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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 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 depletion blocks the S1PR1-activation induced VE-cadherin stabilization at junctions.
Rab11a/Rab11 family-interacting protein 2-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 and KDM4C in orchestrating mESC differentiation to endothelial cells through the activation of Flk1 and VE-cadherin promoters, respectively
In the absence of Tie-2, VE-PTP inhibition destabilizes endothelial barrier integrity in agreement with the VE-cadherin-supportive effect of VE-PTP.
identification of novel components of the adherens junction complex, and introduction of a novel molecular mechanism through which the VE-cadherin complex controls YAP transcriptional activity
Endotoxin challenge initiates interrelated changes in microvessel Cx43, VE-cadherin, and microvessel permeability, with changes in Cx43 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.
mRNA of HIF-2alpha and Ets-1 were significantly increased by HIF-3alpha ablation. Both factors activate the VE-cadherin gene, the transcriptional repression of these factors by HIF-3alpha is important for silencing the irrelevant expression of the VE-cadherin
iPS cell-derived Flk1(+)VE-cadherin(+) cells expressing the Er71 are as angiogenic as mES cell-derived cells and incorporate into CD31(+) neovessels.
VE-cadherin tyrosine phosphorylation at Y685 is a physiological and hormonally regulated process in female reproductive organs.
Conclude that the site Y685 in VE-cadherin is involved in the physiological regulation of capillary permeability in mouse ovary/uterus.
Findings support the importance of adhesion molecules (VE-cadherin and CD31), survivin, and Ajuba in modulating the Hippo pathway, which regulates, in part, proliferation and survival in hemangioendotheliomas.
role of eNOS and VE-cadherin in angiopoietin-1 regulation of microvascular reactivity and protection of the microcirculation during acute endothelial dysfunction
Fusing VE-cadherin to alpha-catenin presents a mutation, which leads to embryonic lethality, due to a lack of fetal liver hematopoiesis and severe lymphedema but no detectable defects in blood vessel formation and remodeling.
Tyr685 and Tyr731 of VE-cadherin distinctly and selectively regulate the induction of vascular permeability or leukocyte extravasation
CD44 regulation of endothelial cell proliferation and apoptosis via modulation of CD31 and VE-cadherin expression.
Sirolimus-FKBP12.6 impairs endothelial barrier function by activation of protein kinase C-alpha and downstream disruption of the p120-VE cadherin interaction in vascular endothelium.
Wnt/beta-catenin signaling regulates VE-cadherin-mediated anastomosis of brain capillaries by counteracting S1pr1 signaling in the process of neovascularization of the central nervous system and blood-brain barrier formation.
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 have distinct and redundant functions during blood vessel morphogenesis
C1qr and c1qrl regulate angiogenesis through controlling endothelial cdh5 expression.
the conserved targeting of VE-cadherin by miR-22 regulates endothelial inflammation, tissue injury, and angiogenesis.
VE-cadherin/amotL2 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 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
fli1, and etsrp, demonstrated that erg and fli1 act cooperatively and are required for angiogenesis possibly via direct regulation of an endothelial cell junction molecule, VE-cadherin
VE-cadherin plays an essential role in vascular development
VE-cadherin internalization from tensile adherens junctions is inhibited by Pacsin2 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.
BMP4 controls leukocyte recruitment through a VE-cadherin-dependent mechanism
hsa-miR-6086 is induced by TNFalpha and mediates TNFalpha-induced HUVEC growth inhibition through downregulating CDH5 expression. Hence, hsa-miR-6086 might be a new target for treating TNFalpha-induced endothelial dysfunction.
activation of PAR2 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 and VM were overexpressed in pancreatic cancer tissues and were associated with poor pathological characteristics. HIF-2alpha contributes to VM formation by regulating the expression of VE-cadherin through the binding of the transcription factor Twist1 to the promoter of VE-cadherin in pancreatic cancer both in vitro and in vivo.
These findings support a general role for VE-cadherin and other RGD cadherins as critical regulators of lung and liver metastasis in multiple solid tumours. These results pave the way for cadherin-specific RGD targeted therapies to control disseminated metastasis in multiple cancers.
This study demonstrated that changes in gene expression of CDH5 and CLDN5 due to shear stress within individual differentiations also revealed no trend.
Data suggest that cadherin 5 (CDH5) may play a key role in hematogenous recurrence of advanced gastric cancer and may be a viable treatment target.
The present study investigated the interplay of VEGF-A165a isoform, the anti-angiogenic VEGF-A165b, placental growth factor (PIGF) and their receptors, VEGFR1 and VEGFR2.on junctional occupancy of VE-cadherin and macromolecular leakage in human endothelial monolayers and the perfused placental microvascular bed.
CDH5 and FABP1 expression levels were both elevated in drug-induced liver injury.
Varenicline promotes HUVEC migration by lowering VE-cadherin expression due to activated ERK/p38/JNK signaling through alpha7 nAChR. These processes probably contribute to varenicline-aggravated atherosclerotic plaque.
Plakoglobin maintains the integrity of vascular endothelial cell junctions and regulates VEGF-induced phosphorylation of VE-cadherin
Endothelial Tspan5- and Tspan17-ADAM10 complexes may regulate inflammation by maintaining normal VE-cadherin expression and promoting T lymphocyte transmigration.
Study found that high VE-cadherin gene expression levels were associated with low expression of miR-27b and that the latter directly bound to its 3'UTR to regulate its expression.
VE-cadherin induces opposing growth signals.
investigated the role of catenin p120-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
a VE-cadherin-dependent pathway may link T2-TrpRS 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