The P2Y₂ Receptor Interacts with VE-Cadherin and VEGF Receptor-2 to Regulate Rac1 Activity in Endothelial Cells.

ABSTRACT: Vascular endothelial cadherin (VE-cadherin) mediates homophylic adhesion between endothelial cells and is an important regulator of angiogenesis, blood vessel permeability and leukocyte trafficking. Rac1, a member of the Rho family of GTPases, controls VE-cadherin adhesion by acting downstream of several growth factors, including angiopoietin-1 and vascular endothelial growth factor (VEGF). Here we show that UTP-induced activation of the G_q protein-coupled P2Y₂ nucleotide receptor (P2Y₂R) in human coronary artery endothelial cells (HCAECs) activated Rac1 and caused a transient complex to form between P2Y₂R, VE-cadherin and VEGF receptor-2 (VEGFR-2). Knockdown of VE-cadherin expression with siRNA did not affect UTP-induced activation of extracellu

SUBMITTER: Liao Z 

PROVIDER: S-EPMC4314728 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature