Arthur Connie M, Rodrigues Lílian Cataldi, Baruffi Marcelo Dias, Sullivan Harold C, Heimburg-Molinaro Jamie, Smith Dave F, Cummings Richard D, Stowell Sean R
The Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA, USA.
Methods Mol Biol. 2015;1207:115-31. doi: 10.1007/978-1-4939-1396-1_8.
Glycan binding proteins (GBPs) possess the unique ability to regulate a wide variety of biological processes through interactions with highly modifiable cell surface glycans. While many studies demonstrate the impact of glycan modification on GBP recognition and activity, the relative contribution of subtle changes in glycan structure on GBP binding can be difficult to define. To overcome limitations in the analysis of GBP-glycan interactions, recent studies utilized glycan microarray platforms containing hundreds of structurally defined glycans. These studies not only provided important information regarding GBP-glycan interactions, but have also resulted in significant insight into the binding specificity and biological activity of the galectin family. We will describe the methods used when employing glycan microarray platforms to examine galectin-glycan binding specificity and function.
聚糖结合蛋白（GBP）具有通过与高度可修饰的细胞表面聚糖相互作用来调节多种生物过程的独特能力。虽然许多研究证明了聚糖修饰对GBP识别和活性的影响，但聚糖结构细微变化对GBP结合的相对贡献可能难以确定。为了克服GBP-聚糖相互作用分析中的局限性，最近的研究利用了包含数百种结构明确的聚糖的聚糖微阵列平台。这些研究不仅提供了有关GBP-聚糖相互作用的重要信息，还对半乳糖凝集素家族的结合特异性和生物活性有了重要的了解。我们将描述使用聚糖微阵列平台检测半乳糖凝集素-聚糖结合特异性和功能时所采用的方法。
