کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2524231 | 1119550 | 2013 | 8 صفحه PDF | دانلود رایگان |
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 × 105 M−1 S−1, the dissociation rate Kd was 6.09 × 10−3 S−1, the dissociation constant KD was 5.74 × 10−8 M. 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.
Journal: Biomedicine & Pharmacotherapy - Volume 67, Issue 7, September 2013, Pages 599–606