胰岛素样生长因子(insulin-like growth factor,IGF)结合蛋白(IGF-binding proteins,IGFBPs)家族包含6个与IGF有高亲和力的蛋白。该蛋白家族能够调节IGF的生物利用度,且具有调控细胞增殖分化的作用。IGFBPs蛋白分子中N端保守区的几个疏水氨基酸位点是该蛋白与IGF具有高亲和力的关键位点。近年来的研究发现,N端结构域的起始与末尾的几个保守的氨基酸位点也与结合有关。而C端不仅含有结合IGF的关键位点,而且还是IGFBPs独立于IGF分子网络作用的主要负责区域。IGFBPs除了在体内调节IGF的生物利用度之外,还具有其独立的作用,诸如细胞凋亡和细胞周期的调控。IGFBPs的细胞表面受体及信号通路等研究已经取得一定成果,但每个成员的具体作用机制还不够精确,因此该蛋白家族更多的作用还有待于进一步的探讨。
The insulin-like growth factor(IGF)-binding proteins(IGFBPs) are a family of six homologous proteins with high binding affinity for IGF-I and IGF-II.Information from nuclear magnetic resonance(NMR) and mutagenesis studies indicated that several amino acids in the N-domain of the protein molecule whose flank form hydrophobic pocket are key residues for their high affinity.However,the C-domain contains not only IGF binding sites but also regions which play role in the molecular independent function.Besides modulation of IGF bioavailability,IGFBPs have functions independent of IGF such as regulation of cell apoptosis and cell cycle.Putative receptors and molecular pathways have been detected in the last 5 years,but the precise mechanism is still obscure and so should be studied deeply.