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Effect of clenbuterol on protease activitiies and protein levels in rat muscle
Author(s) -
Mantle David,
Delday Margaret I.,
Maltin Charlotte A.
Publication year - 1992
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.880150410
Subject(s) - clenbuterol , skeletal muscle , myosin , protease , endocrinology , medicine , enzyme , chemistry , downregulation and upregulation , protein subunit , anabolism , biochemistry , biology , gene
To elucidate the biochemical mechanism by which the sympathomimetic agent clenbuterol promotes skeletal muscle growth, We have determined the activity of a range of proteolytic enzyme types (acid, neutral and alkaline proteinases and peptidases), together with the levels of souble and structural proteins (via SDS‐polyacrylamide) in 5 inner‐vated and denervated muscle types from for any enzyme type in any muscle (in‐nervated or denervated) following clenbuterol treatment; however, one enzyme, arginyl aminopeptidase, showed a small but consistent decrease in acticvity in all of the innervated muscles investigated. Smilar fractionation muscle types (innervated or denervated) in control or clenbuterol‐treated animals, with the exception of one band (subunit molecular mass 18 kD). We conclude that the anabolic action of clenbuterol in promoting skeletal muscle growth does not occur via downregulation of protease activity, or increase in levels of individual muscle proteins.