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Department of Pediatrics, Stanford University School of Medicine, Palo Alto, California 94305
Extracellular glutathione peroxidase (EGPx) is
a glycosylated selenoprotein capable of reducing hydrogen peroxide,
organic hydroperoxides, free fatty acid hydroperoxides, and
phosphatidylcholine hydroperoxides. We found that human large
intestinal explant cultures synthesize EGPx and cellular glutathione
peroxidase (CGPx) and secrete EGPx. The level of EGPx mRNA
expression relative to
-tubulin was similar throughout the mouse
gastrointestinal tract. EGPx mRNA transcripts have been localized to
mature absorptive epithelial cells in human and mouse large intestine.
Western blot analysis of mouse intestinal protein has demonstrated the
presence of EGPx protein in the small intestine, cecum, and large
intestine, with the highest protein levels found in the cecum.
Immunohistochemistry studies of human large intestine and mouse small
and large intestine sections demonstrated the presence of EGPx protein
within mature absorptive epithelial cells. In human large intestine and
mouse small intestine, EGPx protein is also present in the
extracellular milieu. These results suggest a role for EGPx in
protection of the intestinal tract from peroxidative damage
and/or in intercellular metabolism of peroxides.
antioxidant; epithelial cells; oxidative damage; peroxides; selenium
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