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http://purl.uniprot.org/citations/22685328http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22685328http://www.w3.org/2000/01/rdf-schema#comment"VE-cadherin-mediated cell-cell junction weakening increases paracellular permeability in response to both angiogenic and inflammatory stimuli. Although Semaphorin 3A has emerged as one of the few known anti-angiogenic factors to exhibit pro-permeability activity, little is known about how it triggers vascular leakage. Here we report that Semaphorin 3A induced VE-cadherin serine phosphorylation and internalisation, cell-cell junction destabilisation, and loss of barrier integrity in brain endothelial cells. In addition, high-grade glioma-isolated tumour-initiating cells were found to secrete Semaphorin 3A, which promoted brain endothelial monolayer permeability. From a mechanistic standpoint, Semaphorin 3A impinged upon the basal activity of the serine phosphatase PP2A and disrupted PP2A interaction with VE-cadherin, leading to cell-cell junction disorganization and increased permeability. Accordingly, both pharmacological inhibition and siRNA-based knockdown of PP2A mimicked Semaphorin 3A effects on VE-cadherin. Hence, local Semaphorin 3A production impacts on the PP2A/VE-cadherin equilibrium and contributes to elevated vascular permeability."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.org/dc/terms/identifier"doi:10.1242/jcs.108282"xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Kettler G."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Dubois S."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Auffray C."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Dwyer J."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Treps L."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Chneiweiss H."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Bidere N."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Gavard J."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Galan-Moya E.M."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Hebda J.K."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/author"Le Guelte A."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/name"J Cell Sci"xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/pages"4137-4146"xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/title"Semaphorin 3A elevates endothelial cell permeability through PP2A inactivation."xsd:string
http://purl.uniprot.org/citations/22685328http://purl.uniprot.org/core/volume"125"xsd:string
http://purl.uniprot.org/citations/22685328http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22685328
http://purl.uniprot.org/citations/22685328http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22685328
http://purl.uniprot.org/uniprot/#_A0A0C4DG50-mappedCitation-22685328http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22685328
http://purl.uniprot.org/uniprot/#_D3Z2A7-mappedCitation-22685328http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22685328
http://purl.uniprot.org/uniprot/#_E9Q668-mappedCitation-22685328http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22685328
http://purl.uniprot.org/uniprot/#_A0A803Z7F8-mappedCitation-22685328http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22685328