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

Ítems similars

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• Thrombin inhibits HMGB1-mediated proinflammatory signaling responses when endothelial protein C receptor is occupied by its natural ligand
  per: Bae, Jong-Sup, et al.
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• Thrombin Inhibits Nuclear Factor κB and RhoA Pathways in Cytokine-stimulated Vascular Endothelial Cells when EPCR is Occupied by Protein C
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• Factor X/Xa Elicits Protective Signaling Responses in Endothelial Cells Directly via PAR-2 and Indirectly via Endothelial Protein C Receptor-dependent Recruitment of PAR-1
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• The ligand occupancy of endothelial protein C receptor switches the protease-activated receptor 1-dependent signaling specificity of thrombin from a permeability-enhancing to a barrier-protective response in endothelial cells
  per: Bae, Jong-Sup, et al.
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