Parkar A A, Day A J
Department of Biochemistry, University of Oxford, UK.
FEBS Lett. 1997 Jun 30;410(2-3):413-7. doi: 10.1016/s0014-5793(97)00621-2.
Link modules are hyaluronan-binding domains that are involved in the formation and stability of extracellular matrix and cell migration. We have examined the glycosaminoglycan specificity of the Link module from the arthritis-associated protein, human TSG-6, by microtitre plate-based assays employing biotinylated-hyaluronan or mono-biotinylated Link module. This domain was found to interact specifically with chondroitin-4-sulphate (C4S), with similar affinity to hyaluronan, but not with chondroitin-6-sulphate or heparin. Competition experiments indicate that C4S and hyaluronan have overlapping binding surfaces on the TSG-6 Link module. Disease-associated changes in C4S expression may influence the localisation and biological role of TSG-6.
连接模块是与细胞外基质的形成和稳定性以及细胞迁移有关的透明质酸结合结构域。我们通过使用生物素化透明质酸或单生物素化连接模块的基于微量滴定板的分析方法，研究了来自与关节炎相关的蛋白质——人TSG-6的连接模块的糖胺聚糖特异性。发现该结构域与硫酸软骨素-4（C4S）特异性相互作用，其亲和力与透明质酸相似，但不与硫酸软骨素-6或肝素相互作用。竞争实验表明，C4S和透明质酸在TSG-6连接模块上具有重叠的结合表面。C4S表达的疾病相关变化可能会影响TSG-6的定位和生物学作用。
