Mass spectrometry for protein sialoglycosylation

Zhang, Qiwei; Li, Zack; Wang, Yawei; Zheng, Qi; Li, Jianjun

doi:10.1002/mas.21555

Cited by 37 publications

(26 citation statements)

References 345 publications

(863 reference statements)

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“…For example, sialic acid, quantified with fluorescence detection-HPLC in the IgM-enriched fraction, was significantly higher in cancer patients [112]. The sialylated proteins, as potentially cancer-associated proteins in serum, were quantified in prostate cancer using LC-MS/MS [113,114].…”

Section: Sialic Acid Analysis Technologymentioning

confidence: 99%

Biological Functions and Analytical Strategies of Sialic Acids in Tumor

Zhou

Yang

Guan

2020

Cells

120

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Sialic acids, a subset of nine carbon acidic sugars, often exist as the terminal sugars of glycans on either glycoproteins or glycolipids on the cell surface. Sialic acids play important roles in many physiological and pathological processes via carbohydrate-protein interactions, including cell–cell communication, bacterial and viral infections. In particular, hypersialylation in tumors, as well as their roles in tumor growth and metastasis, have been widely described. Recent studies have indicated that the aberrant sialylation is a vital way for tumor cells to escape immune surveillance and keep malignance. In this article, we outline the present state of knowledge on the metabolic pathway of human sialic acids, the function of hypersialylation in tumors, as well as the recent labeling and analytical techniques for sialic acids. It is expected to offer a brief introduction of sialic acid metabolism and provide advanced analytical strategies in sialic acid studies.

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Section: Sialic Acid Analysis Technologymentioning

confidence: 99%

Biological Functions and Analytical Strategies of Sialic Acids in Tumor

Zhou

Yang

Guan

2020

Cells

120

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“…Only the levels of sialylation seem slightly higher for CE-MS and HILIC-MS results as compared to RPLC-MS (∼2 and 4% lower). Presence of sialic acids may result in relatively lower ionization of glycopeptides (47), whereas this effect may be less pronounced for the ionization of the much larger Fc/2 subunits. The characterization of IgG-Fc sialylation is important because of its anti-inflammatory effects (48).…”

Section: Development Of a Middle-up Ms-based Strategy For The Analysimentioning

confidence: 99%

MS-Based Allotype-Specific Analysis of Polyclonal IgG-Fc N-Glycosylation

et al. 2020

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Current approaches to study glycosylation of polyclonal human immunoglobulins G (IgG) usually imply protein digestion or glycan release. While these approaches allow in-depth characterization, they also result in a loss of valuable information regarding certain subclasses, allotypes and co-occuring post-translational modifications (PTMs). Unfortunately, the high variability of polyclonal IgGs makes their intact mass spectrometry (MS) analysis extremely challenging. We propose here a middle-up strategy for the analysis of the intact fragment crystallizable (Fc) region of human plasma IgGs, with the aim of acquiring integrated information of the N-glycosylation and other PTMs of subclasses and allotypes. Human plasma IgG was isolated using Fcspecific beads followed by an on-bead C H 2 domain digestion with the enzyme IdeS. The obtained mixture of Fc subunits was analyzed by capillary electrophoresis (CE) and hydrophilic interaction liquid chromatography (HILIC) hyphenated with MS. CE-MS provided separation of different IgG-subclasses and allotypes, while HILIC-MS allowed resolution of the different glycoforms and their oxidized variants. The orthogonality of these techniques was key to reliably assign Fc allotypes. Five individual donors were analyzed using this approach. Heterozygosis was observed in all the analyzed donors resulting in a total of 12 allotypes identified. The assignments were further confirmed using recombinant monoclonal IgG allotypes as standards. While the glycosylation patterns were similar within allotypes of the same subclass, clear differences were observed between IgG subclasses and donors, highlighting the relevance of the proposed approach. In a single analysis, glycosylation levels specific for each allotype, relative abundances of subclasses and information on co-occurring modifications are obtained. This middle-up method represents an important step toward a comprehensive analysis of immunoglobulin G-Fc variants.

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“…The applications of glycoproteomics in clinical samples are far more than what we described in this section, there are many comprehensive reviews covering the importance of glycoproteomic technologies in biomedical research (Kim and Varki, ; Tian and Zhang, ; Plomp et al, ; Ruhaak et al, ; Zhang et al, ). Due to the irreplaceable roles of glycoproteins playing in various diseases, high‐throughput glycoproteomic technologies will continue to be developed to enable large‐scale profiling of glycopeptides and glycan structures.…”

Section: Applications Of Ms‐based Glycoproteomicsmentioning

confidence: 99%

Global and site‐specific analysis of protein glycosylation in complex biological systems with Mass Spectrometry

Xiao

Sun

Suttapitugsakul

et al. 2019

Mass Spectrometry Reviews

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Protein glycosylation is ubiquitous in biological systems and plays essential roles in many cellular events. Global and site‐specific analysis of glycoproteins in complex biological samples can advance our understanding of glycoprotein functions and cellular activities. However, it is extraordinarily challenging because of the low abundance of many glycoproteins and the heterogeneity of glycan structures. The emergence of mass spectrometry (MS)‐based proteomics has provided us an excellent opportunity to comprehensively study proteins and their modifications, including glycosylation. In this review, we first summarize major methods for glycopeptide/glycoprotein enrichment, followed by the chemical and enzymatic methods to generate a mass tag for glycosylation site identification. We next discuss the systematic and quantitative analysis of glycoprotein dynamics. Reversible protein glycosylation is dynamic, and systematic study of glycoprotein dynamics helps us gain insight into glycoprotein functions. The last part of this review focuses on the applications of MS‐based proteomics to study glycoproteins in different biological systems, including yeasts, plants, mice, human cells, and clinical samples. Intact glycopeptide analysis is also included in this section. Because of the importance of glycoproteins in complex biological systems, the field of glycoproteomics will continue to grow in the next decade. Innovative and effective MS‐based methods will exponentially advance glycoscience, and enable us to identify glycoproteins as effective biomarkers for disease detection and drug targets for disease treatment. © 2019 Wiley Periodicals, Inc. Mass Spec Rev 9999: XX–XX, 2019.

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Mass spectrometry for protein sialoglycosylation

Cited by 37 publications

References 345 publications

Biological Functions and Analytical Strategies of Sialic Acids in Tumor

Biological Functions and Analytical Strategies of Sialic Acids in Tumor

MS-Based Allotype-Specific Analysis of Polyclonal IgG-Fc N-Glycosylation

Global and site‐specific analysis of protein glycosylation in complex biological systems with Mass Spectrometry

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