Hadjiargyrou M, Kaprielian Z, Kato N, Patterson P H
Division of Biology, California Institute of Technology, Pasadena 91125, USA.
J Neurochem. 1996 Dec;67(6):2505-13. doi: 10.1046/j.1471-4159.1996.67062505.x.
The cell surface glycoprotein CD9 is a member of a group of proteins known as the "tetraspan" or "transmembrane 4 superfamily." Previous work with non-neural cells has shown that CD9 associates in cis with integrins and small GTP-binding proteins on the cell surface. To extend our recent findings showing that perturbation of CD9 alters Schwann cell adhesion, proliferation, and migration, as well as neurite outgrowth in sympathetic neurons, we have searched for CD9-associated proteins in S-16 Schwann cells. We demonstrate here that CD9 is specifically coprecipitated from S-16 cell extracts by antibodies against integrins alpha 3, alpha 6, and beta 1. In addition, double immunofluorescence labeling and co-capping experiments indicate that CD9 is specifically co-localized with these integrins on the cell membrane of S-16 Schwann cells.
细胞表面糖蛋白CD9是被称为“四跨膜蛋白”或“跨膜4超家族”的一组蛋白质的成员。先前对非神经细胞的研究表明，CD9在细胞表面与整合素和小GTP结合蛋白顺式结合。为了扩展我们最近的研究结果，即CD9的扰动会改变雪旺细胞的粘附、增殖和迁移，以及交感神经元的神经突生长，我们在S-16雪旺细胞中寻找与CD9相关的蛋白质。我们在此证明，抗整合素α3、α6和β1的抗体可从S-16细胞提取物中特异性共沉淀CD9。此外，双重免疫荧光标记和共帽实验表明，CD9与这些整合素在S-16雪旺细胞的细胞膜上特异性共定位。
