Endothelial cell protein C receptor

A type I transmembrane protein called endothelial cell protein C receptor (EPCR), which is expressed at high levels exclusively on a subset of endothelial cells, has also been identified. EPCR has a role in the protein C pathway (30). EPCR binds to both protein C and activated protein C (APC) with equal affinity. Activation of protein C presumably requires interaction of the protein C-EPCR complex with the thrombin-thrombomodulin complex. APC that is formed as a result of this interaction is reversibly bound to EPCR until it dissociates to react subsequently with protein S. The APC-protein S complex inactivates activated factor V (Va). 

Regan, L. M., Mnllica, J. S., Rezaic, A. R, and Esmon, C, T. (1997). The interaction between the endothelial cell protein C receptor and pmteln C is dictated by the y-carboxyglu-tamic acid domain of protein t. /. fjfni. Clicm. 272,26279-26284,... 

White, S. J., Simmonds, R. E., Lane, D. A., Baker, A. H. (2005). Efficient isolation of peptide ligands for the endothelial cell protein C receptor (EPCR) using candidate receptor phage display biopanning. Peptides, 26, 1264-1269. 

Sidhu JS, Cowan D, Kaski JC, The effects of Rosiglitazone, a peroxisome proliferator activated receptor gamma agonist, on markers of endothelial cell activation, C-reactive protein, and fibrinogen levels in non-diabetic coronary artery disease patients. J Am Coll Cardiol 2003 42 1757-1763. 

Sexl V, Mancusi G, Holler C, Gloria-Maercker E, Schutz W, Freissmuth M. 1997. Stimulation of the mitogen-activated protein kinase via the A2A-adenosine receptor in primary human endothelial cells. J Biol Chem 272 5792-5799. 

Kanse SM, Kost C, Wilhelm OG, Andreasen PA, Preissner KT. The urokinase receptor is a major vitronectin-binding protein on endothelial cells. Exp Cell Res 1996 224(2) 344-353. 

Lee, H., Shi, W., Tontonoz, P., Wang, S., Subbanagouder, G., Hedrick, C.C., Hama, S., Borromeo, C., Evans, R.M., Berliner, J.A., and Nagy, L., 2000, Role for peroxisome prohferator-activated receptor [alpha] in oxidized phospholipid-induced synthesis of monocyte chematactic protein-1 and interleukin-8 by endothelial cells, Circ. Res. 87 516-521. 

Two different mechanisms have been proposed to explain the cellular events involved in the Ox-LDL-induced endothelin secretion in endothelial cells. Boulanger et al. [126-127] demonstrated that the peptide secretion is mediated by the stimulation of the scavenger receptors by Ox-LDL and that protein kinase C interferes in this process, while Martin-Nizard et al. [128] have reported that lysophosphatidylcholine (LPC) in Ox-LDL exerts a major role in the induction of the secretion of immunoreactive endothelin in endothelial cells. However, M. Jougasaki et al. [133] recently published opposing results. They showed that Ox-LDL suppresses the endothelin secretion by LPC in cultured vascular endothelial cells. 

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