Conover C A
Division of Endocrinology and Metabolism, Mayo Clinic, Rochester, MN, USA.
Prog Growth Factor Res. 1995;6(2-4):301-9. doi: 10.1016/0955-2235(95)00032-1.
Insulin-like growth factor binding protein (IGFBP) proteases-their identification, regulation, and biological significance-are currently an area of ardent investigation. This has developed from the very recent realization that IGFBP availability and bioactivity is determined not only by gene expression, but also by the controlled proteolytic processing of the protein in the pericellular environment. In each case identified so far, the modified IGFBP acts dramatically different from native or recombinant IGFBP in solution. This post-translational modification of IGFBP structure/function could have widespread significance since IGFBPs modulate the diverse growth-promoting activities of the IGFs. In fact, it may be argued that local IGF action is largely controlled by this mechanism. Therefore, knowledge of the form, function, and control of the various IGFBP proteases is likely to have major implications for our understanding of the physiology and pathophysiology of the IGFs.
胰岛素样生长因子结合蛋白（IGFBP）蛋白酶——它们的鉴定、调节及其生物学意义——目前是一个热门的研究领域。这一领域的发展源于最近的认识，即IGFBP的可利用性和生物活性不仅由基因表达决定，还由细胞周围环境中该蛋白的可控蛋白水解加工所决定。在迄今已确定的每种情况下，修饰后的IGFBP在溶液中的行为与天然或重组IGFBP截然不同。IGFBP结构/功能的这种翻译后修饰可能具有广泛的意义，因为IGFBPs调节IGFs的多种促生长活性。事实上，可以说局部IGF作用在很大程度上受该机制控制。因此，了解各种IGFBP蛋白酶的形式、功能和调控，可能对我们理解IGFs的生理学和病理生理学具有重要意义。
