TY - JOUR
T1 - Design and characterization of an active site selective caspase-3 transnitrosating agent.
AU - Mitchell, Douglas A.
AU - Morton, Sarah U.
AU - Marletta, Michael A.
PY - 2006/11/21
Y1 - 2006/11/21
N2 - 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.
AB - 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.
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U2 - 10.1021/cb600393x
DO - 10.1021/cb600393x
M3 - Article
C2 - 17168570
AN - SCOPUS:34250734460
SN - 1554-8929
VL - 1
SP - 659
EP - 665
JO - ACS chemical biology
JF - ACS chemical biology
IS - 10
ER -