Phosphoproteomic analysis of thrombin- and p38 MAPK-regulated signaling networks in endothelial cells.

ABSTRACT: Endothelial dysfunction is a hallmark of inflammation and is mediated by inflammatory factors that signal through G protein-coupled receptors including protease-activated receptor-1 (PAR1). PAR1, a receptor for thrombin, signals via the small GTPase RhoA and myosin light chain intermediates to facilitate endothelial barrier permeability. PAR1 also induces endothelial barrier disruption through a p38 mitogen-activated protein kinase-dependent pathway, which does not integrate into the RhoA/MLC pathway; however, the PAR1-p38 signaling pathways that promote endothelial dysfunction remain poorly defined. To identify effectors of this pathway, we performed a global phosphoproteome analysis of thrombin signaling regulated by p38 in human cultured endothelial cells using multiplexed quantitative

SUBMITTER: Molinar-Inglis O 

PROVIDER: S-EPMC8987612 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature