Tesch G H, Cornell H J, Herington A C, Oakes S
Department of Applied Chemistry, Royal Melbourne Institute of Technology, Victoria, Australia.
Growth Regul. 1993 Jun;3(2):151-9.
Insulin-like growth factor binding protein (IGF-BP) complexes containing either IGF-I or IGF-II were purified from human plasma and coincubated with human foreskin fibroblasts. Incorporation of [3H]thymidine into fibroblasts was measured to determine the mitogenic effects of the IGF-BP complexes in comparison with purified recombinant IGF-I or IGF-II. The IGF-I-BP complex was shown to have no stimulatory activity when added to cultures at a comparable Non Suppressible Insulin-Like Activity (NSILA) dose level to that of purified recombinant IGF-I which produced maximal stimulation. In contrast, the IGF-II-BP complex produced a similar stimulatory activity to that of purified recombinant IGF-II when added at comparable NSILA doses. NSILA-p, a contaminating factor in the purified preparations of IGF-BP complexes, was shown to have no effect on fibroblast growth. This study suggests that plasma IGF binding proteins may have a differential effect on the stimulatory activities of IGFs I and II on human fibroblasts.
从人血浆中纯化出含有胰岛素样生长因子-I（IGF-I）或胰岛素样生长因子-II（IGF-II）的胰岛素样生长因子结合蛋白（IGF-BP）复合物，并与人包皮成纤维细胞共同孵育。通过测量[3H]胸腺嘧啶核苷掺入成纤维细胞的情况，来确定IGF-BP复合物与纯化的重组IGF-I或IGF-II相比的促有丝分裂作用。结果显示，当以与产生最大刺激作用的纯化重组IGF-I相当的不可抑制胰岛素样活性（NSILA）剂量水平添加到培养物中时，IGF-I-BP复合物没有刺激活性。相反，当以相当的NSILA剂量添加时，IGF-II-BP复合物产生的刺激活性与纯化的重组IGF-II相似。NSILA-p是IGF-BP复合物纯化制剂中的一种污染因子，对成纤维细胞生长没有影响。这项研究表明，血浆IGF结合蛋白可能对IGF-I和IGF-II对人成纤维细胞的刺激活性有不同的影响。
