Abstract
Glycosylation is estimated to be found in over 50% of human proteins. Aberrant protein glycosylation and alteration of glycans are closely related to many diseases. More than half of the cancer biomarkers are glycosylated-proteins, and specific glycoforms of glycosylated-proteins may serve as biomarkers for either the early detection of disease or the evaluation of therapeutic efficacy for treatment of diseases. Glycoproteomics, therefore, becomes an emerging field that can make unique contributions to the discovery of biomarkers of cancers. The recent advances in mass spectrometry (MS)-based glycoproteomics, which can analyze thousands of glycosylated-proteins in a single experiment, have shown great promise for this purpose. Herein, we described the MS-based strategies that are available for glycoproteomics, and discussed the sensitivity and high throughput in both qualitative and quantitative manners. The discovery of glycosylated-proteins as biomarkers in some representative diseases by employing glycoproteomics was also summarized.
Highlights
Proteomics, aiming at the large-scale protein analysis in biological samples, is useful for monitoring proteins that are involved in physiological changes in cells or organisms [1]
Proteins perform a vast array of biological functions in living organisms, posttranslational modifications (PTMs) that are introduced after translation further extended the range of functions of the protein [3]
We have summarized the current existing mass spectrometry (MS)-based technologies that are utilized for characterization and quantification of N-glycosylated-proteins, and the understanding of glycosylated-proteins as biomarkers of some representative diseases
Summary
Proteomics, aiming at the large-scale protein analysis in biological samples, is useful for monitoring proteins that are involved in physiological changes in cells or organisms [1]. The iTRAQ approach revealed 80/437 deglycosylated-peptides with altered abundance, while dimethyl labeling confirmed 46 of these and revealed an additional 62 significant changes In their strategy, they employed a series of different enrichment methods including hydrazide capture, titanium dioxide and HILIC with multiple proteases to increase glycoproteome coverage [45]. By employing the TOSIL approach, it yielded a good linearity for the quantitative response of the N-glycosylated site occupancy, which was within a 10-fold dynamic range with a correlation coefficient r2 > 0.99 This strategy was successfully applied to the analysis of serum glycoproteome between ovarian cancer patients and healthy controls, and results showed that changes in N-glycosylation occupancy at specific sites did not always have the same trends as those of protein expression levels [68]. These above findings clearly suggest that glycosylated-protein modifications may be a useful means to identify novel markers for detection of cancer and monitoring of cancer progression
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
