Linked Life Data

2559079

Source:http://linkedlifedata.com/resource/pubmed/id/2559079

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1990-3-5
pubmed:abstractText
We studied the regulation of dephosphorylation of cAMP-dependent phosphorylated proteins of isolated, permeabilized (skinned) myocardial cells from adult rat. Staurosporine, a potent inhibitor of protein kinase, inhibited cAMP-dependent phosphorylation of phospholamban and troponin-I, the key proteins in the control of contraction and relaxation of the myocardial cells. Staurosporine antagonized the stimulatory action of cAMP on the spontaneous beating of the myocytes accompanied by dephosphorylation of phospholamban but not of troponin-I at pCa 7-8. In cold ATP dilution experiments with apparent stoppage of protein phosphorylation, dephosphorylation of phospholamban was accelerated both by Ca2+ and staurosporine but that of troponin-I took place only in the presence of Ca2+ ion (pCa less than 6.5). These phenomena suggest a bi-directional regulation of dephosphorylation of the key proteins by the intracellular messengers cAMP and Ca2+.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
106
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
894-9
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Bi-directional regulation of dephosphorylation of cAMP-dependent phosphorylated proteins by cAMP and calcium in permeabilized rat heart cells.
pubmed:affiliation
Department of Biology, Faculty of Science, Osaka University.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't