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Muscular dystrophy and activation of proteinases
Author(s) -
Kar Nirmal C.,
Pearson Carl M.
Publication year - 1978
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880010407
Subject(s) - cathepsin , muscular dystrophy , skeletal muscle , biochemistry , duchenne muscular dystrophy , proteolytic enzymes , cathepsin d , proteolysis , dipeptidyl peptidase , enzyme , endopeptidase , catabolism , intracellular , biology , chemistry , endocrinology , genetics
Evidence is presented for the existence of many different systems of proteolytic enzymes in human skeletal muscle. These include the lysosomal system of cathepsins as well as proteinases and peptide hydrolases that are optimally active at neutral and alkaline pH ranges. The majority of proteolytic enzymes examined are found to show increased activity in dystrophic human muscle. Moreover, a high initial rise is observed in cathepsin B 1 , a thiol‐dependent endopeptidase of lysosomes, and in dipeptidyl peptidase IV, a membrane‐associated peptidase. In addition, a calcium‐activated neutral proteinase is found to be significantly elevated in muscle from patients with Duchenne dystrophy. The possible roles of these proteinases in intracellular protein catabolism and muscle wasting are discussed.