Stimulated platelets use serotonin to enhance their retention of procoagulant proteins on the cell surface

Dale, GL; Friese, P; Batar, P; Hamilton, SF; Reed, GL; Jackson, KW; Clemetson, KJ; Alberio, L (2002). Stimulated platelets use serotonin to enhance their retention of procoagulant proteins on the cell surface. Nature, 6868(415), pp. 175-9. London: Macmillan Journals Ltd. 10.1038/415175a

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Activated platelets bind numerous adhesive and procoagulant proteins by receptor-mediated processes. Although there is little evidence to suggest that these processes are heterogeneous in platelets, we previously found that platelets co-stimulated with collagen and thrombin express functional alpha-granule factor V only on a subpopulation of cells. Here we show that these cells, referred to as 'COAT-platelets', bind additional alpha-granule proteins, including fibrinogen, von Willebrand factor, thrombospondin, fibronectin and alpha2-antiplasmin. These proteins are all transglutaminase substrates, and inhibitors of transglutaminase prevent the production of COAT-platelets. A synthetic transglutaminase substrate (CP15) also binds to COAT-platelets, and analysis by high performance liquid chromatography/mass spectrometry shows that a product is formed with a relative molecular mass (Mr) equal to CP15 plus 176. Serotonin, an abundant component of platelet-dense granules, has an Mr of 176, and fibrinogen isolated from COAT-platelets contains covalently linked serotonin. Synthetic bovine serum albumin-(serotonin)6 binds selectively to COAT-platelets and also inhibits the retention of procoagulant proteins on COAT-platelets. These data indicate that COAT-platelets use serotonin conjugation to augment the retention of procoagulant proteins on their cell surface through an as yet unidentified serotonin receptor.

Item Type:	Journal Article (Original Article)
Division/Institute:	04 Faculty of Medicine > Pre-clinic Human Medicine > Theodor Kocher Institute
UniBE Contributor:	Clemetson, Kenneth John
ISSN:	0028-0836
ISBN:	11805836
Publisher:	Macmillan Journals Ltd.
Language:	English
Submitter:	Factscience Import
Date Deposited:	04 Oct 2013 14:52
Last Modified:	05 Dec 2022 14:16
Publisher DOI:	10.1038/415175a
PubMed ID:	11805836
Web of Science ID:	000173159300043
URI:	https://boris.unibe.ch/id/eprint/22169 (FactScience: 32180)