Thrombin stimulates human endothelial arginase enzymatic activity via RhoA/ROCK pathway: implications for atherosclerotic endothelial dysfunction

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Animals Aorta, Thoracic/physiopathology Apolipoproteins E/genetics Arginase/*metabolism Arteriosclerosis/*enzymology/physiopathology Cells, Cultured Endothelial Cells/enzymology Endothelium, Vascular/*enzymology/physiopathology Enzyme Activation Humans Intracellular Signaling Peptides and Proteins Isoenzymes/metabolism Male Mice Mice, Inbred C57BL Mice, Knockout Mutation Nitric Oxide Synthase/biosynthesis Nitric Oxide Synthase Type II Nitric Oxide Synthase Type III Protein-Serine-Threonine Kinases/antagonists & inhibitors/genetics/*physiology Signal Transduction Thrombin/*physiology Umbilical Veins/cytology rhoA GTP-Binding Protein/antagonists & inhibitors/genetics/*physiology


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X. F. Ming et al., « Thrombin stimulates human endothelial arginase enzymatic activity via RhoA/ROCK pathway: implications for atherosclerotic endothelial dysfunction », Serveur académique Lausannois, ID : 10.1161/01.CIR.0000142867.26182.32


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Abstract 0

BACKGROUND: Arginase competes with endothelial nitric oxide synthase (eNOS) for the substrate l-arginine and decreases NO production. This study investigated regulatory mechanisms of arginase activity in endothelial cells and its role in atherosclerosis. METHODS AND RESULTS: In human endothelial cells isolated from umbilical veins, thrombin concentration- and time-dependently stimulated arginase enzymatic activity, reaching a 1.9-fold increase (P

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