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Nitric oxide inhibits calpain-mediated proteolysis of talin in skeletal muscle cellsWe tested the hypothesis that nitric oxide can inhibit cytoskeletal breakdown in skeletal muscle cells by inhibiting calpain cleavage of talin. The nitric oxide donor sodium nitroprusside prevented many of the effects of calcium ionophore on C(2)C(12) muscle cells, including preventing talin proteolysis and release into the cytosol and reducing loss of vinculin, cell detachment, and loss of cellular protein. These results indicate that nitric oxide inhibition of calpain protected the cells from ionophore-induced proteolysis. Calpain inhibitor I and a cell-permeable calpastatin peptide also protected the cells from proteolysis, confirming that ionophore-induced proteolysis was primarily calpain mediated. The activity of m-calpain in a casein zymogram was inhibited by sodium nitroprusside, and this inhibition was reversed by dithiothreitol. Previous incubation with the active site-targeted calpain inhibitor I prevented most of the sodium nitroprusside-induced inhibition of m-calpain activity. These data suggest that nitric oxide inhibited m-calpain activity via S-nitrosylation of the active site cysteine. The results of this study indicate that nitric oxide produced endogenously by skeletal muscle and other cell types has the potential to inhibit m-calpain activity and cytoskeletal proteolysis.
Document ID
20040141446
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Koh, T. J.
(University of California Los Angeles, California 90095, United States)
Tidball, J. G.
Date Acquired
August 22, 2013
Publication Date
September 1, 2000
Publication Information
Publication: American journal of physiology. Cell physiology
Volume: 279
Issue: 3
ISSN: 0363-6143
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: AR-08479
CONTRACT_GRANT: AR-40343
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Musculoskeletal
Non-NASA Center

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