Abstract
The observation that Glanzmann thrombasthenia, a rare autosomal recessive congenital bleeding disorder characterized by the absence of macroscopic platelet aggregation in response to all physiologic stimuli (Caen et al., 1966; reviewed by Nurden, 1989), was associated with the absence, or marked reduction of the content, of two platelet surface glycoproteins, GPIIb (135 kDa) and GPIIIa (95 kDa), (Nurden and Caen, 1974) provided the first evidence to assign a given platelet function to specific membrane glycoproteins (Nurden and Caen, 1975; Phillips et al., 1975). Moreover, the well-documented role of fibrinogen as an essential cofactor for platelet aggregation (Caen and Inceman, 1963; McLean et al., 1964; reviewed by Peerschke, 1985; Plow et al., 1986), together with the demonstration of a direct association of fibrinogen with a single, or predominant, class of inducible, (∼mM) Ca2+-dependent, specific and saturable platelet receptor (Mustard et al., 1978; Marguerie et al., 1979; Bennett and Vilaire, 1979), and the failure of thrombasthenic platelets to bind fibrinogen and aggregate upon activation (Mustard et al., 1979), suggested a role for GPIIb and/or GPIIIa as part of the platelet fibrinogen receptor system (reviewed by Marguerie and Plow, 1983; Plow et al., 1984; Peerschke, 1985).
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Calvete, J.J. (1993). Elements for a Structural/Functional Model of Human Platelet Plasma Membrane Fibrinogen Receptor, the Glycoprotein IIb/IIIa Complex (Integrin αIIb/β3). In: Hemler, M.E., Mihich, E. (eds) Cell Adhesion Molecules. Pezcoller Foundation Symposia, vol 4. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2830-2_6
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