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Prepublished online as a Blood First Edition Paper on June 14, 2002; DOI 10.1182/blood-2002-02-0354.
Submitted February 4, 2002
Accepted June 4, 2002
Thrombospondin and fibrinogen bind serotonin-derivatized proteins on COAT-platelets
Robert Szasz and George L Dale*
Deptartment of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA
* Corresponding author; email: george-dale{at}ouhsc.edu.
Activation of platelets with two agonists, collagen and thrombin, reveals a subpopulation of cells, referred to as COAT-platelets. These cells are enriched in several membrane-bound, procoagulant proteins, including fibrinogen, thrombospondin, factor V, von Willebrand factor and fibronectin. Alpha-granule proteins bound to COAT-platelets are derivatized with serotonin by a transglutaminase-mediated process, and the interaction of conjugated-serotonins with unidentified serotonin binding sites on the platelet surface enhances retention of these proteins. We now demonstrate that both thrombospondin and fibrinogen provide the requisite serotonin-binding sites. Thrombospondin and fibrinogen were identified using photo-reactive crosslinking to an albumin-(serotonin)6 conjugate during COAT-platelet production. We subsequently verified that biotin-BSA-(serotonin)6 binds in vitro to thrombospondin, fibrinogen and fibrinogen fragment D in a saturable manner. These data support a model for COAT-platelets where serotonin-derivatized procoagulant proteins interact with their respective receptors (e.g. fibrinogen with glycoprotein IIb/IIIa or factor V with phosphatidylserine) as well as serotonin binding sites on fibrinogen and thrombospondin resulting in a stable, multivalent complex on the cell surface.
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