Nelson Bryce P
Gentel Biosciences, Inc., 5500 Nobel Drive, Suite 230, Madison, WI 53711, USA.
Bioanalysis. 2009 Nov;1(8):1431-44. doi: 10.4155/bio.09.119.
Protein glycosylation, the enzymatic linkage of mono- and poly-saccharides to proteins, is a critical determinant of protein function; however, there is a lack of tools for studying the glycosylation of specific proteins in complex samples. A new type of antibody-lectin sandwich assay enables the measurement of the glycosylation of specific proteins that have been captured from complex samples using antibody arrays combined with lectin-based detection probes. Antibody-lectin sandwich arrays have the potential to expand our understanding of the role of glycans and protein glycosylation in disease and to identify and investigate new biomarkers for early detection, disease prognosis and therapeutic response prediction. While antibody-lectin sandwich arrays yield less-detailed structural information regarding protein glycosylation than other available methods, they do provide a simple and reproducible method for investigating changes in protein abundance and glycosylation of multiple proteins and can be easily applied to large or small sample sets. By profiling protein and glycan variations, new disease-associated glycan alterations can be identified and validated for use as biomarkers.
蛋白质糖基化,即单糖和多糖与蛋白质的酶促连接,是蛋白质功能的关键决定因素;然而,在复杂样品中研究特定蛋白质糖基化的工具却很匮乏。一种新型的抗体-凝集素夹心测定法能够测量特定蛋白质的糖基化情况,这些蛋白质是使用抗体阵列结合基于凝集素的检测探针从复杂样品中捕获的。抗体-凝集素夹心阵列有可能扩展我们对聚糖和蛋白质糖基化在疾病中的作用的理解,并识别和研究用于早期检测、疾病预后和治疗反应预测的新生物标志物。虽然与其他现有方法相比,抗体-凝集素夹心阵列提供的关于蛋白质糖基化的结构信息不够详细,但它们确实为研究多种蛋白质的丰度变化和糖基化提供了一种简单且可重复的方法,并且可以轻松应用于大样本集或小样本集。通过分析蛋白质和聚糖的变化,可以识别和验证与新疾病相关的聚糖改变,以用作生物标志物。