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Functions of GI‐GPx: Lessons from selenium‐dependent expression and intracellular localization
Author(s) -
BrigeliusFlohé R.,
Müller C.,
Menard J.,
Florian S.,
Schmehl K.,
Wingler K.
Publication year - 2001
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.5520140114
Subject(s) - selenium , glutathione peroxidase , intracellular , selenium deficiency , apoptosis , messenger rna , peroxidase , microbiology and biotechnology , gastrointestinal tract , gpx1 , biology , chemistry , antioxidant , biochemistry , enzyme , catalase , gene , organic chemistry
Gastro intestinal glutathione peroxidase (GI‐GPx) is one of the four distinct mammalian selenoperoxidases. It had been reported to be restricted to the gastrointestinal tract but has more recently been identified also in human liver and some tumor cell lines. GI‐GPx ranks high in the hierarchy of selenoproteins. The GI‐GPx mRNA rather increases than decreases in selenium deficiency. GI‐GPx protein responds poorly to selenium deprivation and increases fast upon resupplementation. Putative biological roles of GI‐GPx, e.g. protection against food‐born hydroperoxides, redox‐regulation of proliferation or apoptosis, and modulation of mucosal immunity, are discussed in the light of cellular and subcellular distribution, transcriptional regulation and observations with k.o. mice.