Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1981-6-13
pubmed:abstractText
The intermediate filament proteins, desmin and vimentin, are phosphorylated in skeletal muscle cells in vivo. Desmin kinase activities have been purified from mature chicken skeletal muscle and identified as the cAMP-dependent kinases. Chicken skeletal muscle contains two cAMP-dependent protein kinases which are similar to those of other tissues in their subunit composition and chromatographic behavior. The catalytic subunits purified from the two chicken cAMP-dependent kinases phosphorylate both desmin and vimentin in vitro, using cytoskeletal residues prepared from cultured myogenic cells as a substrate. Likewise, the purified catalytic subunits of the rabbit skeletal muscle and bovine heart cAMP-dependent protein kinases phosphorylate desmin and vimentin in vitro. Desmin and vimentin phosphorylation by the rabbit skeletal muscle catalytic subunit is inhibited by the addition of its regulatory subunit. This inhibition is reversed by the presence of cAMP in the reaction mixture. A small fraction of the vimentin phosphorylation is cAmP-independent. Tryptic peptide analysis of desmin phosphorylated in vivo shows two major phosphopeptides. Serine is the phosphorylated amino acid in both peptides. The same two peptides are phosphorylated in vitro by the bovine heart catalytic subunit, but additional peptides are also phosphorylated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
135-43
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Phosphorylation of intermediate filament proteins by cAMP-dependent protein kinases.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't