Linked Life Data

9742943

Source:http://linkedlifedata.com/resource/pubmed/id/9742943

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-10-8
pubmed:abstractText
Adenosine and mitogen-activated protein kinases (MAPKs) have been separately implicated in cardiac ischaemic preconditioning. We investigated the activation of MAPK subfamilies by adenosine in perfused rat hearts. p38-MAPK was rapidly phosphorylated and activated (10-fold activation, maximal at 5 min) by 10 mM adenosine, as was the p38-MAPK substrate, MAPKAPK2 (4.5-fold). SAPKs/JNKs were activated (5-fold) and ERKs were phosphorylated (both maximal at 5 min). The concentration dependences of activation of p38-MAPK and ERKs were biphasic with a 'high affinity' component (maximal at 10-100 microM adenosine) and a 'low affinity' component that had not saturated at 10 mM. SAPKs/JNKs were activated only by 10 mM adenosine. These results are consistent with MAPK involvement in adenosine-mediated ischaemic preconditioning.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
434
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
305-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Activation of mitogen-activated protein kinases (p38-MAPKs, SAPKs/JNKs and ERKs) by adenosine in the perfused rat heart.
pubmed:affiliation
NHLI Division (Cardiac Medicine), Imperial College School of Medicine, London, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't