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Studies on Prokaryotic Expression of Wild-type and Mutant Soluble Ectodomains of Human Fibroblast Growth Factor Receptor 2IIIc and Their Inhibitory Effects on Tumor

Author: LiuXueZuo
Tutor: HongAn
School: Jinan University
Course: Genetics
Keywords: S252W mutation FGFR2 ectodomain Tumor suppressor Angiogenesis Inclusion Refolding Affinity FGF-2
CLC: Q78
Type: Master's thesis
Year: 2008
Downloads: 88
Quote: 0
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Abstract


The wild-type and mutant FGFR2 Ⅲ c S252W extracellular fragment cloned into pET3c carrier, through the engineered strain of E. coli recombinant proteins expressed as inclusion bodies . Refolding gel chromatography , heparin affinity chromatography , the purity greater than 95% of the target protein . By surface plasmon resonance , the molecular determination refolded FGFR2 Ⅲ c extracellular domain of the FGF-2 affinity , results show that the refolded and purified wild-type and S252W mutant FGFR2 Ⅲ c extracellular domain of the FGF-2 between the specific combined . S252W mutant receptor extracellular domain and the binding of FGF-2 than the wild -type receptor extracellular domain with FGF-2 binding stronger. By Western blotting detection membrane FGFRs phosphorylation level changes ; MTT assay, flow cytometry , cells from wild-type and the level of proven S252W mutant FGFR2 Ⅲ c ectodomain of prostate cancer DU145 cell proliferation was inhibited , S252W mutant soluble FGFR2 Ⅲ c extracellular more significant inhibition . Through breast cancer MCF-7 cells in nude mice xenograft model , BALB / C 4T1 mouse breast cancer cells in the lung metastasis model , chorioallantoic membrane model in vivo levels of proof from the wild-type and mutant FGFR2 Ⅲ c S252W extracellular segment of breast cancer growth , metastasis and angiogenesis inhibition , S252W mutant FGFR2 Ⅲ C soluble extracellular fragment inhibited more pronounced. These results suggest that , FGFR2 Ⅲ c ectodomain significantly inhibited tumor can be used as a wide range of anticancer drugs development .

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