The mechanism of IGPR-1 activation in endothelial cells

• Main Author: Tahboub, Rawan
• Other Authors: Rahimi, Nader
• Language: en_US
• Published: 2018
• Subjects: Pathology; Endothelial cells; IGPR-1
• Online Access: https://hdl.handle.net/2144/30874

Disruption of the integrity of vascular endothelium plays an essential role in the development and the progression of numerous human diseases, including sepsis, atherosclerosis and others. A complex array of transmembrane adhesive proteins located in junctional structures, support endothelial integrity and control vascular permeability. Furthermore, they are able to transmit intracellular signals to coordinate various endothelial biological responses to insure normal vascular function. Immunoglobulin-containing and proline rich receptor-1 (IGPR-1) is a novel cell adhesion molecule that is involved in angiogenesis and in the regulation of endothelial permeability. IGPR-1 is phosphorylated at Ser220, which is required for its ability to mediate actin fibril reorganization. In this study, we demonstrate that the phosphorylation of IGPR-1 at Ser220 is stimulated by cell spreading and cell adhesion in porcine aortic endothelial (PAE) cells. Blocking homophilic trans-dimerization of IGPR-1 by a blocking antibody inhibited cell-density phosphorylation of IGPR-1. More importantly, phosphorylation of IGPR-1 at Ser220 is increased in PAE cells under shear stress, which was essential for IGPR-1-mediated endothelial cell alignment in response to shear stress. Taken together, this study demonstrate that IGPR-1 activity is regulated be endothelial cell spreading and density. And its activity plays an important role in endothelial cell alignment in response to shear stress. === 2020-07-03T00:00:00Z