Seeing the forest through the trees: characterizing the glycoproteome

Critcher, Meg; Hassan, Abdullah A.; Huang, Mia L.

doi:10.1016/j.tibs.2022.02.007

Cited by 18 publications

(14 citation statements)

References 97 publications

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“…It requires extensive research to develop chemical tools to selectively modify a certain carbohydrate residue in a glycan of a glycopeptide or protein. The first hesitating steps in this direction have been made. , As an example, it turned out that glucose residues in several peptides could be oxidized with reasonable selectivity . The resulting ketone function was subsequently used to ligate the glycopeptide to biotin, for analysis by mass spectrometry.…”

Section: Discussionmentioning

confidence: 99%

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Site-Selective Modification of (Oligo)Saccharides

Witte

Minnaard

2022

ACS Catal.

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Oligosaccharides, either as such or as part of glycolipids, glycopeptides, or glycoproteins, are ubiquitous in nature and fulfill important roles in the living cell. Also in medicine and to some extent in materials, oligosaccharides play an important role. In order to study their function, modifying naturally occurring oligosaccharides, and building in reactive groups and reporter groups in oligosaccharides, are key strategies. The development of oligosaccharides as drugs, or vaccines, requires the introduction of subtle modifications in the structure of oligosaccharides to optimize efficacy and, in the case of antibiotics, circumvent bacterial resistance. Provided the natural oligosaccharide is available, site-selective modification is an attractive approach as total synthesis of the target is often very laborious. Researchers in catalysis areas, such as transition-metal catalysis, enzyme catalysis, organocatalysis, and photoredox catalysis, have made considerable progress in the development of site-selective and late-stage modification methods for mono- and oligosaccharides. It is foreseen that the fields of enzymatic modification of glycans and the chemical modification of (oligo)saccharides will approach and potentially meet each other, but there is a lot to learn and discover before this will be the case.

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Section: Discussionmentioning

confidence: 99%

“…The first hesitating steps in this direction have been made. 48,49 As an example, it turned out that glucose residues in several peptides could be oxidized with reasonable selectivity. 50 The resulting ketone function was subsequently used to ligate the glycopeptide to biotin, for analysis by mass spectrometry.…”

Section: ■ Discussionmentioning

confidence: 99%

Site-Selective Modification of (Oligo)Saccharides

Witte

Minnaard

2022

ACS Catal.

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“…Although several methods have been developed to survey the protein-binding partners of glycoconjugates in live cells, these techniques have not been applied directly to the study of free glycans. 18 Thus, we hypothesized that photoaffinity labeling could be applied towards the study of HMO interactions in live cells. 19,20 Photoaffinity labeling is able to capture transient and low affinity interactions, and has been previously combined with metabolic oligosaccharide engineering to profile interactions with glycoconjugates.…”

Section: Introductionmentioning

confidence: 99%

Chemoproteomic mapping of human milk oligosaccharide (HMO) interactions in cells

et al. 2022

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“…The role of glycosylation in modulating various aspects of protein biology is a broad research field ( Ward et al, 2021 ; Critcher et al, 2022 ). O-linked glycosylation and N-linked glycosylation are the two most important forms of protein glycosylation ( Sun et al, 2021 ).…”

Section: Introductionmentioning

confidence: 99%

Nascent Glycoproteome Reveals That N-Linked Glycosylation Inhibitor-1 Suppresses Expression of Glycosylated Lysosome-Associated Membrane Protein-2

Cao

Meng

Shao

et al. 2022

Front. Mol. Biosci.

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Glycosylation inhibition has great potential in cancer treatment. However, the corresponding cellular response, protein expression and glycosylation changes remain unclear. As a cell-permeable small-molecule inhibitor with reduced cellular toxicity, N-linked glycosylation inhibitor-1 (NGI-1) has become a great approach to regulate glycosylation in mammalian cells. Here for the first time, we applied a nascent proteomic method to investigate the effect of NGI-1 in hepatocellular carcinoma (HCC) cell line. Besides, hydrophilic interaction liquid chromatography (HILIC) was adopted for the enrichment of glycosylated peptides. Glycoproteomic analysis revealed the abundance of glycopeptides from LAMP2, NICA, and CEIP2 was significantly changed during NGI-1 treatment. Moreover, the alterations of LAMP2 site-specific intact N-glycopeptides were comprehensively assessed. NGI-1 treatment also led to the inhibition of Cathepsin D maturation and the induction of autophagy. In summary, we provided evidence that NGI-1 repressed the expression of glycosylated LAMP2 accompanied with the occurrence of lysosomal defects and autophagy.

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Seeing the forest through the trees: characterizing the glycoproteome

Cited by 18 publications

References 97 publications

Site-Selective Modification of (Oligo)Saccharides

Site-Selective Modification of (Oligo)Saccharides

Chemoproteomic mapping of human milk oligosaccharide (HMO) interactions in cells

Nascent Glycoproteome Reveals That N-Linked Glycosylation Inhibitor-1 Suppresses Expression of Glycosylated Lysosome-Associated Membrane Protein-2

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