Glycosaminoglycans play an important role in tissue organisation through interactions with a diverse range of proteins, growth factors and other chemokines. In this report, we demonstrate the GAG-binding 'fingerprint' of two important GAG-binding proteins - osteoprotogerin and TIMP-3. The technique uses a straightforward method for attaching GAGs to assay surfaces in a non-covalent manner using plasma polymerization that leaves the adsorbed GAG able to participate in subsequent ligand binding. We show that OPG and TIMP-3 bind preferentially to different GAGs in a simple ELISA and that this binding does not correlate directly with simple GAG properties such as degree of sulfation. The methods outlined in this report can be easily applied to tissue engineering scaffolds in order to exploit the potential of surface-bound GAGs in influencing the structure of engineered tissues.

译文

糖胺聚糖通过与多种蛋白质,生长因子和其他趋化因子的相互作用在组织中发挥重要作用。在本报告中,我们证明了两种重要的GAG结合蛋白-骨原蛋白和TIMP-3的GAG结合 “指纹”。该技术使用一种简单的方法,使用等离子体聚合以非共价方式将GAG附着到测定表面,使吸附的GAG能够参与随后的配体结合。我们表明,OPG和TIMP-3在简单的ELISA中优先结合不同的GAG,并且这种结合与简单的GAG特性 (例如硫酸化程度) 不直接相关。本报告中概述的方法可以轻松地应用于组织工程支架,以便利用表面结合的GAGs在影响工程组织结构方面的潜力。

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