Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-2-13
pubmed:abstractText
Plasmalogen-specific, calcium-independent phospholipase A2 (iPLA2) is activated during myocardial ischemia. Accordingly, we have assessed the activation of myocardial protein kinases by the iPLA2 product, lysoplasmenylcholine. Lysoplasmenylcholine-activated protein kinase activity from heart cytosol fractionated on a DE-52 column was identified as cAMP-dependent protein kinase (PKA) based on the following: (1) protein kinase activity stimulated by cAMP and lysoplasmenylcholine co-eluted on sequential chromatographic steps; (2) lysoplasmenylcholine-activated protein kinase activity was inhibited by the PKA inhibitor, PKI; and (3) the unprimed PKA form generated from the primed form of PKA was activated by cAMP and lysoplasmenylcholine. These results demonstrate a novel mechanism for PKA activation by lysoplasmenylcholine.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
420
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Activation of myocardial cAMP-dependent protein kinase by lysoplasmenylcholine.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, St. Louis University Health Science Center, MO 63104, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.