A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors
A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors
复制标题
DOI：
10.1073/pnas.94.7.2859
复制
发表时间：
1997-04-01
影响因子：
11.1
通讯作者：
Nathans, J
中科院分区：
文献类型：
--
作者：
Rattner, A;Hsieh, JC;Nathans, J
本文描述了一个新的哺乳动物基因家族的鉴定，其编码的分泌蛋白含有与在跨膜受体的卷曲家族中发现的富含半胱氨酸的配体结合结构域的同源性。分泌的卷曲相关蛋白（sFRPs）的大小约为30 kDa，并且每个含有推定的信号序列、卷曲样富含半胱氨酸的结构域和保守的亲水性羧基末端结构域，sFRP不是已知卷曲基因的差异剪接的产物，在转染的人胚肾细胞中产生的sFRP-2和sFRP-3的糖基磷脂酰肌醇锚定衍生物赋予果蝇无翼蛋白的细胞表面结合。这些观察结果表明，sFRP可能在体内起调节Wnt信号传导的作用，或者作为尚未鉴定的受体的新型配体。
This paper describes the identification of a new family of mammalian genes that encode secreted proteins containing homology to the cysteine-rich ligand-binding domain found in the frizzled family of transmembrane receptors, The secreted frizzled-related proteins (sFRPs) are approximately 30 kDa in size, and each contains a putative signal sequence, a frizzled-like cysteine-rich domain, and a conserved hydrophilic carboxy-terminal domain, The sFRPs are not the products of differential splicing of the known frizzled genes, Glycosylphosphatidylinositol-anchored derivatives of sFRP-2 and sFRP-3 produced in transfected human embryonic kidney cells confer cell-surface binding by the Drosophila Wingless protein, These observations suggest that sFRPs may function in vivo to modulate Wnt signaling, or, alternatively, as novel ligands for as yet unidentified receptors.