Hossenlopp P, Seurin D, Segovia-Quinson B, Binoux M
FEBS Lett. 1986 Nov 24;208(2):439-44. doi: 10.1016/0014-5793(86)81065-1.
Human cerebrospinal fluid (CSF) has been found to contain several different molecular forms of IGF-specific binding proteins (BPs). Qualitatively, they are similar to those present in serum, although their relative proportions are very different, as well as to those present in the culture media of brain tissue from which these BPs presumably arise. One particular form of BP is predominant in CSF. It has an Mr of 34,000, as estimated by SDS-polyacrylamide gel electrophoresis followed by transfer onto nitrocellulose, and an isoelectric point around 5.0 based on chromatofocusing. It has a selective affinity for IGF-II (approximately 4 X 10(10) M-1) as shown by competitive binding experiments in which biosynthetic IGF-I was about 40-times less potent than native IGF-II in displacing 125I-labelled IGF-II. These findings are in agreement with the preponderance of IGF-II in nervous tissue and in CSF and suggest that this BP plays an important role in the interaction of IGF-II with its target cells.
已发现人类脑脊液(CSF)中含有几种不同分子形式的胰岛素样生长因子特异性结合蛋白(BP)。从性质上讲,它们与血清中的类似,尽管其相对比例差异很大,并且与这些BP可能产生的脑组织培养基中的类似。一种特定形式的BP在脑脊液中占主导地位。通过SDS-聚丙烯酰胺凝胶电泳,然后转移到硝酸纤维素膜上估计,其分子量为34000,基于色谱聚焦法,其等电点约为5.0。竞争性结合实验表明,它对IGF-II具有选择性亲和力(约4×10¹⁰M⁻¹),在该实验中,生物合成的IGF-I在置换¹²⁵I标记的IGF-II方面的效力比天然IGF-II低约40倍。这些发现与神经组织和脑脊液中IGF-II的优势一致,并表明这种BP在IGF-II与其靶细胞的相互作用中起重要作用。