Pan Sheng, Tamura Yasuko, Chen Ru, May Damon, McIntosh Martin W, Brentnall Teresa A
Department of Medicine, University of Washington, Seattle, WA 98195, USA.
Mol Biosyst. 2012 Nov;8(11):2850-6. doi: 10.1039/c2mb25268f. Epub 2012 Aug 14.
Disease-associated aberrant glycosylation may be protein specific and glycosylation site specific. Quantitative assessment of glycosylation changes at a site-specific molecular level may represent one of the initial steps for systematically revealing the glycosylation abnormalities associated with a disease or biological state. Comparative quantitative profiling of glycoproteome to provide accurate quantification of site-specific glycosylation occupancy has been a challenging task, requiring a concerted approach drawing from a variety of techniques. In this report, we present a quantitative glycoproteomics method that allows global scale identification and comparative quantification of glycosylation site occupancy using mass spectrometry. We further demonstrated this approach by quantitatively characterizing the N-glycoproteome of human pancreas.
疾病相关的异常糖基化可能具有蛋白质特异性和糖基化位点特异性。在位点特异性分子水平上对糖基化变化进行定量评估可能是系统揭示与疾病或生物学状态相关的糖基化异常的初始步骤之一。对糖蛋白质组进行比较定量分析以提供位点特异性糖基化占有率的准确量化一直是一项具有挑战性的任务，需要综合运用多种技术。在本报告中，我们提出了一种定量糖蛋白质组学方法，该方法可利用质谱对糖基化位点占有率进行全局规模的鉴定和比较定量。我们通过对人胰腺的N-糖蛋白质组进行定量表征进一步证明了该方法。
