CDH5

(redirected from VE-cadherin)

CDH5

A gene on chromosome 16q22.1 that encodes a calcium-dependent cell–cell adhesion glycoprotein (cadherin), which is involved in regulating cell–cell adhesions, mobility and proliferation of epithelial cells. CDH5 is thought to play a key role in endothelial cell biology by controlling cohesion and organisation of intercellular junctions.
References in periodicals archive ?
Abbreviations PA Panduratin A HUVECs human umbilical vein endothelial cells iTRAQ isobaric tags for relative and absolute quantification IPA Ingenuity Pathway Analysis mTOR mammalian target of rapamycin protein kinase VEGF vascular endothelial growth factor HIF1[alpha] hypoxia-inducible factor l[alpha] GRB-2 growth factor receptor-bound protein 2 STAB-1 stabilin-1 ICAM-2 Intercellular adhesion molecule-2 CTNND1 p120-catenin ARPC2 actin-related protein 2/3 complex subunit 2 STMN1 stathmin PI propidium iodide ANOVA one-way analysis of variance VE-cadherin vascular endothelial cadherin
Recent preclinical research has also shown that CA4P disrupts the molecular engagement of VE-cadherin, a junction protein important for endothelial cell survival and function, and inhibits the associated B-catenin/AKT signaling pathway, leading to rapid vascular collapse and necrosis.
Vascular endothelial growth factor induces VE-cadherin tyrosine phosphorylation in endothelial cells.
Differential localization of VE- and N-cadherins in human endothelial cells: VE-cadherin competes with N-cadherin for junctional localization.
Recent preclinical research has also shown that CA4P disrupts the molecular engagement of VE-cadherin, a junction protein important for endothelial cell survival and function, and inhibits the associated beta-catenin/AKT signaling pathway, leading to rapid vascular collapse and tumor cell death, or necrosis.
VE-cadherin and beta-catenin binding dynamics during histamine-induced endothelial hyperpermeability.
In vivo studies, including murine cornea angiogenesis and tumor models, which validate VE-Cadherin as a target will also be presented, announces Strategic Research Institute.
Preclinical research has shown that CA4P disrupts the molecular engagement of VE-cadherin, a junction protein important for endothelial cell survival and function, and inhibits the associated (beta)-catenin/AKT signaling pathway, leading to rapid vascular collapse and necrosis.
Recent preclinical research has also shown that CA4P disrupts the molecular engagement of VE-cadherin, a junction protein important for endothelial cell survival and function, and inhibits the associated (beta)-catenin/AKT signaling pathway, leading to rapid vascular collapse and tumor cell death, or necrosis.
Researchers observed that CA4P induces destabilization of VE-cadherin, a junctional protein between endothelial cells, and that the associated inhibition of the VE-cadherin/(beta)-catenin/Akt pathway influences many aspects of endothelial cell function, including inhibition of endothelial cell migration, proliferation and capillary tube formation pathways critical in angiogenesis.
In the study, researchers observed that CA4P induces destabilization of VE-cadherin and that the associated inhibition of the VE-cadherin/(beta)-catenin/Akt pathway profoundly influences many aspects of endothelial cell function, including inhibition of endothelial cell migration, proliferation and capillary tube formation pathways critical in angiogenesis.