Recent development of analytical methods for disease-specific protein<i>O</i>-GlcNAcylation

Hu, Wenhua; Zhang, Guolin; Zhou, Yu; Xia, Jun; Zhang, Peng; Xiao, Wenjin; Xue, Mingzhu; Lu, Zhaohui; Yang, Shuang

doi:10.1039/d2ra07184c

Cited by 11 publications

(11 citation statements)

References 193 publications

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“…The underlying mechanism remains to be discovered, but it can be inferred from this result that there is no direct link between urinary and serum N-glycan groups in PD. Characterizing the glycome is important even if the same patient sample is collected for disease-specific glycan analysis. , …”

Section: Resultsmentioning

confidence: 99%

“…Characterizing the glycome is important even if the same patient sample is collected for disease-specific glycan analysis. 39,40 Dysregulated expression of glycosyltransferases has been implicated in the pathogenesis of PD, so altered glycosylation is expected. Sialylation of triantennary glycans, such as Oglycans 41 and IgG N-glycans, 42 is reduced in PD patients.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Mass Spectrometric Analysis of Urinary N-Glycosylation Changes in Patients with Parkinson’s Disease

Xu,

Jin,

et al. 2023

ACS Chem. Neurosci.

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Urine is thought to provide earlier and more sensitive molecular changes for biomarker discovery than blood. Numerous glycoproteins, peptides, and free glycans are present in urine through glomerular filtration of plasma, cell shedding, apoptosis, proteolytic cleavage, and exosome secretion. Urine biomarkers have enormous diagnostic potential, and the use of these biomarkers is a long-standing practice. The discovery of non-urological disease biomarkers from urine is also gaining attention due to its non-invasive sample collection and ease of analysis. Abnormal protein glycosylation in plasma or cerebrospinal fluid has been associated with Parkinson’s disease, however, whether urine with Parkinson’s disease has characteristic glycosylation remains to be explored. Here, we use mass spectrometry-based glycomics and glycoproteomics approaches to analyze urine samples for glycans, glycosites, and intact glycopeptides of urine samples. Reduced abundance of N-glycans was detected at the level of total glycans as well as specific glycosites of glycopeptides. The most abundant N-glycan in urine is S(6)1H5N4F1; S(6)2H5N4 and N4H4F1 are highly present in serum and urine, and 10 biantennary galactosylated N-glycans in the urine of PD patients were significantly decreased. The downregulation of sialylation may be due to the reduction of ST3GAL2. Site-specific N-glycosylation analysis revealed that AMBP, UMOD, and RNase1 have PD-specific N-glycosylation sites. GO and KEGG analysis revealed that N-glycosylation changes may provide clues to identify disease-specific glycosylation biomarkers in Parkinson’s disease.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Mass Spectrometric Analysis of Urinary N-Glycosylation Changes in Patients with Parkinson’s Disease

Xu,

Jin,

et al. 2023

ACS Chem. Neurosci.

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“…Therefore, real-time monitoring of a biologically important saccharide or a tumor marker will result in further health promotion. , However, such simultaneous selectivity and sensitivity are difficult owing to the heavy hydration, structural/conformational diversity, and low concentration of saccharides in the blood. ,− In contrast, the most successful materials for mono- and disaccharide sensing are chemosensors, which exhibit dynamic boronate formation with saccharide diols − or supramolecular cages that interact with the saccharides via noncovalent interactions. − These lock-and-key type chemosensors are the most popular strategies; however, there is a limitation for targeting higher oligomeric analogues because the binding site should be expanded to exactly fit to the higher ones in size and shape. In contrast to the lock-and-key or “rigid” approach, nature adopts an induced-fit or “flexible” manner to achieve smarter sensing toward more complicated oligosaccharides; therefore, highly spreading networks of hydrogen bonds and CH−π interactions may hold great promise. − Recently, we observed that curdlan (Cur), as shown in Figure a, functions as a polymer receptor that traps oligosaccharides in dynamic hydrogen-bonding networks. − …”

Section: Introductionmentioning

confidence: 99%

“…Oligosaccharide recognition/sensing by artificial supramolecular hosts or chemosensors in aqueous media has become one of the most attractive topics in current multidisciplinary chemistry; however, it faces a major challenge from the viewpoints of both basic science and practical applications. − In fact, highly selective and sensitive sensing of target saccharides in physiological solutions is particularly desirable in real medical sites. Therefore, real-time monitoring of a biologically important saccharide or a tumor marker will result in further health promotion. , However, such simultaneous selectivity and sensitivity are difficult owing to the heavy hydration, structural/conformational diversity, and low concentration of saccharides in the blood. ,− In contrast, the most successful materials for mono- and disaccharide sensing are chemosensors, which exhibit dynamic boronate formation with saccharide diols − or supramolecular cages that interact with the saccharides via noncovalent interactions. − These lock-and-key type chemosensors are the most popular strategies; however, there is a limitation for targeting higher oligomeric analogues because the binding site should be expanded to exactly fit to the higher ones in size and shape.…”

Section: Introductionmentioning

confidence: 99%

Oligosaccharide Sensing Using Fluorophore-Probed Curdlans in Aqueous Media

Hori

Numata

Fukuhara

2023

ACS Appl. Polym. Mater.

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Saccharide sensing in aqueous media has recently garnered considerable attention in supramolecular and analytical chemistry; however, it still faces significant challenges. Herein, we report oligosaccharide sensing using the designed and synthesized fluorophore-probed curdlans. Aggregation-induced emission of the tetraphenylethylene (TPE) chromophore is a powerful candidate for outputting fluorescence signals upon the addition of the target oligosaccharide acarbose. Among the saccharides tested, the TPE-Cur chemosensors simultaneously exhibited high sensitivity and excellent selectivity toward acarbose. Morphological studies using atomic force microscopy, dynamic light scattering, fluorescence spectroscopy, and lifetime measurements revealed the importance of globule-to-coaggregation conversion upon oligosaccharide incorporation into the dynamic hydrogen-bonding networks of the curdlan string. This study provides perspectives for saccharide-responsive materials that are an attractive alternative to conventional chemosensors, which are difficult to sense in aqueous media.

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“…One category involves direct capture of O-GlcNAcylated proteins by antibodies or lectins that recognize the GlcNAc moiety [27][28][29][30][31][32][33] . O-GlcNAc antibodies including RL2 and CTD110.6, as well as O-GlcNAc-binding lectins such as wheat germ agglutinin (WGA), are commonly used for enrichment.…”

Section: Introductionmentioning

confidence: 99%

Olfactory learning inDrosophilarequires O-GlcNAcylation of mushroom body ribosomal subunits

Yu,

Liu,

Zhang

et al. 2023

Preprint

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O-GlcNAcylation is a dynamic post-translational modification that diversifies the proteome. Its dysregulation is associated with neurological disorders that impair cognitive function, and yet identification of phenotype-relevant candidate substrates in a brain-region specific manner remains unfeasible. By combining an O-GlcNAc binding activity derived fromClostridium perfringensOGA (Cp OGA) with TurboID proximity labeling inDrosophila, we developed an O-GlcNAcylation profiling tool that translates O-GlcNAc modification into biotin conjugation for tissue-specific candidate substrates enrichment. We mapped the O-GlcNAc interactome in major brain regions ofDrosophilaand found that components of the translational machinery, including many ribosomal subunits, were abundantly O-GlcNAcylated in the mushroom body, the computational center of theDrosophilabrain. Hypo-O-GlcNAcylation induced by ectopic expression of active Cp OGA in the mushroom body decreased local ribosomal activity, leading to olfactory learning deficits that could be rescued by increasing ribosome biogenesis. Our study reveals that O-GlcNAcylation contributes to the links between protein synthesis and cognitive function in the brain learning center, and provides a useful tool for future dissection of tissue-specific functions of O-GlcNAcylation inDrosophila.

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Recent development of analytical methods for disease-specific proteinO-GlcNAcylation

Abstract: The enzymatic modification of protein serine or threonine residues by N-acetylglucosamine, namely O-GlcNAcylation, is a ubiquitous post-translational modification that frequently occurs in the nucleus and cytoplasm.

Cited by 11 publications

References 193 publications

Mass Spectrometric Analysis of Urinary N-Glycosylation Changes in Patients with Parkinson’s Disease

Mass Spectrometric Analysis of Urinary N-Glycosylation Changes in Patients with Parkinson’s Disease

Oligosaccharide Sensing Using Fluorophore-Probed Curdlans in Aqueous Media

Olfactory learning inDrosophilarequires O-GlcNAcylation of mushroom body ribosomal subunits

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