Zheng J, Ito Y, Imanishi Y
Division of Material Chemistry, Faculty of Engineering, Kyoto University, Japan.
J Biomater Sci Polym Ed. 1995;7(6):515-22. doi: 10.1163/156856295x00571.
The tetrapeptide, Arg-Gly-Asp-Ser (RGDS), which corresponds to a core sequence of cell adhesion proteins, was coimmobilized with insulin on to surface-hydrolyzed poly(methyl methacrylate) film. Adhesion of STO mouse fibroblast cells was enhanced by the immobilization of RGDS, but not of insulin. On the other hand, growth of the cells was accelerated by the insulin immobilization, but not by the RGDS immobilization. Coimmobilization of insulin and RGDS did not affect cell adhesion but accelerated cell growth remarkably. This acceleration effect is considered to be attributable to a prolonged interaction of immobilized insulin and insulin receptor by adhesion enhancement, and to a postulated interaction between activated insulin receptor and integrin.
四肽精氨酸-甘氨酸-天冬氨酸-丝氨酸(Arg-Gly-Asp-Ser,RGDS),它对应于细胞黏附蛋白的核心序列,与胰岛素共同固定在表面水解的聚甲基丙烯酸甲酯薄膜上。固定化的RGDS可增强STO小鼠成纤维细胞的黏附,但胰岛素则无此作用。另一方面,固定化胰岛素可促进细胞生长,而固定化RGDS则无此作用。胰岛素和RGDS的共同固定化不影响细胞黏附,但显著加速了细胞生长。这种加速作用被认为归因于固定化胰岛素与胰岛素受体通过增强黏附作用而延长的相互作用,以及活化的胰岛素受体与整合素之间的假定相互作用。