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ACS Chem Biol. 2006 Nov 21;1(10):659-65.

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

Author information

1
Department of Chemistry, University of California, Berkeley, California 94720-1460, USA.

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.

PMID:
17168570
DOI:
10.1021/cb600393x
[Indexed for MEDLINE]

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