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Papers In Press, published online ahead of print September 18, 2001
Animal Science, Cornell University, Ithaca, NY 14853
Corresponding Author: XL20{at}cornell.edu
Oxidative injuries including apoptosis can be induced by reactive oxygen species (ROS) and reactive nitrogen species (RNS) in aerobic metabolism. We determined impacts of a selenium-dependent glutathione peroxidase-1 (GPX1) on apoptosis induced by diquat (DQ), a ROS (superoxide) generator, and peroxynitrite (PN), a potent RNS. Hepatocytes were isolated from GPX1 knockout (GPX1-/-) or wild-type (WT) mice, and treated with 0.5 mM DQ or 0.1 to 0.8 mM PN for up to 12 h. Loss of cell viability, high levels of apoptotic cells, and severe DNA fragmentation were produced by DQ in only GPX1-/- cells and by PN in only WT cells. These two groups of cells shared similar cytochrome c release, caspase-3 activation, and p21WAF1/CIP1 cleavage. Higher levels of protein nitration were induced by PN in WT than GPX1-/- cells. Much less and(or) slower cellular GSH depletion was caused by DQ or PN in GPX1-/- than in WT cells, and corresponding GSSG accumulation occurred only in the latter. In conclusion, it is most striking that while GPX1 protects against apoptosis induced by superoxide-generator DQ, the enzyme actually promotes apoptosis induced by PN in murine hepatocytes. Indeed, GSH is a physiological substrate for GPX1 in coping with ROS in these cells.
J. Biol. Chem, 10.1074/jbc.M106946200
Submitted on July 23, 2001
Revised on September 14, 2001
Accepted on September 17, 2001
Opposite Roles of Selenium-Dependent Glutathione Peroxidase-1 in Superoxide Generator Diquat- and Peroxynitrite-Induced Apoptosis and Signaling
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