* / Q000378:metabolism*; D007564:Japan; D008251:Macaca / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D010802:Phylogeny
D017931:DNA Primers; D005979:Glutathione Peroxidase