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J. Biol. Chem., Vol. 276, Issue 31, 29596-29602, August 3, 2001
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§,¶,,,
From the Oxidative stress may cause tissue
injury through activation of the precursors of matrix metalloproteinase
(proMMPs). In this study, we observed glutathione
(GSH)-dependent proMMP activation induced by peroxynitrite,
a potent oxidizing agent formed during inflammatory processes.
Peroxynitrite strongly activated all three types of purified human
proMMPs (proMMP-1, -8, and -9) in the presence of similar
concentrations of GSH. Of the potential reaction products between
peroxynitrite and GSH, only S-nitroglutathione (GSNO2) caused proMMP activation. Extensive
S-glutathiolation of the proMMP protein occurred during
activation of proMMP by peroxynitrite and GSH, as shown by
radiolabeling studies with [35S]GSH or
[3H]GSH. Evidence of appreciable
S-glutathiolation persisted even after dithiothreitol and
protein-denaturing treatment, however, suggesting that some
S-glutathiolation did not occur through formation of simple
mixed disulfide. Matrix-assisted laser-desorption
ionization-time-of-flight mass spectrometry indicated that not only
peroxynitrite plus GSH but also synthetic GSNO2 produced
dithiothreitol-resistant S-glutathiolation of the synthetic
peptide PRCGVPD, which is a well conserved Cys-containing sequence of
the propeptide autoinhibitory domain of proMMPs. PRCGVPD S-glutathiolation is presumed to be formed through
glutathione disulfide S-oxide (GS(O)SR), based on the
m/z 1064. Our results illustrate a unique mechanism of
oxidative proMMP activation and oxidative tissue injury during inflammation.
Department of Microbiology, Kumamoto
University School of Medicine, Kumamoto 860-0811, Japan and the
§ Division of Pulmonary/Critical Care Medicine, Department
of Internal Medicine, School of Medicine, University of California,
Davis, California 95616
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