Phosphorylation of VE-cadherin is modulated by haemodynamic forces and contributes to the regulation of vascular permeability in vivo

摘要: Endothelial adherens junctions maintain vascular integrity. Arteries and veins differ in their permeability but whether organization strength of vary has not been demonstrated vivo. Here we report that endothelial cadherin, an specific adhesion protein located at junctions, is phosphorylated Y658 Y685 vivo arteries under resting conditions. This difference due to shear stress-induced junctional Src activation veins. Phosphorylated endothelial-cadherin internalized ubiquitinated response permeability-increasing agents such as bradykinin histamine. Inhibition blocks cadherin phosphorylation bradykinin-induced permeability. Point mutation Y658F Y685F prevents internalization, ubiquitination increase by vitro. Thus, contributes a dynamic state sufficient the absence inflammatory agents.