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- W2023684807 abstract "Background Cross-talk between integrins and cadherins regulates cell function. We tested the hypothesis that vitronectin (VN), a multi-functional adhesion molecule present in the extracellular matrix and plasma, regulates vascular permeability via effects on VE-cadherin, a critical regulator of endothelial cell (EC) adhesion. Methodology/Principal Findings Addition of multimeric VN (mult VN) significantly increased VE-cadherin internalization in human umbilical vein EC (HUVEC) monolayers. This effect was blocked by the anti-αVβ3 antibody, pharmacological inhibition and knockdown of Src kinase. In contrast to mult VN, monomeric VN did not trigger VE-cadherin internalization. In a modified Miles assay, VN deficiency impaired vascular endothelial growth factor-induced permeability. Furthermore, ischemia-induced enhancement of vascular permeability, expressed as the ratio of FITC-dextran leakage from the circulation into the ischemic and non-ischemic hindlimb muscle, was significantly greater in the WT mice than in the Vn−/− mice. Similarly, ischemia-mediated macrophage infiltration was significantly reduced in the Vn−/− mice vs. the WT controls. We evaluated changes in the multimerization of VN in ischemic tissue in a mouse hindlimb ischemia model. VN plays a previously unrecognized role in regulating endothelial permeability via conformational- and integrin-dependent effects on VE-cadherin trafficking. Conclusion/Significance These results have important implications for the regulation of endothelial function and angiogenesis by VN under normal and pathological conditions." @default.
- W2023684807 created "2016-06-24" @default.
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- W2023684807 date "2012-05-11" @default.
- W2023684807 modified "2023-10-15" @default.
- W2023684807 title "Vitronectin Increases Vascular Permeability by Promoting VE-Cadherin Internalization at Cell Junctions" @default.
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- W2023684807 doi "https://doi.org/10.1371/journal.pone.0037195" @default.
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