Protease activated receptor 1 (PAR-1) activation by thrombin is protective in human pulmonary artery endothelial cells if endothelial protein C receptor is occupied by its natural ligand

We recently demonstrated that the occupancy of endothelial protein C receptor (EPCR) by its natural ligand activated protein C (APC)/protein C switches the protease activated receptor 1 (PAR-1)-dependent signaling specificity of thrombin from a disruptive to a protective effect in cultured human umb...

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Bibliographic Details
Published in:	Thrombosis and haemostasis Vol. 100; no. 1; p. 101
Main Authors:	Bae, Jong-Sup, Rezaie, Alireza R
Format:	Journal Article
Language:	English
Published:	Germany 01.07.2008
Subjects:	Antigens, CD - metabolism Apoptosis beta-Cyclodextrins - pharmacology Capillary Permeability Caveolin 1 - metabolism Cell Adhesion Cell Line, Tumor Cells, Cultured Cholesterol - deficiency Cytoprotection Dose-Response Relationship, Drug Endothelial Cells - drug effects Endothelial Cells - metabolism Endothelial Cells - pathology Endothelial Protein C Receptor Humans Inflammation - metabolism Ligands Lipopolysaccharides - pharmacology Membrane Microdomains - metabolism Monocytes - metabolism Mutation Peptides - pharmacology Protein C - genetics Protein C - metabolism Pulmonary Artery - drug effects Pulmonary Artery - metabolism Pulmonary Artery - pathology Receptor, PAR-1 - agonists Receptor, PAR-1 - genetics Receptor, PAR-1 - metabolism Receptors, Cell Surface - metabolism Receptors, Lysosphingolipid - metabolism Receptors, Thrombin - metabolism RNA Interference RNA, Small Interfering - metabolism Signal Transduction - drug effects Thrombin - metabolism Tumor Necrosis Factor-alpha - metabolism
ISSN:	0340-6245
Online Access:	Get more information
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