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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1985-7-25
|
| pubmed:abstractText |
A widely distributed Ca2+- and phospholipid-dependent protein kinase, protein kinase C, may play a major role in cellular regulation. We now report that arachidonate can directly activate protein kinase C from human neutrophils. Activation was Ca2+-dependent and was enhanced by diolein, but did not require phosphatidylserine. Arachidonate enhanced the apparent affinity of the kinase for Ca2+ in the presence of phosphatidylserine. Other unsaturated, but not saturated, fatty acids also activated protein kinase C. These results suggest a novel means of leukocyte activation and cellular regulation: arachidonate, which is released by ligand-receptor interactions in neutrophils and many other cell types, could function as a second messenger via activation and modulation of protein kinase C.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0066-9458
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
97
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
222-31
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading | |
| pubmed:year |
1984
|
| pubmed:articleTitle |
A potential second messenger role for arachidonic acid: activation of Ca2+-dependent protein kinase.
|
| pubmed:publicationType |
Journal Article
|