The antiangiogenic activity of a soluble fragment of the VEGFR extracellular domain - 01/10/13
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Abstract |
Vascular endothelial growth factor (VEGF) is a key regulator of pathological angiogenesis and vascular permeability and overexpressed by most solid tumors. VEGF receptor-2 (VEGFR-2 or kinase-insert domain-containing receptor as it is called in human, KDR) is a specific receptor of VEGF with a high binding affinity. A solube recombinant extracellular domain 1-3 of human VEGFR-2 (rKDR1-3) was expressed in Escherichia coli (E. Coli) and purified from the bacterial periplasmic extracts by immobilized metal affinity chromatography and anion exchange chromatography to inhibit the VEGF-induced angiogenesis. A surface plasmon resonance (SPR) technology was adopted to analyze the affinity and kinetics constant between rKDR1-3 and VEGF165. Under the given experimental conditions, the association rate constant Ka was 1.06×105M−1 S−1, the dissociation rate Kd was 6.09×10−3 S−1, the dissociation constant KD was 5.74×10−8M. The effect of rKDR1-3 on VEGF-induced endothelial cell proliferation was studied using MTT assay, scratch-wound healing assay and chorioallantoic membrane (CAM) assay. The results showed that rKDR1-3 could inhibit neovascularization and serve as a useful drug candidate in research, diagnostics and therapy of cancer.
Le texte complet de cet article est disponible en PDF.Keywords : VEGFR-2, Periplasmic expression, Antiangiogenic activity
Abbreviations : VEGF, VEGFR2, KDR, E. Coli, SPR, CAM, EC, EGF, FGF, TNF-α, IFN-γ, FBS, BSA, mAB, ELISA, Ka, Kd, KD
Plan
Vol 67 - N° 7
P. 599-606 - septembre 2013 Retour au numéroBienvenue sur EM-consulte, la référence des professionnels de santé.
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