Linked Life Data

10623589

Source:http://linkedlifedata.com/resource/pubmed/id/10623589

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-2-8
pubmed:abstractText
Activation of the cytosolic Group IV phospholipase A(2) (cPLA(2)) by agonists has been correlated with the direct phosphorylation of the enzyme by members of the mitogen-activated protein kinase (MAPK) cascade. Phosphorylation of the cPLA(2) increases the specific activity of the enzyme, thereby stimulating the arachidonic acid release. We show here, however, that conditions that lead to full phosphorylation of the cPLA(2) do not lead to enhanced AA release. As the above observations were made under both Ca(2+)-dependent and Ca(2+)-independent conditions, they emphasize that the current paradigm for activation of the cPLA(2) in cells involving both phosphorylation and Ca(2+) is incomplete and that other factors should be taken into account.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
145-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Phosphorylation of cytosolic group IV phospholipase A(2) is necessary but not sufficient for Arachidonic acid release in P388D(1) macrophages.
pubmed:affiliation
Department of Chemistry, University of California at San Diego, La Jolla, California, 92093-0601, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.