Department of Integrative Biology and Pharmacology, University of Texas Health Science Center, Houston, TX 77030, USA.
Anal Biochem. 2010 Jun 15;401(2):288-94. doi: 10.1016/j.ab.2010.03.009. Epub 2010 Mar 12.
Wnts are secreted lipid-modified glycoproteins that carry out various signaling functions during development and in adult tissue. Wnt signaling is mediated by frizzled receptors (Fzds) at the cell surface and can be modulated by the secreted frizzled-related proteins (SFRPs) and other molecular antagonists. Abnormal Wnt signaling has been implicated in several diseases. However, due to the complexity of the Wnt signal and the lack of knowledge pertaining to the binding properties of different Wnt ligands, no therapeutic agents that target this pathway exist. Using a novel enzyme-linked immunosorbent assay (ELISA)-based technique, we were able to determine the first measurements of binding affinity for specific Wnt interactions. This study shows that purified Wnt3a, Wnt7a, and Wnt5a have different binding specificities for Fzds and SFRPs.
Wnts 是分泌的脂质修饰糖蛋白，在发育过程中和成人组织中发挥各种信号功能。Wnt 信号由细胞表面的卷曲受体 (Fzds) 介导，并可被分泌的卷曲相关蛋白 (SFRPs) 和其他分子拮抗剂调节。异常的 Wnt 信号已被牵连到几种疾病中。然而，由于 Wnt 信号的复杂性以及对不同 Wnt 配体结合特性的了解不足，目前还没有针对该途径的治疗药物。使用一种新的基于酶联免疫吸附试验 (ELISA) 的技术，我们能够首次测量特定 Wnt 相互作用的结合亲和力。这项研究表明，纯化的 Wnt3a、Wnt7a 和 Wnt5a 对 Fzds 和 SFRPs 具有不同的结合特异性。
