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- Title
Fas-induced caspase denitrosylation.
- Authors
Mannick, J B; Hausladen, A; Liu, L; Hess, D T; Zeng, M; Miao, Q X; Kane, L S; Gow, A J; Stamler, J S
- 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.
- Publication
Science (New York, N.Y.), 1999, Vol 284, Issue 5414, p651
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.284.5414.651