Linked Life Data

3953807

Source:http://linkedlifedata.com/resource/pubmed/id/3953807

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3 Pt 1
pubmed:dateCreated
1986-4-11
pubmed:abstractText
The expression of phosphorylase kinase was investigated in rat skeletal muscle cells developing in vitro. The enzyme was immunoprecipitated from cells cultured in the presence of [35S]methionine, and the 35S-labeled alpha-, alpha'-, and beta-subunits of the kinase were resolved by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Fusion of myoblasts into myotubes was associated with marked increases in the amounts of kinase activity and the three 35S-labeled subunits. In 2-wk-old myotubes, the net amount of alpha'-subunit represented less than 20% of the total alpha-subunits (alpha + alpha'); however, alpha'-subunits appeared to be synthesized at least as rapidly as alpha-subunits. That alpha'-subunits were degraded more rapidly was confirmed by pulse-chase experiments, which also indicated that alpha'-subunits were not formed by proteolytic processing of the larger alpha-subunit. Inhibition of the spontaneous contractile activity of the myotubes with lidocaine markedly increased both phosphorylase kinase activity and the amounts of the 35S-labeled subunits. The divalent cation ionophore, A23187, decreased the alpha-subunits by 60%, but did not change levels of the alpha'-subunits. Taken together, the present results indicate that rat myotubes synthesize the two isozymes of phosphorylase kinase, and that levels of both are controlled by differentiation and muscle activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
250
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C365-73
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Rat skeletal muscle phosphorylase kinase: turnover and control of isozyme levels in culture.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't