Fas-induced caspase denitrosylation

Joan B. Mannick, Alfred Hausladen, Limin Liu, Douglas T. Hess, Ming Zeng, Qian X. Miao, Laurie S. Kane, Andrew J. Gow, Jonathan S. Stamler

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Only a few intracellular S-nitrosylated proteins have been identified, and it is unknown if protein 5-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 tines 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.

Original languageEnglish
Pages (from-to)651-654
Number of pages4
Issue number5414
Publication statusPublished - 23 Apr 1999
Externally publishedYes

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    Mannick, J. B., Hausladen, A., Liu, L., Hess, D. T., Zeng, M., Miao, Q. X., Kane, L. S., Gow, A. J., & Stamler, J. S. (1999). Fas-induced caspase denitrosylation. Science, 284(5414), 651-654. https://doi.org/10.1126/science.284.5414.651