Calcium-dependent proteolysis of calcium-binding proteins.
In several myopathic disorders, the internal muscle cell calcium concentration increases significantly as compared to normal muscle cells. We report that in the presence of elevated calcium levels, the calcium-binding proteins troponin C and calmodulin are protected from digestion by the chymotrypsin-like serine proteinase that co-purifies with isolated myofibrils. Degradation of the 67k calcimedin in the presence of calcium shows altered major cleavage fragments while degradation of myosin is unaffected by the presence of calcium. A role for this serine proteinase in muscle-wasting diseases is suggested.
D000818:Animals; D017317:Annexin A6; D017302:Annexins; D002118:Calcium / Q000502:physiology*; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D002147:Calmodulin / Q000378:metabolism; D002384:Catalysis; D010450:Endopeptidases / Q000378:metabolism*; D008297:Male; D009132:Muscles / Q000201:enzymology; D009218:Myosins / Q000378:metabolism; D051381:Rats; D012697:Serine Endopeptidases; D014336:Troponin / Q000378:metabolism; D019209:Troponin C
D017317:Annexin A6; D017302:Annexins; D002135:Calcium-Binding Proteins; D002147:Calmodulin; D014336:Troponin; D019209:Troponin C; D010450:Endopeptidases; D012697:Serine Endopeptidases; D009218:Myosins; D002118:Calcium