Müller W E, Müller I, Zahn R K, Kurelec B
J Cell Sci. 1976 Jul;21(2):227-41. doi: 10.1242/jcs.21.2.227.
An aggregation receptor from the siliceous sponge Geodia cydonium has been isolated and purified in an almost pure form. It sediments at about 2-6s, has a buoyant density of 1-51 g/ml in CsCl and elutes from Sephadex G-50 at a Ve/V0 value of 1-311. Chemical analysis revealed that the receptor consists of 81% neutral carbohydrate and 7-5% protein. The activity of the receptor is rapidly destroyed by Na-periodate. The receptor is released from the cell surface after removal of Ca2+ from the medium or after incubation of the cells with trypsin. The depleted cells can be charged again with isolated receptor molecules. The binding of the receptor molecules on the cell surface is prevented in the presence of trypsin. For optimal binding, physiological salt concentrations with respect to NaCl (540 mM NaCl) and Ca2+ ions are necessary. The receptor whose isolation is described in this report, is involved in secondary aggregation processes, which are initiated by a soluble aggregation factor. The primary aggregation of the cells is not influenced by the receptor. Time-course studies with receptor-depleted cells revealed that new aggregation receptor molecules are formed during the aggregation process. By competition experiments it could be shown that high concentrations of soluble aggregation receptor molecules inhibit secondary aggregation. The soluble receptor molecules can complete with surface-bound receptor molecules only if these are not linked with the aggregation factor.
一种来自硅质海绵地穴海绵(Geodia cydonium)的聚集受体已被分离并纯化至几乎纯的形式。它在约2 - 6s沉降,在CsCl中的浮力密度为1.51 g/ml,从Sephadex G - 50以Ve/V0值1.311洗脱。化学分析表明该受体由81%的中性碳水化合物和7.5%的蛋白质组成。该受体的活性会被高碘酸钠迅速破坏。从培养基中去除Ca2+后或细胞与胰蛋白酶孵育后,受体会从细胞表面释放。耗尽受体的细胞可以再次用分离的受体分子进行补充。在胰蛋白酶存在的情况下,受体分子在细胞表面的结合受到抑制。为实现最佳结合,需要生理盐浓度的NaCl(540 mM NaCl)和Ca2+离子。本报告中描述其分离过程的这种受体参与由可溶性聚集因子引发的二级聚集过程。细胞的一级聚集不受该受体影响。对耗尽受体的细胞进行的时间进程研究表明,在聚集过程中会形成新的聚集受体分子。通过竞争实验可以表明,高浓度的可溶性聚集受体分子会抑制二级聚集。只有当表面结合的受体分子未与聚集因子相连时,可溶性受体分子才能与它们竞争。