Proteolysis of the calcium-dependent protease inhibitor by myocardial calcium-dependent protease |
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| Authors: | R L Mellgren M T Mericle R D Lane |
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| Affiliation: | 1. Department of Clinical Pharmacy, Shanghai General Hospital, School of Medicine, Shanghai Jiaotong University, No. 85 Wujin Road, Shanghai 200080, PR China;2. Shanghai Key Laboratory for Pharmaceutical Metabolite Research, School of Pharmacy, Second Military Medical University, No. 325 Guohe Road, Shanghai 200433, PR China;3. School of Medicine, Tongji University, No. 1239 Siping Road, Shanghai 200092, PR China;4. Department of Clinical Pharmacy, Shanghai University of Medicine and Health Science, Shanghai, China;5. Department of Pharmacy, Shanghai Fourth People''s Hospital affiliated to Tongji University School of Medicine, No. 1878 North Sichuan Road, Shanghai 200081, PR China;6. Ridley College, 2 Ridley Road, St. Catharines, Ontario L2R TC3, Canada;1. Università degli Studi di Roma “Foro Italico”, Department of Movement, Human and Health Sciences, Unit of Biology, Genetics and Biochemistry, Rome, Italy;2. Università degli Studi di Roma “Foro Italico”, Department of Movement, Human and Health Sciences, Unit of Endocrinology, Rome, Italy;3. Università degli Studi di Roma “Foro Italico”, Department of Movement, Human and Health Sciences, Laboratory of Exercise Physiology, Rome, Italy |
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| Abstract: | Bovine heart peak II calcium-dependent protease was capable of hydrolyzing its specific inhibitor protein at high molar ratios of protease to inhibitor. The proteolysis was inhibited by leupeptin and required millimolar calcium. Thus, it appeared to be attributable to the calcium-dependent protease and not to possible contaminating proteases in the purified preparations of inhibitor or calcium-dependent protease. Incubation of the purified inhibitor with the calcium-dependent protease produced a discrete pattern of inhibitor fragments on Western blots developed with an inhibitor-specific monoclonal antibody. Traces of similar or identical lower molecular weight immunoreactive material could be observed in Western blots of bovine heart extracts, and the immunoreactivity present as these lower molecular weight forms could be increased by incubation of the extracts with calcium ion. These results suggest that the inhibitor can be proteolyzed to low molecular weight forms which can be detected in cardiac tissue extracts, and that calcium-dependent protease(s) may be responsible for this phenomenon. |
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