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Fas-Induced Caspase Denitrosylation

Science  23 Apr 1999:
Vol. 284, Issue 5414, pp. 651-654
DOI: 10.1126/science.284.5414.651

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Abstract

Only a few intracellular S-nitrosylated proteins have been identified, and it is unknown if protein S-nitrosylation/denitrosylation is a component of signal transduction cascades. Caspase-3 zymogens were found to be S-nitrosylated on their catalytic-site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway. Decreased caspase-3 S-nitrosylation was associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active-site thiol. Protein S-nitrosylation/denitrosylation can thus serve as a regulatory process in signal transduction pathways.

  • * To whom correspondence should be addressed. E-mail: (J.S.S.) staml001{at}mc.duke.edu and (J.B.M.) Joan_mannick{at}dfci.harvard.edu

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