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Heparin-induced thrombocytopenia (HIT) is an immune-mediated thrombocytopenia, characterized by thrombocytopenia and platelet-associated antibodies. In the setting of HIT, an array of clinical, pathologic and diagnostic tests are used to assess acute and chronic thrombocytopenia and thrombosis. The HIT antibodies recognized by patients (referred to as HIT IgG) bind to glycoprotein (GP)IIb/IIIa, which is the integrin subunit responsible for platelet aggregation. These interactions lead to platelet activation, aggregates, and ultimately thrombosis. Although many regions of the GPIIb/IIIa have been implicated as binding sites for HIT, these sites have been difficult to identify for several reasons. First, little is known about how the HIT antibody activates platelets, and the role of the integrin’s cytoplasmic domain in these processes has not been studied. Second, the role of lysine residues as the primary antigenic determinant in HIT has not been elucidated. Third, the mechanisms by which the HIT IgG binds to the integrin are unknown. We recently identified a unique sequence of the GPIIb/IIIa, Arg254-Trp-Lys327 (RKL), that is necessary for HIT antibody binding. We have now shown that the RKL sequence has several other roles in the platelet, as expression of this peptide blocked GPIIb/IIIa-mediated platelet aggregation and cell adhesion to fibrinogen, vitronectin, collagens and immobilized fibronectin. These results are consistent with a role for the RKL sequence in regulating the binding of other ligands to the integrin. This finding has allowed us to demonstrate that both the binding of platelet-bound HIT IgG to GPIIb/IIIa and activation of platelets are dependent upon the same ubiquitin/proteasome pathway. Since the peptide mimicking the
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