Proteinases in cardiac and skeletal muscle.
Although changes in proteolysis in muscle tissue are now well documented for a variety of physiological and pathological conditions, the mechanism of degradation of cellular protein during normal protein turnover remains to be elucidated. Data from several laboratories have suggested the involvement of alkaline serine proteinases. Recent studies have questioned these results, and demonstrated that the serine proteinases are of mast cell origin and are not present in muscle cells. The only proteinases to date that have been shown to be present in muscle cells and capable of degrading myofibrillar proteins are Ca2+-activated proteinase, cathepsin B, and cathepsin D. Recent interest and developing awareness of endogenous enzyme inhibitors in cells may unmask many new enzymes.
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D002403:Cathepsins / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008247:Lysosomes / Q000201:enzymology; D009124:Muscle Proteins / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D012694:Serine; D013379:Substrate Specificity
D009124:Muscle Proteins; D011480:Protease Inhibitors; D012694:Serine; D002403:Cathepsins; D010447:Peptide Hydrolases; D002118:Calcium