Sugrue S P
J Biol Chem. 1987 Mar 5;262(7):3338-43.
In the present paper, we report the isolation and characterization of embryonic corneal membrane glycoproteins that demonstrate specific affinity for collagen. Two collagen binding proteins have been isolated: a novel 70-kDa protein and a 47-kDa protein which is apparently similar to that reported by Kurkinen et al. (Kurkinen, M., Taylor, A., Garrels, J. I., and Hogan, B. (1984) J. Biol. Chem. 259, 5915-5922). Both proteins label metabolically with [35S]methionine and [3H] glucosamine. 125I iodination of cell surface proteins revealed that the two collagen binding proteins are expressed on the epithelial cell surface. The 70-kDa protein appears to be an integral membrane protein, whereas the 47-kDa protein can be removed from membranes by alkali treatment. The isolated proteins exhibit binding to native type IV collagen as well as heat-denatured type I collagen. It seems likely that we have isolated, at least in part, the cell surface receptor or receptor complex that binds collagen to the basal surface of epithelia.
在本论文中，我们报告了对胚胎角膜膜糖蛋白的分离与特性分析，这些糖蛋白对胶原蛋白表现出特异性亲和力。已分离出两种胶原蛋白结合蛋白：一种新的70 kDa蛋白和一种47 kDa蛋白，后者显然与Kurkinen等人（Kurkinen, M., Taylor, A., Garrels, J. I., and Hogan, B. (1984) J. Biol. Chem. 259, 5915 - 5922）报道的蛋白相似。这两种蛋白都能用[35S]甲硫氨酸和[3H]葡糖胺进行代谢标记。对细胞表面蛋白进行125I碘化显示，这两种胶原蛋白结合蛋白在上皮细胞表面表达。70 kDa蛋白似乎是一种整合膜蛋白，而47 kDa蛋白可通过碱处理从膜上除去。分离出的蛋白表现出与天然IV型胶原蛋白以及热变性I型胶原蛋白的结合。我们似乎至少部分分离出了将胶原蛋白结合到上皮基底表面的细胞表面受体或受体复合物。
