Protein glycosylation governs key physiological and pathological processes in human cells. Aberrant glycosylation is thus closely associated with disease progression. Mass spectrometry (MS)-based glycoproteomics has emerged as an indispensable tool for investigating glycosylation changes in biological samples with high sensitivity. Following rapid improvements in methodologies for reliable intact glycopeptide identification, site-specific quantification of glycopeptide macro- and micro-heterogeneity at the proteome scale has become an urgent need for exploring glycosylation regulations. Here, we summarize recent advances in N- and O-linked glycoproteomic quantification strategies and discuss their limitations. We further describe a strategy to propagate MS data for multilayered glycopeptide quantification, enabling a more comprehensive examination of global and site-specific glycosylation changes. Altogether, we show how quantitative glycoproteomics methods explore glycosylation regulation in human diseases and promote the discovery of biomarkers and therapeutic targets.
【저자키워드】 mass spectrometry, quantification, glycoproteomics, stable-isotope labeling, label free, 【초록키워드】 Biomarker, glycosylation, improvement, Disease progression, sensitivity, proteome, methodology, Quantitative, therapeutic targets, physiological, changes, Regulation, human disease, human cells, limitations, changes in, promote, biological sample, 【제목키워드】 Strategy, macro,