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Product of the Schistosoma mansoni Glutathione Peroxidase Gene is a Selenium ContainingPhospholipid Hydroperoxide Glutathione Peroxidase (PHGPx) Sharing MolecularWeight and Substrate Specificity WithIts Mammalian Counterpart
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作者 MATILDE MAIORINO RAYMOND PIERCE +2 位作者 AND LEOPOLD FLOHE (Dipartimento di Chimica Biologica, Universitd di Padova, Padova, Italy Reltion hote-parasite stratigies vaccinales, INSERM U167, Institut Pasteur, Lille Cedex, France Department of Physiological Chemistr 《Biomedical and Environmental Sciences》 SCIE CAS CSCD 1997年第2期209-213,共5页
In the blood fluke Schistosoma mansoni a functionally active, monomeric, phospholipid hydroperoxide glutathione peroxidase (PHGPx) has been purified and characterized. This enzyme contains a catalytically active selen... In the blood fluke Schistosoma mansoni a functionally active, monomeric, phospholipid hydroperoxide glutathione peroxidase (PHGPx) has been purified and characterized. This enzyme contains a catalytically active selenocysteine. The protein has been shown to be the product of a cloned gene, previously referred to as a glutathione peroxidase gene. S. mansoni PHGPx has been found 5 times more abundant in female than in male worm extract. As in vertebrate PHGPx, homology alignment indicates that the residues involved in the glutathione binding by the tetrameric cellular glutathione peroxidase are mutated in the S. mansoni enzyme. Thus, this aspect appears a landmark of the PHGPx-type of glutathione peroxidases,which might be of functional relevance 展开更多
关键词 Sharing MolecularWeight and Substrate Specificity WithIts Mammalian Counterpart gene Product of the Schistosoma mansoni Glutathione peroxidase gene is a Selenium ContainingPhospholipid Hydroperoxide Glutathione peroxidase PHGPX
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Expression and Chromosomal Mapping of Mouse Gpx2 Gene Encoding the Gastrointestinal Form of Glutathione Peroxidase, GPX-GI 被引量:5
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作者 FONG-FONG CHU R. STEVEN ESWORTHY +4 位作者 YE SHIH HO MARGIT BERMEISTER KRISTINE SWIDEREK AND ROSEMARY W. ELLIOTT(Department of Medical Oncology, City of Hope Midical Center, Duarte,CA91010, USA Department of Psychiatry and Human Genetics,Mintal Health Research 《Biomedical and Environmental Sciences》 SCIE CAS CSCD 1997年第2期156-162,共7页
GPX-GI is a cytosolic tetrameric Se-dependent glutathione peroxidase, similar in properties to GPX-1. Unlike the almost ubiquitous GPX-1, GPX-GI is mainly expressed in the epithelium of gastrointestinal tract. GPX-GI ... GPX-GI is a cytosolic tetrameric Se-dependent glutathione peroxidase, similar in properties to GPX-1. Unlike the almost ubiquitous GPX-1, GPX-GI is mainly expressed in the epithelium of gastrointestinal tract. GPX-GI contributes to at least fifty percent of GPX activity in rodent small intestmal epithelium. The total GPX activity consists of at least 70% of selenium-dependent GPX activity in this compartment.By analyzing a panel of mouse mterspecies DNA from the Jackson Laboratory's backcross resource,we mapped Gpx2 gene to mouse chromosome 12 between D12Mit4 and D12Mit5, near the Ccs1 locus which contains a colon cancer susceptibility gene. A pseudogene, Gpx2-ps is mapped to mouse chromosome 7.Comparison of Gpx2 gene expression in three pairs of C57BL/6Ha and ICR/Ha mice which are respectively resistant and sensitive to dimethylhydrazine-induced colon cancer, we found a higher Gpx2 mRNA level in C57BL/6Ha colon than ICR/Ha colon. Interestingly, a lower level of GPX activity is found in the resistant strain of mice. Because GPX-1 has three times higher specific activity than GPX GI, our data suggest that the decreased GPX activity may result from a higher level of Gpx2 gene expression in those cells co-express GPx1 gene 展开更多
关键词 GPX-GI GPx gene FORM Expression and Chromosomal Mapping of Mouse Gpx2 gene Encoding the Gastrointestinal Form of Glutathione peroxidase GI
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