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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908#_5 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908#_4 http://www.w3.org/ns/prov#value Factor XII deficiency has been postulated to be a risk factor for thrombosis suggesting that factor XII is an antithrombotic protein. The biochemical mechanism leading to this clinical observation is unknown. We have previously reported high molecular weight kininogen (HK) inhibition of thrombin-induced platelet aggregation by binding to the platelet glycoprotein (GP) Ib-IX-V complex. Although factor XII will bind to the intact platelet through GP Ibalpha (glycocalicin) without activation, we now report that factor XIIa (0. 37 microm), but not factor XII zymogen, is required for the inhibition of thrombin-induced platelet aggregation. Factor XIIa had no significant effect on SFLLRN-induced platelet aggregation. Moreover, an antibody to the thrombin site on protease-activated receptor-1 failed to block factor XII binding to platelets. Inhibition of thrombin-induced platelet aggregation was demonstrated with factor XIIa but not with factor XII zymogen or factor XIIf, indicating that the conformational exposure of the heavy chain following proteolytic activation is required for inhibition. However, inactivation of the catalytic activity of factor XIIa did not affect the inhibition of thrombin-induced platelet aggregation. Factor XII showed displacement of biotin-labeled HK (30 nm) binding to gel-filtered platelets and, at concentrations of 50 nm, was able to block 50% of the HK binding, suggesting involvement of the GP Ib complex. Antibodies to GP Ib and GP IX, which inhibited HK binding to platelets, did not block factor XII binding. However, using a biosensor, which monitors protein-protein interactions, both HK and factor XII bind to GP Ibalpha. Factor XII may serve to regulate thrombin binding to the GP Ib receptor by co-localizing with HK, to control the extent of platelet aggregation in vivo. http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908#_4 http://www.w3.org/ns/prov#wasQuotedFrom http://www.ncbi.nlm.nih.gov/pubmed/10801853 http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908#_5 http://www.w3.org/2000/01/rdf-schema#label Selventa http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908#assertion http://www.w3.org/ns/prov#hadPrimarySource http://www.ncbi.nlm.nih.gov/pubmed/10801853 http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908#assertion http://www.w3.org/ns/prov#wasDerivedFrom http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908#assertion http://www.w3.org/ns/prov#wasDerivedFrom http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908#_4 http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908#pubinfo http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908 http://purl.org/dc/terms/created 2014-07-03T14:29:50.982+02:00 http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908 http://purl.org/pav/createdBy http://orcid.org/0000-0001-6818-334X http://www.tkuhn.ch/bel2nanopub/RAE-TFJvcSjpAyjgPBI5pBEgdtk7BNWjik12ibdVGF908 http://purl.org/pav/createdBy http://orcid.org/0000-0002-1267-0234