Phosphoproteomic analysis of protease-activated receptor-1 biased signaling reveals unique modulators of endothelial barrier function

Thrombin, a procoagulant protease, cleaves and activates proteaseactivated receptor-1 (PAR1) to promote inflammatory responses and endothelial dysfunction. In contrast, activated protein C (APC), an anticoagulant protease, activates PAR1 through a distinct cleavage site and promotes anti-inflammator...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2020-03, Vol.117 (9), p.5039-5048
Hauptverfasser:	Lin, Ying, Wozniak, Jacob M., Grimsey, Neil J., Girada, Sravan, Patwardhan, Anand, Molinar-Inglis, Olivia, Smith, Thomas H., Lapek, John D., Gonzalez, David J., Trejo, JoAnn
Format:	Artikel
Sprache:	eng
Schlagworte:	Ablation Actin Activated protein C Adducin AKT protein Anticoagulants Biological Sciences Calmodulin-Binding Proteins Carrier Proteins Cleavage Depletion Disruption Endothelial cells Endothelial Cells - metabolism Humans Inflammation Kinases Mass spectrometry Mass spectroscopy Microfilament Proteins Modulators Permeability Phosphorylation Protease Protein C Inhibitor - metabolism Proteinase-activated receptor 1 Proteins Proteomics Receptor, PAR-1 - metabolism Regulators Signal Transduction Signaling siRNA Thrombin Thrombin - metabolism Transcription
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