Mechanistic and Therapeutic Implications of Protein and Lipid Sialylation in Human Diseases DOI Open Access
Xiaotian Zhong, Aaron M. D’Antona, Jason C. Rouse

et al.

International Journal of Molecular Sciences, Journal Year: 2024, Volume and Issue: 25(22), P. 11962 - 11962

Published: Nov. 7, 2024

Glycan structures of glycoproteins and glycolipids on the surface glycocalyx luminal sugar layers intracellular membrane compartments in human cells constitute a key interface between biological processes external environments. Sialic acids, class alpha-keto acid sugars with nine-carbon backbone, are frequently found as terminal residues these glycoconjugates, forming critical components layers. Changes status content cellular sialic acids closely linked to many diseases such cancer, cardiovascular, neurological, inflammatory, infectious, lysosomal storage diseases. The molecular machineries responsible for biosynthesis sialylated glycans, along their interacting partners, important therapeutic strategies targets drug development. purpose this article is comprehensively review recent literature provide new scientific insights into mechanisms implications sialylation across various Recent advances clinical developments acid-related therapies also summarized discussed.

Language: Английский

Chemoenzymatic synthesis of human natural killer-1-containing glycans and application as serum antibodies probes DOI
Mehman Bunyatov, Margreet A. Wolfert, Lin Liu

et al.

Nature Synthesis, Journal Year: 2023, Volume and Issue: 3(1), P. 85 - 98

Published: Oct. 2, 2023

Language: Английский

Citations

8

Non-targeted N-glycome profiling reveals multiple layers of organ-specific diversity in mice DOI Creative Commons
Johannes Helm, Stefan Mereiter, Tiago Oliveira

et al.

Nature Communications, Journal Year: 2024, Volume and Issue: 15(1)

Published: Nov. 9, 2024

N-glycosylation is one of the most common protein modifications in eukaryotes, with immense importance at molecular, cellular, and organismal level. Accurate reliable N-glycan analysis essential to obtain a systems-wide understanding fundamental biological processes. Due structural complexity glycans, their still highly challenging. Here we make publicly available consistent N-glycome dataset 20 different mouse tissues demonstrate multimodal data workflow that allows for unprecedented depth coverage features. This scalable, LC-MS/MS data-driven method integrates automated identification spectra, application non-targeted profiling strategies isomer-sensitive glycan structures. Our delineation critical sub-structural determinants isomers across uncovered tissue-specific glycosylation patterns, expression non-canonical structures highlights multiple layers derive from organ-specific regulations glycobiological pathways.

Language: Английский

Citations

2

Biology-driven material design for ischaemic stroke repair DOI
Nhi V. Phan,

Elle M. Rathbun,

Yunxin Ouyang

et al.

Nature Reviews Bioengineering, Journal Year: 2023, Volume and Issue: 2(1), P. 44 - 63

Published: Oct. 27, 2023

Language: Английский

Citations

6

N-glycans show distinct spatial distribution in mouse brain DOI
Maxence Noël, Richard D. Cummings, Robert G. Mealer

et al.

Glycobiology, Journal Year: 2023, Volume and Issue: 33(11), P. 935 - 942

Published: Oct. 4, 2023

Abstract The development and function of the brain requires N-linked glycosylation proteins, which is a ubiquitous modification in secretory pathway. N-glycans have distinct composition undergo tight regulation brain, but spatial distribution these structures remains relatively unexplored. Here, we systematically employed carbohydrate binding lectins with differing specificities to various classes appropriate controls identify glycan expression multiple regions mouse brain. Lectins high-mannose-type N-glycans, most abundant class showed diffuse staining some punctate observed on high magnification. specific motifs complex including fucose bisecting GlcNAc, more partitioned labeling, synapse-rich molecular layer cerebellum. Understanding across will aid future studies critical protein modifications disease

Language: Английский

Citations

4

The tissue glycome as regulator of immune activation and tolerance mediated by C-type lectins and Siglecs DOI Creative Commons
Eleonora Nardini, Ernesto Rodríguez, Yvette van Kooyk

et al.

Seminars in Immunology, Journal Year: 2024, Volume and Issue: 76, P. 101913 - 101913

Published: Nov. 1, 2024

Language: Английский

Citations

1

A draft of human N-glycans of glycoRNA DOI Creative Commons
Ming Bi, Zirui Zhang, Tao Wang

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2023, Volume and Issue: unknown

Published: Sept. 22, 2023

Abstract In addition to the backbone molecules of proteins and lipids, RNAs have recently been found be N-glycosylated as well in cell models. Some overlap N-glycans between RNA protein exist terms monosaccharide composition. Here we report a draft human tissue glycoRNA covering 12 typical organs characterized by mass spectrometry-based N-glycomics. were first prepared, then enzymatically released, hydrophilically enriched, permethylated, analyzed RPLC-MS/MS, finally identified N-glycan search engine GlySeeker. A total 676 putative sequence structures with 236 compositions across organs. Organ-specific similarity heterogeneity N-glycosylation glycoRNAs annotated. This comprehensive serves foundation for future structural functional studies. TOC Graphic

Language: Английский

Citations

3

Small but big leaps towards neuroglycomics: exploring N-glycome in the brain to advance the understanding of brain development and function DOI Creative Commons
Boyoung Lee, Hyun Joo An

Neural Regeneration Research, Journal Year: 2023, Volume and Issue: 19(3), P. 489 - 490

Published: July 20, 2023

Center for Cognition and Sociality, Institute Basic Science (IBS), Daejeon, South Korea (Lee B) Asia-Pacific Glycomics Reference Site, (An HJ) Graduate School of Analytical & Technology, Chungnam National University, Correspondence to: Hyun Joo An, PhD, [email protected]. Received April 5, 2023 in revised form 28, Accepted May 15, This is an open-access article distributed under the terms Creative Commons Attribution-Noncommercial-Share Alike 4.0 Unported, which permits unrestricted use, distribution, reproduction any medium, provided original work properly cited.

Language: Английский

Citations

2

Human-specific features and developmental dynamics of the brain N-glycome DOI Open Access
Thomas Klarić, Ivan Gudelj, Gabriel Santpere

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2023, Volume and Issue: unknown

Published: Jan. 11, 2023

Comparative "omics" studies have revealed unique aspects of human neurobiology, yet an evolutionary perspective the brain N-glycome is lacking. Here, we performed multi-regional characterization rat, macaque, chimpanzee, and N-glycomes using chromatography mass spectrometry, then integrated these data with complementary glycotranscriptomic data. We found that in primates has evolved more rapidly than underlying transcriptomic framework, providing a mechanism for generating additional diversity. show evolution hominids been characterized by increase complexity α(2-6)-linked N-acetylneuraminic acid along human-specific cell-type expression key glycogenes. Finally, comparing prenatal adult N-glycome, identify region-specific neurodevelopmental pathways lead to distinct spatial N-glycosylation profiles mature brain.Evolution marked shift sialic linkage.

Language: Английский

Citations

1

N-glycans show distinct spatial distribution in mouse brain DOI Creative Commons
Maxence Noël, Richard D. Cummings, Robert G. Mealer

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2023, Volume and Issue: unknown

Published: May 31, 2023

ABSTRACT Protein N-linked glycosylation is a ubiquitous modification in the secretory pathway that plays critical role development and function of brain. N-glycans have distinct composition undergo tight regulation brain, but spatial distribution these structures remains relatively unexplored. Here, we systematically employed carbohydrate binding lectins with differing specificities to various classes appropriate controls identify multiple regions mouse Lectins high-mannose-type N-glycans, most abundant class brain showed diffuse staining some punctate observed on high magnification. specific motifs complex including fucose bisecting GlcNAc, more partitioned labeling, synapse-rich molecular layer cerebellum. Understanding across will aid future studies protein modifications disease

Language: Английский

Citations

1

New avenues for human blood plasma biomarker discovery via improved in-depth analysis of the low-abundantN-glycoproteome DOI Creative Commons
Frania J. Zuniga-Banuelos, Marcus Hoffmann, Udo Reichl

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2023, Volume and Issue: unknown

Published: Oct. 22, 2023

Abstract To understand implications of protein glycosylation for clinical diagnostic and biopharmaceuticals, innovative glycoproteomic technologies are required. Recently, significant advances were made, particularly toward structure-focused N- glyco-proteomic analyses. The mass spectrometric analysis intact glycopeptides using stepped collision fragmentation along with glycan oxonium ion profiling now enables to reliably discriminate between different structures. Still, there weaknesses that current approaches must overcome: 1) handling incorrect identifications, 2) identification rare modified glycans, 3) insufficient coverage, especially in complex samples. address these shortcomings, we have developed an workflow aims at providing comprehensive site-specific structural data on human blood plasma glycoproteins. features depletion plus various fractionation strategies the use high-resolution spectrometry fragmentation. Furthermore, by including a decision tree procedure established validation, could significantly improve description micro-heterogeneity. Our allows reliable differentiation ambiguous structures like antenna-versus core-fucosylation glycans such as sulfated glucuronidated ones. With this workflow, able advance glycoproteins concentrations low 10 pg/mL. A total 1,929 942 glycosites derived from 805 middle-to low-abundant identified. Overall, presented holds great potential our understanding foster discovery biomarkers. Figure

Language: Английский

Citations

1