Design and characterization of an active site selective caspase-3 transnitrosating agent.

Douglas A. Mitchell, Sarah U. Morton, Michael A. Marletta

Research output: Contribution to journalArticlepeer-review

Abstract

The oxidative addition of nitric oxide (NO) to a thiol, S-nitrosation, is a focus of studies on cyclic guanosine monophosphate (cGMP)-independent NO signaling. S-Nitrosation of the catalytic cysteine of the caspase proteases has important effects on apoptosis and consequently has received attention. Here we report on a small molecule that can directly probe the effects of S-nitrosation on the caspase cascade. This chemical tool is capable of permeating the mammalian cell membrane, selectively transnitrosating the caspase-3 active site cysteine, and halting apoptosis in cultured human T-cells. The efficacy of this reagent was compared with the commonly used reagent S-nitrosoglutathione and an esterified derivative.

Original languageEnglish (US)
Pages (from-to)659-665
Number of pages7
JournalACS chemical biology
Volume1
Issue number10
DOIs
StatePublished - Nov 21 2006
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine

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