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Gene. 1997 Oct 1;198(1-2):245-9.

Cloning and sequencing of the mouse cDNA encoding a phospholipid hydroperoxide glutathione peroxidase.

Author information

1
Department of Veterinary Anatomy, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Japan. aa47126@hongo.ecc.u-tokyo.ac.jp

Abstract

Phospholipid hydroperoxide glutathione peroxidase (PHGPx), a selenoprotein, reduces the hydroperoxides of phospholipid, cholesterol, and cholesteryl ester in biomembranes. In this study, a full-length cDNA clone encoding the PHGPx was isolated from mouse testes using a RACE (rapid amplification of cDNA ends) technique. According to sequence analysis, the cDNA encodes a polypeptide of 197 amino acids (aa) that initiates the translation at ATG(145-147) and contains an inframe TGA selenocysteine codon. It also has selenocysteine insertion sequences in the 3'-UTR that are involved in the insertion of selenocysteine at an opal codon. Moreover, the mouse PHGPx contains the active-site residues Gln108 and Trp163 that interact with selenocysteine, and the N-terminal 27-aa residues that may act as a potential mitochondrial targeting signal. According to the deduced aa analysis, mouse PHGPx shares a high level of aa identity with pig (93.4%), human (92.9%), and rat (98%) PHGPxs. However, the PHGPx mRNA particularly showed a high degree of expression in testis. This suggests that the PHGPx in testis may have more than just an antioxidant function.

PMID:
9370288
DOI:
10.1016/s0378-1119(97)00321-1
[Indexed for MEDLINE]

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