Linked Life Data

9916342

Source:http://linkedlifedata.com/resource/pubmed/id/9916342

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1999-2-5
pubmed:abstractText
The main threat from a beginning thrombus is that it tends to grow, and hence become occlusive and/or embolise. Although the progressive nature of thrombi has been recognised since a long time, the mechanisms behind thrombus growth remain only partially resolved. In order to investigate in what ways thrombi can themselves become foci of further thrombin -and hence fibrin-formation, we studied the effect of fibrin clots on thrombin generation in platelet poor--and platelet rich plasma (PPP and PRP). The thrombin always adsorbed on a natural fibrin clot is not inactivated by plasmatic antithrombins and could be shown to retain its ability to enhance further thrombin formation by activation of clotting factors V and VIII as well as of blood platelets. To our surprise, fibrin clots without any active thrombin adsorbed, because they were obtained by a snake-venom enzyme or because thrombin had been inhibited, retained their capacity to activate blood platelets and make them procoagulant. The activation could be shown to be due to a rearrangement of cell-membrane phospholipids, by which the procoagulant species (phosphatidyl serine and phosphatidyl ethanolamine) became available at the outer cell surface. The platelet membrane receptor involved could be recognised as glycoprotein Ib, interacting with fibrin through the plasma protein von Willebrand factor (vWf). In fact it appeared that vWf is indispensable for the generation of thrombin in PRP, with or without added clot. This assigns a new and hitherto unknown role to vWf. Our results also show that fibrin is far from being the inert end-product of coagulation but is a potent activator of blood platelets and by this action may foster thrombin generation and hence further fibrin production. We surmise this mechanism to be instrumental in the progression of thrombotic processes.
pubmed:language
fre
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0001-4079
pubmed:author
pubmed:issnType
Print
pubmed:volume
182
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1479-91; discussion 1491-2
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
[Procoagulant nature of fibrin].
pubmed:affiliation
Département de Biochimie, Cardiovascular Research Institute Maastricht (CARIM), Université de Maastricht, Pays-Bas.
pubmed:publicationType
Journal Article, Comparative Study, English Abstract, Research Support, Non-U.S. Gov't