Calcium-dependent proteolysis of calcium-binding proteins |
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| Authors: | I Sohar J W Bird P B Moore |
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| Affiliation: | 1. Department of Veterinary Medical Sciences, University of Bologna, Via Tolara di Sopra, 50 40064 Ozzano Emilia, Bologna, Italy;2. Department of Animal Pathology, School of Veterinary Medicine, Viale delle Piagge 2, Pisa, Italy;3. University of Maryland, School of Medicine, 10 South Pine St., MSTF, Suite G-100, Baltimore, MD, USA;1. Department of Bio and Health Informatics, Technical University of Denmark, Kgs. Lyngby, Denmark;2. Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark;3. Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica, San José, Costa Rica;1. Department of “Health Sciences”, Nephrology Unit, Magna Graecia University, Catanzaro I-88100, Italy;2. Department of “Public Health”, Nephrology Unit, Federico II University, Naples I-80131, Italy;3. Department of Food Quality and Nutrition, Fondazione Edmund Mach, Research and Innovation Centre, San Michele all''Adige, I-38010, Italy;4. Department of “Health Sciences”, Pharmacology Unit, Magna Graecia University, Catanzaro I-88100, Italy;5. Department of “Drug Sciences and Products for Health”, University of Messina, I-98168 Messina, Italy;1. Department of Surgery, University of São Paulo, Brazil;2. Rush University Medical Center, Chicago, IL, United States;3. Department of Surgery, Cantonal Hospital Winterthur and Institute of Physiology, University of Zurich, Switzerland |
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| Abstract: | 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. |
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