Bach Leon A, Headey Stephen J, Norton Raymond S
University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg 3084, Australia.
Trends Endocrinol Metab. 2005 Jul;16(5):228-34. doi: 10.1016/j.tem.2005.05.005.
The six insulin-like growth factor (IGF)-binding proteins (IGFBPs) are important regulators of IGF actions. IGF-independent actions of several IGFBPs have also been described. IGFBPs contain highly conserved N- and C-terminal domains, both of which are important for high-affinity IGF binding. The C-domain also binds a large number of other biomolecules, thereby modulating IGF binding and mediating IGF-independent effects. The 3D structures of the IGF-binding region of the N-domain of IGFBP-5 and the entire C-domain of IGFBP-6 have been solved recently, providing new insights into IGFBP modulation of IGF actions, and structural studies might be expected to do the same for IGF-independent actions. IGFBP-based therapies for diseases such as cancer are promising, and this recent progress will enhance their development.
六种胰岛素样生长因子（IGF）结合蛋白（IGFBP）是IGF作用的重要调节因子。几种IGFBP的非IGF依赖性作用也已被描述。IGFBP包含高度保守的N端和C端结构域，这两个结构域对于高亲和力IGF结合都很重要。C结构域还结合大量其他生物分子，从而调节IGF结合并介导非IGF依赖性效应。最近已解析出IGFBP-5的N结构域的IGF结合区域和IGFBP-6的整个C结构域的三维结构，为IGFBP对IGF作用的调节提供了新见解，并且结构研究有望对非IGF依赖性作用也有同样的发现。基于IGFBP的癌症等疾病治疗方法很有前景，而这一最新进展将加速其发展。
