Metabolic Regulation and Function of Glutathione Peroxidase-1

Annual Review of Nutrition - Tập 27 Số 1 - Trang 41-61 - 2007
Xin Gen Lei1, Wen‐Hsing Cheng2, James P. McClung3
1Department of Animal Science, Cornell University, Ithaca, New York 14853
2Laboratory of Molecular Gerontology, National Institute on Aging, National Institutes of Health, Baltimore, Maryland 21224, and Department of Nutrition and Food Science, University of Maryland, College Park, Maryland 20742
3Military Nutrition Division, U.S. Army Research Institute of Environmental Medicine, Natick, Massachusetts 01760

Tóm tắt

Glutathione peroxidase-1 (GPX1) represents the first identified mammalian selenoprotein, and our understanding in the metabolic regulation and function of this abundant selenoenzyme has greatly advanced during the past decade. Selenocysteine insertion sequence–associating factors, adenosine, and Abl and Arg tyrosine kinases are potent, Se-independent regulators of GPX1 gene, protein, and activity. Overwhelming evidences have been generated using the GPX1 knockout and transgenic mice for the in vivo protective role of GPX1 in coping with oxidative injury and death mediated by reactive oxygen species. However, GPX1 exerts an intriguing dual role in reactive nitrogen species (RNS)-related oxidative stress. Strikingly, knockout of GPX1 rendered mice resistant to toxicities of drugs including acetaminophen and kainic acid, known as RNS inducers. Intracellular and tissue levels of GPX1 activity affect apoptotic signaling pathway, protein kinase phosphorylation, and oxidant-mediated activation of NFκB. Data are accumulating to link alteration or abnormality of GPX1 expression to etiology of cancer, cardiovascular disease, neurodegeneration, autoimmune disease, and diabetes. Future research should focus on the mechanism of GPX1 in the pathogeneses and potential applications of GPX1 manipulation in the treatment of these disorders.

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Annual Review of Nutrition

Tập 27 Số 1

41-61

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