Glycosylation is one of the most common and important
protein modifications,
and it regulates the properties and functions of a wide range of proteins.
Aberrant glycosylation is directly related to human diseases. Recently,
with the advancement of mass spectrometry (MS) instrumentation and
MS-based glycoproteomic methods, global characterization of glycoproteins
in complex biological samples has become possible. Using quantitative
proteomics, the abundance of glycoproteins in different samples can
be quantified, which provides a wealth of information to further our
understanding of protein functions, cellular activities, and the molecular
mechanisms of diseases. In this review, we discuss quantitative proteomic
methods used for comprehensive analysis of protein glycosylation,
and cover the applications of quantitative glycoproteomics to unveil
the properties and functions of glycoproteins and their association
with various diseases. It is expected that quantitative proteomic
methods will be extensively applied to explore the role of protein
glycosylation in complex biological systems, and to identify glycoproteins
as biomarkers for disease detection and as therapeutic targets for
disease treatment.