PECAM-1 Affects GSK-3β-Mediated β-Catenin Phosphorylation and Degradation

摘要: Platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) regulates a variety of and immune biological responses. PECAM-1-null mice exhibit prolonged increased permeability after inflammatory insults. We observed that in cells (ECs), β-catenin remained tyrosine phosphorylated, coinciding with sustained increase permeability. Src homology 2 domain containing phosphatase (SHP-2) association was diminished ECs, suggesting lack PECAM-1 inhibits the ability this adherens junction component to become dephosphorylated, promoting β-Catenin/Glycogen synthase kinase 3 (GSK-3β) serine phosphorylation levels were expression reduced ECs. Glycogen (inactivation) blunted ECs histamine treatment or shear stress. Our data suggest serves as critical dynamic regulator barrier On stimulation by vasoactive substance stress, became enabling recruitment SHP-2 tyrosine-phosphorylated its cytoplasmic domain, facilitating dephosphorylation β-catenin, allowing reconstitution junctions. In addition, modulated regulating activity GSK-3β, which turn affected proteosomal degradation, affecting reform junctions timely fashion.