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Dynamic aspects of structural proteins in vertebrate skeletal muscle
Author(s) -
Obinata T.,
Maruyama K.,
Sugita H.,
Kohama K.,
Ebashi S.
Publication year - 1981
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.880040604
Subject(s) - myofibril , proteases , tropomyosin , myosin , actin , skeletal muscle , biochemistry , titin , protease , biology , desmin , sarcoplasm , cathepsin d , troponin , sarcomere , microbiology and biotechnology , myocyte , enzyme , anatomy , medicine , vimentin , immunohistochemistry , endoplasmic reticulum , immunology , myocardial infarction
In this review, our current knowledge on the structural proteins of vertebrate skeletal muscle is briefly outlined. Structural proteins include the contractile proteins (actin and myosin), the major regulatory proteins (troponin and tropomyosin), the minor regulatory proteins (M‐protein, C‐protein, F‐protein, l‐protein, and actinins), and the scaffold proteins (connectin, desmin, and Z‐protein). In addition, the relative turnover rates of the muscle proteins (M‐protein < troponin > soluble protein as a whole > tropomyosin = α‐actinin > myosin > 10S‐actinin > actin) are discussed. The changes in the turnover of muscle proteins are compared in denervated and dystrophic muscles. The properties of the various proteases in muscle, including alkaline protease, calcium‐activated neutral protease (CANP), and acidic protease (cathepsins), and the structural alterations of myofibrils by these proteases are also described. Finally, the role of proteases and their inhibitors in diseased muscle is summarized, with focus on CANP and its inhibitors, leupeptin and E‐64.