Linked Life Data

9662442

Source:http://linkedlifedata.com/resource/pubmed/id/9662442

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-7-29
pubmed:abstractText
Some low molecular mass heat shock proteins (HSPs) appear to act as molecular chaperones, but their exact physiological roles have not been fully elucidated. We reported previously that a 20-kDa protein (p20), which is classified as a low molecular mass HSP, is present at high levels in skeletal and smooth muscles. In the present study, we investigated a physiological role of p20 on platelet function in vitro and ex vivo. p20 inhibited platelet aggregation using human platelets dose-dependently induced by botrocetin. On the other hand, HSP27, the other type of low molecular mass HSP, did not affect platelet aggregation. When p20 (300 microg/kg) was injected intravenously as a bolus in hamsters, platelet aggregation ex vivo induced by botrocetin was also significantly inhibited. In order to further investigate the inhibitory effect by p20 on platelet activation, we performed platelet aggregation induced by thrombin or ADP using human platelets. p20 markedly prevented platelet aggregation induced by thrombin, but not ADP. These findings suggest that p20 can act intercellularly to regulate platelet functions. Our results may provide the basis for a novel defensive system to thrombus formation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
429
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
327-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
A heat shock-related protein, p20, plays an inhibitory role in platelet activation.
pubmed:affiliation
Department of Pharmacology, Gifu University School of Medicine, Japan.
pubmed:publicationType
Journal Article, Comparative Study