Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2019–2020

Harvey, David J.

doi:10.1002/mas.21806

Cited by 15 publications

(6 citation statements)

References 1,622 publications

(508 reference statements)

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“…Ongoing advances in MSI in sample preparation, ion sources, and mass analyzers have enabled broader and more diverse research in glycoscience. As these have been reviewed recently, − we focus on a special topic: mass-tag-based strategies for MSI of glycans. A typical probe contains a labeling module targeting known GOIs and a mass tag (or several mass tags) that can be easily released for MALDI detection.…”

Section: Recent Progress In Glycan Imagingmentioning

confidence: 99%

In Situ Glycan Analysis and Editing in Living Systems

Li,

Wang,

Chen

et al. 2024

JACS Au

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Besides proteins and nucleic acids, carbohydrates are also ubiquitous building blocks of living systems. Approximately 70% of mammalian proteins are glycosylated. Glycans not only provide structural support for living systems but also act as crucial regulators of cellular functions. As a result, they are considered essential pieces of the life science puzzle. However, research on glycans has lagged far behind that on proteins and nucleic acids. The main reason is that glycans are not direct products of gene coding, and their synthesis is nontemplated. In addition, the diversity of monosaccharide species and their linkage patterns contribute to the complexity of the glycan structures, which is the molecular basis for their diverse functions. Research in glycobiology is extremely challenging, especially for the in situ elucidation of glycan structures and functions. There is an urgent need to develop highly specific glycan labeling tools and imaging methods and devise glycan editing strategies. This Perspective focuses on the challenges of in situ analysis of glycans in living systems at three spatial levels (i.e., cell, tissue, and in vivo) and highlights recent advances and directions in glycan labeling, imaging, and editing tools. We believe that examining the current development landscape and the existing bottlenecks can drive the evolution of in situ glycan analysis and intervention strategies and provide glycan-based insights for clinical diagnosis and therapeutics.

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Section: Recent Progress In Glycan Imagingmentioning

confidence: 99%

In Situ Glycan Analysis and Editing in Living Systems

Li,

Wang,

Chen

et al. 2024

JACS Au

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“…The low abundance of glycoproteins, dynamic nature of glycosylation, and difficulty in EVs separation are major limitations of studies on glycosylation of EVs. In addition, the low ionization efficiency of glycans, diverse glycan structures, and interference from non‐glycopeptides or other hydrophobic substances can also seriously affect the detection of glycopeptides and glycans [57]. Therefore, enrichment or purification of glycoproteins or glycans is necessary before mass spectrometric analysis.…”

Section: General Approaches For Studying Protein Glycosylation Includ...mentioning

confidence: 99%

Comprehensive review of MS‐based studies on N‐glycoproteome and N‐glycome of extracellular vesicles

et al. 2023

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Extracellular vesicles (EVs) are lipid bilayer‐enclosed particles that can be released by all type of cells. Whereas, as one of the most common post‐translational modifications, glycosylation plays a vital role in various biological functions of EVs, such as EV biogenesis, sorting, and cellular recognition. Nevertheless, compared with studies on RNAs or proteins, those investigating the glycoconjugates of EVs are limited. An in‐depth investigation of N‐glycosylation of EVs can improve the understanding of the biological functions of EVs and help to exploit EVs from different perspectives. The general focus of studies on glycosylation of EVs primarily includes isolation and characterization of EVs, preparation of glycoproteome/glycome samples and MS analysis. However, the low content of EVs and non‐standard separation methods for downstream analysis are the main limitations of these studies. In this review, we highlight the importance of glycopeptide/glycan enrichment and derivatization owing to the low abundance of glycoproteins and the low ionization efficiency of glycans. Diverse fragmentation patterns and professional analytical software are indispensable for analysing glycosylation via MS. Altogether, this review summarises recent studies on glycosylation of EVs, revealing the role of EVs in disease progression and their remarkable potential as biomarkers.

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“…This result suggests that DAN is unsuitable for use in the ISD analysis of cAFGPs. On the other hand, the use of DHB (Figure 2c), DAN/DHB/Na (Figure 2d), and AHB/Na (Figure 2e In general, the MALDI-TOFMS of glycoprotein glycans involves the cleavage and separation of the glycan component from the protein, which is then mixed with the matrix for analysis [15]. The addition of aniline derivatives to DHB has been reported to improve the ionization efficiency of cleaved glycan components [17,18].…”

Section: Maldi-isd Analysis Of O-linked Cyclic Glycopeptidesmentioning

confidence: 99%

“…However, AHB was soon replaced by 2,5dihydroxybenzoic acid (DHB; Figure 1) [13,14], which was discovered in the same year (1991) due to its high ionization efficiency and versatility. Nowadays, DHB is the gold standard matrix for glycan analysis, and few studies utilize AHB [15,16].…”

Section: Introductionmentioning

confidence: 99%

Sodium-Doped 3-Amino-4-hydroxybenzoic Acid: Rediscovered Matrix for Direct MALDI Glycotyping of O-Linked Glycopeptides and Intact Mucins

Urakami,

Hinou

2023

IJMS

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3-Amino-4-hydroxybenzoic acid (AHB) was the first matrix identified by glycoprotein glycan analysis using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). However, compared to commonly used matrices, such as 2,5-dihydroxybenzoic acid (DHB), AHB is less efficient at glycan ionization and lacks the ability to ionize other molecular species, such as peptides, and thus is no longer used. In this study, we focused on the glycan-selective ionization ability of AHB and its low-noise properties in the low-molecular-weight region, as we expected that these properties could be enhanced by adding sodium to AHB. Sodium-doped AHB (AHB/Na) selectively imparts sodium adduct ions onto O-glycan fragments generated by the in-source decay (ISD) of glycopeptides and glycoproteins containing O-glycans that occurs during intense laser irradiation, enabling direct O-glycan analysis. Furthermore, we demonstrated that it is possible to investigate the internal structure of each O-glycan fragment with pseudo-MS/MS/MS using the sodium adduct ion of the O-glycan-derived ISD fragments from an intact mucin mixture.

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Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2019–2020

Cited by 15 publications

References 1,622 publications

In Situ Glycan Analysis and Editing in Living Systems

In Situ Glycan Analysis and Editing in Living Systems

Comprehensive review of MS‐based studies on N‐glycoproteome and N‐glycome of extracellular vesicles

Sodium-Doped 3-Amino-4-hydroxybenzoic Acid: Rediscovered Matrix for Direct MALDI Glycotyping of O-Linked Glycopeptides and Intact Mucins

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