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Prepublished online as a Blood First Edition Paper on June 14, 2002; DOI 10.1182/blood-2002-02-0354.
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Blood, 15 October 2002, Vol. 100, No. 8, pp. 2827-2831
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Thrombospondin and fibrinogen bind serotonin-derivatized
proteins on COAT-platelets
Robert Szasz and
George L. Dale
From the W. K. Warren Medical Research Institute,
Department of Medicine, University of Oklahoma Health Sciences Center,
Oklahoma City, OK.
Activation of platelets with 2 agonists, collagen and thrombin,
reveals a subpopulation of cells referred to as COAT-platelets (collagen and thrombin activated).
These cells are enriched in several membrane-bound, procoagulant
proteins, including fibrinogen, thrombospondin, factor V, von
Willebrand factor, and fibronectin.  -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
photoreactive cross-linking to an albumin-(serotonin)6 conjugate during COAT-platelet production. We subsequently verified that biotin-albumin-(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 (eg, 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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