Abstract
This study was designed to investigate the nature of modification of myofibrillar proteins by nitric oxide (NO) and the extent to which S-nitrosylation alters their susceptibility to calpain-1 proteolysis. Isolated myofibrils from porcine semimembranosus muscle were incubated with the NO donor S-nitrosoglutathione (GSNO) at 0, 20, 50, 250, 1000 µM for 30 min at 37 °C and then incubated with purified calpain-1. GSNO treatment decreased the thiol content of myofibrillar proteins and increased their intensity and amount of S-nitrosylation. GSNO caused the formation of proteins cross-linkage through intermolecular disulfide. More desmin and titin (T2, the degraded fragment of original titin) were degraded by calpain-1 when myofibrils were incubated with 1000 µM GSNO. Incubation with 250 and 1000 µM GSNO suppressed calpain-1-catalyzed cleavage of troponin-T. The data suggest that NO could change the redox state of myofibrillar proteins and subsequently affect the extent of proteolysis by calpain-1 in a protein-dependent manner.
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