Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1992-5-18
pubmed:abstractText
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 soluble and structural proteins (via SDS-polyacrylamide gel electrophoresis) in 5 innervated and denervated muscle types from control and drug-treated rats. No gross change in activity was found for any enzyme type in any muscle (innervated or denervated) following clenbuterol treatment; however, one enzyme, arginyl aminopeptidase, showed a small but consistent decrease in activity in all of the innervated muscles investigated. Similar fractionation profiles were obtained for structural or soluble proteins from corresponding muscle types (innervated or denervated) in control or clenbuterol-treated animals, with the exception of cardiac muscle, which showed a 50% increase in staining intensity 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0148-639X
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
471-8
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Effect of clenbuterol on protease activities and protein levels in rat muscle.
pubmed:affiliation
Neurochemistry Department, Regional Neurological Centre, Newcastle General Hospital, Newcastle upon Tyne, UK.
pubmed:publicationType
Journal Article