Muscle breakdown and lysosomal activation (biochemistry).
Muscle tissue levels of lysosomal catheptic enzymes, such as cathepsins D, A, B1, C, and dipeptidyl peptidase II, were measured in control subjects and patients with muscular dystrophies, polymyositis, and certain denervating diseases. The results show that, in general, the activities of these enzymes are increased in muscles of patients with muscular dystrophies and other diseases. The increases in cathepsin D and autolytic activities are not significant until the late stage of the disease process. Cathepsins A, B1, and C are, however, significantly elevated in mildly affected dystrophic and other diseased muscles. Of these catheptic enzymes, cathepsin B1 displays the highest rise at an early stage, suggesting that it may be one of the rate-controlling enzymes of proteolysis. Dipeptidyl peptidase II is increased slightly in dystrophic and other myopathic muscles but is unchanged in denervated muscle. These data clearly implicate the lysosomal group of proteinases as largely responsible for mediating muscle breakdown in the muscular dystrophies and certain other muscle and neuromuscular diseases in man.
D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D004150:Dipeptidases / Q000378:metabolism; D006168:Guinea Pigs; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology*; D009132:Muscles / Q000201:enzymology*; D009136:Muscular Dystrophies / Q000201:enzymology*; D009468:Neuromuscular Diseases / Q000378:metabolism*; D013379:Substrate Specificity; D014018:Tissue Distribution
D007527:Isoenzymes; D002403:Cathepsins; D004150:Dipeptidases