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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Biochemicai characterization of Wnt-Frizzled interactions using , soluble, biologicaily active vertebrate Wnt protein
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Biochemicai characterization of Wnt-Frizzled interactions using , soluble, biologicaily active vertebrate Wnt protein

机译：使用可溶的，具有生物学活性的脊椎动物Wnt蛋白对Wnt-毛躁相互作用进行生化表征

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摘要

Biochemical studies of Wnt signaling have been hampered by difficulties in obtaining large quantities of soluble, biologically active Wnt proteins. In this paper, we report the production in Drosophifo S2 cells of biologically active Xenopus Wnt8 (XWnt8) . Epitope- or alkaline phosphatase- tagged Wnth proteins are secreted by concentrated S2 cells in a form that is suitable for quantitative biochemical experiments with yields of 5 and 0.5 mg per liter, respectively. Conditions also are described for the production in 293 cells of an IgG fusion of the cysteine-rich domain (CRD) of mouse Frizzled & with a yield of 20 mg/lite. We demonstrate the use of these proteins for studying the interactions between soluble Wnth and various Frizzled proteins, membrane anchored or secreted CRDs, and a set of insertion mutants in the CRD of Drosophila Frizzled 2. In a solid phase binding assay, the affinity of the XWnt8-alkaline phosphatase fusion for the purified mouse Frizzled 8-CRD-IgG fusion is approximately equals 9 nM.
机译：Wnt信号转导的生化研究由于难以获得大量可溶的，具有生物活性的Wnt蛋白而受到阻碍。在本文中，我们报告了在具有生物活性的非洲爪蟾Wnt8（XWnt8）的Drosophifo S2细胞中的生产。抗原决定簇或碱性磷酸酶标记的Wnth蛋白由浓缩的S2细胞分泌，其形式适于定量生化实验，每升的产量分别为5和0.5 mg。还描述了在293细胞中产生Friszzled小鼠的富含半胱氨酸结构域（CRD）的IgG融合体的条件，产量为20mg / lite。我们证明了使用这些蛋白质来研究可溶性Wnth和各种卷曲蛋白，膜锚定或分泌的CRD和果蝇卷曲蛋白2的CRD中的一组插入突变体之间的相互作用。在固相结合测定中，纯化的小鼠卷曲的8-CRD-IgG融合物的XWnt8-碱性磷酸酶融合大约等于9 nM。

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