http://purl.uniprot.org/citations/27761847 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/27761847 | http://www.w3.org/2000/01/rdf-schema#comment | "Fibrosis is the dramatic consequence of a dysregulated reparative process in which activated fibroblasts (myofibroblasts) and Transforming Growth Factor β1 (TGFβ1) play a central role. When exposed to TGFβ1, fibroblast and epithelial cells differentiate in myofibroblasts; in addition, endothelial cells may undergo endothelial-to-mesenchymal transition (EndoMT) and actively participate to the progression of fibrosis. Recently, the role of αv integrins, which recognize the Arg-Gly-Asp (RGD) tripeptide, in the release and signal transduction activation of TGFβ1 became evident. In this study, we present a class of triazole-derived RGD antagonists that interact with αvβ3 integrin. Above different compounds, the RGD-2 specifically interferes with integrin-dependent TGFβ1 EndoMT in Endothelial Colony-Forming Cells (ECPCs) derived from circulating Endothelial Precursor Cells (ECPCs). The RGD-2 decreases the amount of membrane-associated TGFβ1, and reduces both ALK5/TGFβ1 type I receptor expression and Smad2 phosphorylation in ECPCs. We found that RGD-2 antagonist reverts EndoMT, reducing α-smooth muscle actin (α-SMA) and vimentin expression in differentiated ECPCs. Our results outline the critical role of integrin in fibrosis progression and account for the opportunity of using integrins as target for anti-fibrotic therapeutic treatment."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.org/dc/terms/identifier | "doi:10.1007/s11010-016-2847-2"xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/author | "Bianchini F."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/author | "Calorini L."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/author | "Pupi A."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/author | "Menchi G."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/author | "Trabocchi A."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/author | "Mazzanti B."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/author | "Biagioni A."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/author | "Fabbrizzi P."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/author | "Peppicelli S."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/name | "Mol Cell Biochem"xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/pages | "99-110"xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/title | "Triazole RGD antagonist reverts TGFbeta1-induced endothelial-to-mesenchymal transition in endothelial precursor cells."xsd:string |
http://purl.uniprot.org/citations/27761847 | http://purl.uniprot.org/core/volume | "424"xsd:string |
http://purl.uniprot.org/citations/27761847 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27761847 |
http://purl.uniprot.org/citations/27761847 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/27761847 |
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