Linked Life Data

8752108

Source:http://linkedlifedata.com/resource/pubmed/id/8752108

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-10-2
pubmed:abstractText
Although cyclic AMP (cAMP) has been reported to cross talk with the protein kinase C (PKC) system, effects of elevated intracellular cAMP on the activities of specific PKC isoforms have not been studied. We report findings from a permeabilized cell assay that was used to examine changes in the activity of the atypical PKC isoforms brought about by exposure of PC12 cells to agents that elevate intracellular cAMP. We found that increases in intracellular cAMP led to rapid stimulation of atypical PKC activity, 40-70% above control, for a sustained period of time, a response that occurred independent of the phorbol 12-myristate 13-acetate (PMA)-sensitive PKC isoforms. Changes in intracellular cAMP levels resulted in a dose-dependent redistribution of zeta-PKC to the cytoplasm with a concomitant increase in the phosphorylation state of the enzyme. Incubation of purified zeta-PKC with increasing concentrations of PKA likewise caused a twofold increase in the phosphorylation state of zeta-PKC. In contrast to the positive effect that PKA-mediated phosphorylation had on the activity of zeta-PKC, the enzyme displayed reduced binding to ras when phosphorylated. Taken together, these findings are consistent with the hypothesis that protein phosphorylation of PKC acts as a positive effector of its enzyme activity and may serve as a negative modulator for interaction with other proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1023-31
pubmed:dateRevised
2009-4-7
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Modulation of zeta-protein kinase C by cyclic AMP in PC12 cells occurs through phosphorylation by protein kinase A.
pubmed:affiliation
Department of Zoology, Auburn University, AL 36849-5414, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't