Yayon A, Klagsbrun M, Esko J D, Leder P, Ornitz D M
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
Cell. 1991 Feb 22;64(4):841-8. doi: 10.1016/0092-8674(91)90512-w.
The role of low affinity, heparin-like binding sites for basic fibroblast growth factor (bFGF) was investigated in CHO cells mutant in their metabolism of glycosaminoglycans. Heparan sulfate-deficient mutants transfected to express a cloned mouse FGF receptor cDNA are not able to bind bFGF. It is demonstrated that free heparin and heparan sulfate can reconstitute a low affinity receptor that is, in turn, required for the high affinity binding of bFGF. These studies suggest that the low affinity receptor is an accessory molecule required for binding of bFGF to the high affinity site. Such an obligatory interaction of low and high affinity FGF receptors suggests a physiological role for heparin-like, low affinity receptors and constitutes a novel mechanism for the regulation of growth factor-receptor interactions.
在糖胺聚糖代谢发生突变的中国仓鼠卵巢（CHO）细胞中，研究了低亲和力、类肝素结合位点对碱性成纤维细胞生长因子（bFGF）的作用。转染以表达克隆的小鼠FGF受体cDNA的硫酸乙酰肝素缺陷型突变体无法结合bFGF。结果表明，游离肝素和硫酸乙酰肝素可以重构一种低亲和力受体，而这种受体反过来又是bFGF高亲和力结合所必需的。这些研究表明，低亲和力受体是bFGF与高亲和力位点结合所需的辅助分子。低亲和力和高亲和力FGF受体之间的这种必然相互作用提示了类肝素低亲和力受体的生理作用，并构成了一种调节生长因子-受体相互作用的新机制。
