Fas-induced caspase denitrosylation.
Published
Journal Article
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.
Full Text
Duke Authors
Cited Authors
- Mannick, JB; Hausladen, A; Liu, L; Hess, DT; Zeng, M; Miao, QX; Kane, LS; Gow, AJ; Stamler, JS
Published Date
- April 23, 1999
Published In
Volume / Issue
- 284 / 5414
Start / End Page
- 651 - 654
PubMed ID
- 10213689
Pubmed Central ID
- 10213689
International Standard Serial Number (ISSN)
- 0036-8075
Digital Object Identifier (DOI)
- 10.1126/science.284.5414.651
Language
- eng
Conference Location
- United States