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J Biol Chem, Vol. 274, Issue 14, 9427-9430, April 2, 1999
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From the S-Nitrosylation of protein thiol
groups by nitric oxide (NO) is a widely recognized protein
modification. In this study we show that nitrosonium tetrafluoroborate
(BF4NO), a NO+ donor, modified the thiol groups
of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by
S-nitrosylation and caused enzyme inhibition. The resultant
protein-S-nitrosothiol was found to be unstable and to
decompose spontaneously, thereby restoring enzyme activity. In
contrast, the NO-releasing compound S-nitrosoglutathione
(GSNO) promoted S-glutathionylation of a thiol group of
GAPDH both in vitro and under cellular conditions. The
GSH-mixed protein disulfide formed led to a permanent enzyme
inhibition, but upon dithiothreitol addition a functional active GAPDH
was recovered. This S-glutathionylation is specific for
GSNO because GSH itself was unable to produce protein-mixed disulfides.
During cellular nitrosative stress, the production of intracellular
GSNO might channel signaling responses to form protein-mixed disulfide
that can regulate intracellular function.
Molecular Cardiovascular Research Center,
Case Western Reserve University School of Medicine and the University
Hospitals of Cleveland, Cleveland, Ohio 44106-4958, the
§ Department of Cell Biology, Cleveland Clinic Foundation,
Cleveland, Ohio 44195, and the ¶ Faculty of Medicine, Department
of Medicine IV-Experimental Division, University of
Erlangen-Nürnberg, 91054 Erlangen, Germany
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