Linked Life Data

7658910

Source:http://linkedlifedata.com/resource/pubmed/id/7658910

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1995-10-2
pubmed:abstractText
We have determined the effects of chronic exposure to the protein kinase C (PKC) activating drug 4-beta phorbol 12-myristate-13-acetate (PMA) on PKC isozymes and the rate of spontaneous contraction in neonatal rat cardiac myocytes in culture. Western blot analyses revealed that a two day exposure to 0.1-1 nM PMA increased the total amount of delta PKC, whereas, 100 nM PMA concentrations caused a complete down-regulation of the alpha PKC and an 80 kDa zeta PKC-like protein. In addition, 100 nM PMA treatment for 2 days did not result in complete down-regulation of the beta, delta, and epsilon PKC isozymes in Western blot and immunocytochemical studies. We also found a PKC-mediated enhancement of the rate of contraction in these cells following prolonged exposure to PMA (1-100nM). Our studies suggest that this enhancement of contraction rate may be mediated by the beta, delta, or epsilon PKC isozymes. A better understanding of the role(s) of PKC isozymes in the modulation of cardiac functions may reveal selective targets for therapies of cardiac disorders.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0024-3205
pubmed:author
pubmed:issnType
Print
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1027-38
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Prolonged phorbol ester treatment down-regulates protein kinase C isozymes and increases contraction rate in neonatal cardiac myocytes.
pubmed:affiliation
Department of Molecular Pharmacology, Stanford University School of Medicine, CA 94305-5332, USA.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't