| First Author | Nam S | Year | 1997 |
| Journal | Gene | Volume | 198 |
| Issue | 1-2 | Pages | 245-9 |
| PubMed ID | 9370288 | Mgi Jnum | J:43287 |
| Mgi Id | MGI:1097467 | Doi | 10.1016/s0378-1119(97)00321-1 |
| Citation | Nam S, et al. (1997) Cloning and sequencing of the mouse cDNA encoding a phospholipid hydroperoxide glutathione peroxidase. Gene 198(1-2):245-9 |
| abstractText | 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. |
