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The assembly of the factor X‐activating complex on activated human platelets
Author(s) -
Ahmad S. S.,
London F. S.,
Walsh P. N.
Publication year - 2003
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1046/j.1538-7836.2003.00020.x
Subject(s) - prothrombinase , factor ixa , chemistry , platelet , thrombin , factor x , hemostasis , coagulation , receptor , tissue factor , biochemistry , factor v , platelet activation , microbiology and biotechnology , biophysics , immunology , medicine , biology , thrombosis
Summary. Platelet membranes provide procoagulant surfaces for the assembly and expression of the factor X‐activating complex and promote the proteolytic activation and assembly of the prothrombinase complex resulting in normal hemostasis. Recent studies from our laboratory and others indicate that platelets possess specific, high‐affinity, saturable, receptors for factors XI, XIa, IX, IXa, X, VIII, VIIIa, V, Va and Xa, prothrombin, and thrombin. Studies described in this review support the hypothesis that the factor X‐activating complex on the platelet surface consists of three receptors (for the enzyme, factor IXa; the substrate, factor X; and the cofactor, factor VIIIa), the colocalization of which results in a 24 million‐fold acceleration of the rate of factor X activation. Whether the procoagulant surface of platelets is defined exclusively by procoagulant phospholipids, or whether specific protein receptors exist for the coagulant factors and proteases, is currently unresolved. The interaction between coagulation proteins and platelets is critical to the maintenance of normal hemostasis and is pathogenetically important in human disease.