EMMPRIN/CD147 is a novel coreceptor of VEGFR-2 mediating its activation by VEGF
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hdl:2117/84621
Tipus de documentArticle
Data publicació2015-03-23
EditorWiley
Condicions d'accésAccés obert
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Reconeixement-NoComercial-SenseObraDerivada 3.0 Espanya
Abstract
EMMPRIN/CD147 is mainly known for its protease inducing function but a role in promoting tumor angiogenesis has also been demonstrated. This study provides evidence that EMMPRIN is a new coreceptor for the VEGFR-2 tyrosine kinase receptor in both endothelial and tumor cells, as it directly interacts with it and regulates its activation by its VEGF ligand, signalling and functional consequences both in vitro and in vivo. Computational docking analyses and mutagenesis studies identified a molecular binding site in the extracellular domain of EMMPRIN located close to the
cell membrane and containing the amino acids 195/199. EMMPRIN is overexpressed in cancer and hence is able to further potentiate VEGFR-2 activation, suggesting that a combinatory therapy of an antiangiogenic drug together with an inhibitor of EMMPRIN/VEGFR-2 interaction may have a greater impact on inhibiting angiogenesis
and malignancy.
CitacióKhayati, Farah [et al.]. EMMPRIN/CD147 is a novel coreceptor of VEGFR-2 mediating its activation by VEGF. "Oncotarget", 23 Març 2015, vol. 6, núm. 12, p. 9766-9780.
ISSN1949-2553
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EMMPRIN CD147 is a novel coreceptor.pdf | 5,149Mb | Visualitza/Obre |