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Structure and Function of the Endothelial Cell Protein C Receptor

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Recent Advances in Thrombosis and Hemostasis 2008
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Abstract

The endothelial cell protein C receptor (EPCR) is a cell surface transmembrane glycoprotein and a novel member of the CD1/major histocompatibility complex class 1 superfamily. It was originally found to express specifically in endothelial cells, but recent studies demonstrated wide distribution of the molecule. EPCR is capable of high-affinity binding specific for protein C (PC) and activated protein C (APC). PC binding to EPCR results in acceleration of conversion to APC mediated by the thrombin/thrombomodulin complex, and it is required for regulation of blood coagulation. APC also binds to EPCR, and the APC-EPCR complex was found to promote activation of protease-activated receptor-1 (PAR-1). Binding to EPCR modulates the enzymatic specificity of APC and enables proteolysis of PAR-1, leading to intracellular signal transduction. The EPCR-APC-PAR-1 signaling induces various genes and explains the antiinflammatory, antiapoptotic, and wound healing effects of APC.

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Fukudome, K. (2008). Structure and Function of the Endothelial Cell Protein C Receptor. In: Tanaka, K., Davie, E.W., Ikeda, Y., Iwanaga, S., Saito, H., Sueishi, K. (eds) Recent Advances in Thrombosis and Hemostasis 2008. Springer, Tokyo. https://doi.org/10.1007/978-4-431-78847-8_13

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  • DOI: https://doi.org/10.1007/978-4-431-78847-8_13

  • Publisher Name: Springer, Tokyo

  • Print ISBN: 978-4-431-78846-1

  • Online ISBN: 978-4-431-78847-8

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