Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
endothelial VE-cadherin is involved in the reconstruction of the blood-brain barrier following ischemic stroke
TM, especially TME45, maintains vascular integrity, at least in part, via Src (show SRC Proteins) signaling.
These results suggest that SHP-2-via association with ICAM-1-mediates ICAM-1-induced Src activation and modulates VE-cadherin switching association with ICAM-1 or actin, thereby negatively regulating neutrophil adhesion to endothelial cells and enhancing their transendothelial migration.
Galphas (show GNAS Proteins) depletion blocks the S1PR1 (show S1PR1 Proteins)-activation induced VE-cadherin stabilization at junctions.
Rab11a/Rab11 (show RAB11A Proteins) family-interacting protein 2 (show RAB11FIP2 Proteins)-mediated VE-cadherin recycling is required for formation of adherens junctions and restoration of vascular endothelial barrier integrity.
These findings together demonstrate the essential role of KDM4A (show KDM4A Proteins) and KDM4C (show KDM4C Proteins) in orchestrating mESC differentiation to endothelial cells through the activation of Flk1 (show KDR Proteins) and VE-cadherin promoters, respectively
In the absence of Tie-2 (show TEK Proteins), VE-PTP (show PTPRB Proteins) inhibition destabilizes endothelial barrier integrity in agreement with the VE-cadherin-supportive effect of VE-PTP (show PTPRB Proteins).
identification of novel components of the adherens junction complex, and introduction of a novel molecular mechanism through which the VE-cadherin complex controls YAP (show YAP1 Proteins) transcriptional activity
Endotoxin challenge initiates interrelated changes in microvessel Cx43 (show GJA1 Proteins), VE-cadherin, and microvessel permeability, with changes in Cx43 (show GJA1 Proteins) temporally leading the other responses.
Mutating Y731 in the cytoplasmic tail of VE-cadherin, known to selectively affect leukocyte diapedesis, but not the induction of vascular permeability, attenuates bleeding.
zebrafish Cdh5 negatively regulates mobilization of aorta-gonad-mesonephros-derived hematopoietic stem cells
reveal biologically relevant changes in VE-cadherin tension that occur as the dorsal aorta matures and upon genetic and chemical perturbations during embryonic development
VE-cadherin and Esama (show ESAM Proteins) have distinct and redundant functions during blood vessel morphogenesis
C1qr (show CD93 Proteins) and c1qrl regulate angiogenesis through controlling endothelial cdh5 expression.
the conserved targeting of VE-cadherin by miR (show MYLIP Proteins)-22 regulates endothelial inflammation, tissue injury, and angiogenesis.
VE-cadherin/amotL2 (show AMOTL2 Proteins) complex is responsible for transmitting mechanical force between endothelial cells for the coordination of cellular morphogenesis consistent with aortic lumen expansion and function.
Cdh5 organizes junctional and cortical actin cytoskeletons and F-actin polymerization during endothelial cell elongation.
Regulatory pathways affecting vascular stabilization via VE-cadherin dynamics
suggest that Ve-cadherin and Moesin1 (show MSN Proteins) function to establish and maintain apical/basal polarity during multicellular lumen formation in the intersegmental vessels
results demonstrate a significant role for VE-cadherin in cardiac development independent of its effects on the formation of the peripheral vasculature
VE-cadherin internalization from tensile adherens junctions is inhibited by Pacsin2 (show PACSIN2 Proteins) protein.
It was found that the levels of integrin alpha1 and VE-cadherin mRNA increased during co-culturing of activated endothelium cells with mesenchymal stromal cells.
Endothelial flow mechanotransduction through the junctional complex is mediated by a specific pool of VE-cadherin that is phosphorylated on cytoplasmic tyrosine Y658 and bound to LGN (show GPSM2 Proteins).
BMP4 (show BMP4 Proteins) controls leukocyte recruitment through a VE-cadherin-dependent mechanism
hsa (show CD24 Proteins)-miR (show MLXIP Proteins)-6086 is induced by TNFalpha (show TNF Proteins) and mediates TNFalpha (show TNF Proteins)-induced HUVEC growth inhibition through downregulating CDH5 expression. Hence, hsa (show CD24 Proteins)-miR (show MLXIP Proteins)-6086 might be a new target for treating TNFalpha (show TNF Proteins)-induced endothelial dysfunction.
activation of PAR2 (show F2RL1 Proteins) compromises the vascular endothelial barrier function by suppressing the expression of Ve-cadherin.
C. pneumoniae infection promotes monocyte transendothelial migration by increasing vascular endothelial cell permeability via the tyrosine phosphorylation and internalization of VE-cadherin in vascular endothelial cells.
The study shows a VE-cadherin-mediated cell dynamics and an endothelial-dependent proliferation in a differentiation-dependent manner.
VE-cadherin activated cell stiffening depends on substrate stiffness. Force loading VE-cadherin receptors triggers cell-matrix junction remodeling. Local, VE-cadherin force transduction signals at the cell level do not alter the mechanical balance of endothelial colonies.
HIF-2alpha (show EPAS1 Proteins) and VM were overexpressed in pancreatic cancer tissues and were associated with poor pathological characteristics. HIF-2alpha (show EPAS1 Proteins) contributes to VM formation by regulating the expression of VE-cadherin through the binding of the transcription factor Twist1 (show TWIST1 Proteins) to the promoter of VE-cadherin in pancreatic cancer both in vitro and in vivo.
VE-cadherin induces opposing growth signals.
investigated the role of catenin p120 (show CTNND1 Proteins)-VE-cadherin interaction in regulation of barrier function in confluent endothelial monolayers
Vascular endothelial-cadherin regulates cytoskeletal tension, cell spreading, and focal adhesions by stimulating RhoA (show RHOA Proteins)
a VE-cadherin-dependent pathway may link T2-TrpRS (show WARS Proteins) to inhibition of new blood vessel formation
results indicate that integrin engagement disrupts VE-cadherin-containing adherens junctions via the activation of Src, but not Ras, possibly as a result of modulation of the actin network
exposure of BAECs to hydrostatic pressure (PHYSIOLOGIC PRESSURE) may downregulate the expression of VE-cadherin, resulting in loss of contact inhibition followed by increased proliferation and formation of a multilayered structure
In all, these results demonstrate that cell-cell contact signals through VE-cadherin, RhoA, and intracellular tension in the actin cytoskeleton to regulate proliferation.
Low expressions of eNOS3 and Ve-cadherin in the salvaged sub-healthy microvascular endothelium of infarcted and marginal areas suggest that endothelial system is impaired at 7-day of reperfused acute myocardial infarction.
This gene is a classical cadherin from the cadherin superfamily and is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Functioning as a classic cadherin by imparting to cells the ability to adhere in a homophilic manner, the protein may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. An alternative splice variant has been described but its full length sequence has not been determined.
cadherin 5, type 2, VE-cadherin (vascular endothelium)
, cadherin 5, type 2, VE-cadherin (vascular epithelium)
, vascular endothelial cadherin
, VE-cadherin (vascular epithelium)
, type 2
, 7B4 antigen
, cd144 antigen
, endothelial-specific cadherin
, VE cadherin