Department of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY 12180, USA.
Biochimie. 2012 Jan;94(1):242-9. doi: 10.1016/j.biochi.2011.10.015. Epub 2011 Nov 6.
Glycosaminoglycans (GAGs) interact with a number of cytokines and growth factors thereby playing an essential role in the regulation of many physiological processes. These interactions are important for both normal signal transduction and the regulation of the tissue distribution of cytokines/growth factors. In the present study, we employed surface plasmon resonance (SPR) spectroscopy to dissect the binding interactions between GAGs and murine and human forms of interleukin-7 (IL-7). SPR results revealed that heparin binds with higher affinity to human IL-7 than murine IL-7 through a different kinetic mechanism. The optimal oligosaccharide length of heparin for the interactions to human and murine IL-7 involves a sequence larger than a tetrasaccharide. These results further demonstrate that while IL-7 is principally a heparin/heparan sulfate binding protein, it also interacts with dermatan sulfate, chondroitin sulfates C, D, and E, indicating that this cytokine preferentially interacts with GAGs having a higher degree of sulfation.
糖胺聚糖 (GAGs) 与许多细胞因子和生长因子相互作用，从而在许多生理过程的调节中发挥重要作用。这些相互作用对于正常的信号转导和细胞因子/生长因子的组织分布调节都很重要。在本研究中，我们采用表面等离子体共振 (SPR) 光谱技术来剖析 GAGs 与鼠类和人类白细胞介素-7（IL-7）之间的结合相互作用。SPR 结果表明，肝素通过不同的动力学机制与人 IL-7 的结合亲和力高于鼠类 IL-7。肝素与人和鼠类 IL-7 相互作用的最佳寡糖长度涉及一个大于四糖的序列。这些结果进一步表明，虽然 IL-7 主要是一种肝素/硫酸乙酰肝素结合蛋白，但它也与硫酸皮肤素、软骨素 C、D 和 E 相互作用，表明这种细胞因子优先与具有更高硫酸化程度的 GAGs 相互作用。
