Linked Life Data

8299726

Source:http://linkedlifedata.com/resource/pubmed/id/8299726

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-3-10
pubmed:abstractText
Activation of protein kinase C (PKC) isozymes is associated with their translocation from the cell-soluble fraction to the cell-particulate fraction, presumably near their protein substrates. Therefore, identifying the subcellular localization of each activated PKC isozyme may help to elucidate its role in cardiac functions. In the present work, we have determined the subcellular localization of six PKC isozymes (alpha, beta I, beta II, delta, epsilon, and zeta) in nonstimulated cardiac myocytes and in myocytes stimulated by norepinephrine (2 microM) or phorbol 12-myristate 13-acetate (100 nM). Activated PKC isozymes were localized in various subcellular compartments such as inside the nucleus and on myofibrils. The presence of serum in the growth medium also caused a redistribution of PKC isozymes in the cells distinct from that obtained with cells cultured in defined medium. We suggest that isozyme-specific localization may determine phosphorylation of different protein substrates present at these respective translocation sites and the resulting PKC-mediated cellular responses.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-4827
pubmed:author
pubmed:issnType
Print
pubmed:volume
210
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
287-97
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Localization of protein kinase C isozymes in cardiac myocytes.
pubmed:affiliation
Department of Molecular Pharmacology, School of Medicine, Stanford University, California 94305.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.