Fas-induced caspase denitrosylation.

Journal Article (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


  • eng

Conference Location

  • United States