Linked Life Data

20517720

Source:http://linkedlifedata.com/resource/pubmed/id/20517720

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-10-15
pubmed:abstractText
Hemopoietic cells express relatively high levels of the type I phosphoinositide (PI) 3-kinase isoforms, with p110? and ? exhibiting specialized signaling functions in neutrophils, monocytes, mast cells, and lymphocytes. In platelets, p110? appears to be the dominant PI 3-kinase isoform regulating platelet activation, irrespective of the nature of the primary platelet activating stimulus. Based on findings with isoform-selective p110? pharmacological inhibitors and more recently with p110?-deficient platelets, p110? appears to primarily signal downstream of G(i)- and tyrosine kinase-coupled receptors. Functionally, inhibition of p110? kinase function leads to a marked defect in integrin ?(IIb)?? adhesion and reduced platelet thrombus formation in vivo. This defect in platelet adhesive function is not associated with increased bleeding, suggesting that therapeutic targeting of p110? may represent a safe approach to reduce thrombotic complications in patients with cardiovascular disease.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0070-217X
pubmed:author
pubmed:issnType
Print
pubmed:volume
346
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
203-24
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
PI 3-Kinase p110? regulation of platelet integrin ?(IIb)?3.
pubmed:affiliation
Australian Centre for Blood Diseases, Alfred Medical Research and Education Precinct (AMREP), Monash University, Melbourne, VIC, 3004, Australia. Shaun.Jackson@med.monash.edu.au
pubmed:publicationType
Journal Article, Review