| http://purl.uniprot.org/citations/17379830 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17379830 | http://www.w3.org/2000/01/rdf-schema#comment | "The endothelial cell membrane glycoprotein thrombomodulin (TM) plays a critical role in the regulation of coagulation. TM is an essential cofactor in protein C activation by thrombin, and a direct inhibitor of thrombin-induced platelet activation and fibrinogen clotting. Protease nexin-1 (PN-1) is a serpin synthesized and secreted by a variety of cells including endothelial cells. PN-1 bound to the cell surface through interactions with glycosaminoglycans, is an efficient inhibitor of thrombin and controls thrombin-induced cell responses. An investigation of the interaction of PN-1 with TM using purified proteins and cultured human aortic endothelial cells was performed. Purified PN-1 was observed to bind to purified TM in a concentration-dependent manner. Double immunofluorescence studies indicated that PN-1 and TM were colocalized at the endothelial cell surface from which they were coprecipitated. Pretreatment of the cells with chondroitinase ABC greatly decreased the amount of the PN-1 associated to TM at the cell surface demonstrating the involvement of the TM chondroitin-sulfate chain in the formation of complexes. The inhibitory activity of the PN-1/TM complexes on the catalytic activity of thrombin, and on thrombin-induced fibrinogen clotting, was markedly enhanced when compared with the inhibitory activity of each partner. PN-1-overexpressing human aortic endothelial cells and PN-1-underexpressing human aortic endothelial cells exhibited respectively a significantly reduced ability and enhanced capacity to activate protein C. Furthermore, PN-1 decreased the cofactor activity of TM on thrombin activable fibrinolysis inhibitor activation by thrombin. These data show for the first time that PN-1 forms complexes with TM and modulates its anticoagulant activity."xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.org/dc/terms/identifier | "doi:10.1161/01.res.0000265066.92923.ee"xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/author | "Pouzet C."xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/author | "Jandrot-Perrus M."xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/author | "Bouton M.C."xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/author | "Arocas V."xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/author | "Richard B."xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/author | "Venisse L."xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/name | "Circ Res"xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/pages | "1174-1181"xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/title | "Protease nexin-1 interacts with thrombomodulin and modulates its anticoagulant effect."xsd:string |
| http://purl.uniprot.org/citations/17379830 | http://purl.uniprot.org/core/volume | "100"xsd:string |
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