Glycoprotein Ib-IX-V complex

The GPIb-IX-V complex is a profuse membrane receptor complex originating in megakaryocytes and exclusively functional on the surface of platelets.[1] It primarily functions to mediate the first critical step in platelet adhesion, by facilitating binding to von Willebrand factor (VWF) on damaged sub-endothelium under conditions of high fluid shear stress.[2][3] Although the primary ligand for the GPIb-V-IX receptor is VWF, it can also bind to a number of other ligands in the circulation such as thrombin, P-selectin, factor XI, factor XII, high molecular weight kininogen as well as bacteria. GPIb-IX-V offers a critical role in thrombosis, metastasis, and the life cycle of platelets, and is implicated in a number of thrombotic pathological processes such as stroke or myocardial infarction.[1][2]

  1. ^ a b Li R, Emsley J (April 2013). "The organizing principle of the platelet glycoprotein Ib-IX-V complex". J. Thromb. Haemost. 11 (4): 605–14. doi:10.1111/jth.12144. PMC 3696474. PMID 23336709.
  2. ^ a b McEwan PA, Andrews RK, Emsley J (November 2009). "Glycoprotein Ibalpha inhibitor complex structure reveals a combined steric and allosteric mechanism of von Willebrand factor antagonism". Blood. 114 (23): 4883–5. doi:10.1182/blood-2009-05-224170. PMID 19726719.
  3. ^ López JA, Andrews RK, Afshar-Kharghan V, Berndt MC (June 1998). "Bernard-Soulier syndrome". Blood. 91 (12): 4397–418. doi:10.1182/blood.V91.12.4397. PMID 9616133.