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Cloning of the mouse phospholipid hydroperoxide glutathione peroxidase gene 1
Author(s) -
Borchert Astrid,
Schnurr Kerstin,
Thiele Bernd J,
Kühn Hartmut
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00221-5
Subject(s) - phospholipid hydroperoxide glutathione peroxidase , microbiology and biotechnology , complementary dna , gene , glutathione peroxidase , biochemistry , genomic library , biology , intron , exon , gene expression , gpx3 , gpx4 , cdna library , cloning (programming) , chemistry , glutathione , enzyme , peptide sequence , computer science , programming language
15‐Lipoxygenases and phospholipid hydroperoxide glutathione peroxidases (PH‐GPx) are counterparts in the metabolism of hydroperoxy lipids and a balanced regulation of both enzymes appears to be important for the cellular peroxide tone regulating the expression of redox sensitive genes. In contrast to lipoxygenases the molecular biology of PH‐GPx is less well investigated. In this study we cloned the PH‐GPx cDNA from a mouse fibroblast cDNA library and the PH‐GPx gene from a mouse genomic library. The gene spans approximately 4 kb which includes 1 kb of 5′‐flanking region and consists of seven exons and six introns. The immediate promoter region does not contain a TATA box but there are binding sites for several transcription factors which also occur in the porcine gene. Our investigations provide useful tools for future targeted gene disruption studies.