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Purpose of review COAT platelets are a recently described subpopulation of cells resulting from simultaneous activation with collagen and thrombin. The complete process by which COAT platelets are produced is still not clear, although significant recent progress has been made. Recent findings COAT platelets retain several procoagulant proteins on their surface by a previously unrecognized mechanism involving transglutaminase mediated conjugation of serotonin to released a-granule proteins. Fibrinogen and thrombospondin have been found to bind serotonin-conjugated proteins and thereby provide the requisite link for stabilization of serotonin-derivatized, procoagulant proteins on COAT platelets. Summary Multivalent interactions, resulting from traditional receptor interactions and binding of conjugated serotonin by fibrinogen and thrombospondin, result in exceptionally strong retention of procoagulant a-granule proteins on the surface of COAT platelets. The physiologic significance of this new subclass of platelets remains to be determined. (C) 2003 Lippincott Williams and Wilkins.
Keyword:
platelet
thrombin
collagen
convulxin
serotonin
fibrinogen
thrombospondin
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IF38.6
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