Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-5-5
pubmed:abstractText
The regulation of phosphatidylcholine-hydrolyzing phospholipase D (PLD) by protein kinase C (PRC) in membranes of Chinese hamster lung fibroblasts (CCL39) was studied using conventional PKC isoforms alpha, beta and gamma isolated from rat brain and recombinant PKC isoforms. Cells were incubated with [14C]choline to label endogenous phosphatidylcholine before membranes were prepared and assayed for release of [14C]choline. PKC alpha was the most potent activator of PLD, producing a maximal effect at approximately 0.1 microgram/ml. PKC beta also stimulated PLD but was less potent and less efficacious, whereas PKC gamma was ineffective. Stimulation required addition of a PKC activator, but the isoform specificity was the same whether phorbol 12-myristate 13-acetate (PMA) or Ca2+ was used. Recombinant Ca(2+)-independent PKC isoforms delta, epsilon, and zeta failed to stimulate PLD, but recombinant PKC beta 1 stimulated PLD in a manner similar to the purified brain PKC beta. Immunoblot analysis of the soluble fraction of CCL 39 fibroblasts detected only the alpha and zeta isoforms of PKC. The results suggest that PKC alpha and beta are activators of PLD and that PKC alpha is responsible for the activation in these fibroblasts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
342
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
149-53
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Phospholipase D activation in fibroblast membranes by the alpha and beta isoforms of protein kinase C.
pubmed:affiliation
Howard Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, TN 37232.
pubmed:publicationType
Journal Article