Probing the CMP‐Sialic Acid Donor Specificity of Two Human β‐<scp>d</scp>‐Galactoside Sialyltransferases (ST3Gal I and ST6Gal I) Selectively Acting on O‐ and N‐Glycosylproteins

Noël, Maxence; Gilormini, Pierre-André; Cogez, Virginie; Yamakawa, Nao; Vicogne, Dorothée; Lion, Cédric; Biot, Christophe; Guérardel, Yann; Harduin-Lepers, Anne

doi:10.1002/cbic.201700024

Cited by 42 publications

(49 citation statements)

References 58 publications

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“…In principle, dual labeling studies with our approach can also be extended to other biomolecules by using two distinct modified precursors of plant cell wall polymers - including all three main monolignols or their metabolic precursors as well as various monosaccharides that constitute the polysaccharide matrix. Since its inception, bioorthogonal chemistry has indeed been mainly developed to investigate glycans/polysaccharides through metabolic oligosaccharide engineering (MOE) 4 5 17 28 , but surprisingly there have been only very few applications to plant biology so far 7 8 9 10 11 12 . In terms of compatibility of the reactions, the study of lignin was indeed a complex case to solve as both chemical reporters are incorporated into the same reticulated polymer.…”

Section: Discussionmentioning

confidence: 99%

Visualizing Lignification Dynamics in Plants with Click Chemistry: Dual Labeling is BLISS!

Simon

Spriet

Hawkins

et al. 2018

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Lignin is one of the most prevalent biopolymers on the planet and a major component of lignocellulosic biomass. This phenolic polymer plays a vital structural and protective role in the development and life of higher plants. Although the intricate mechanisms regulating lignification processes in vivo strongly impact the industrial valorization of many plant-derived products, the scientific community still has a long way to go to decipher them. In a simple three-step workflow, the dual labeling protocol presented herein enables bioimaging studies of actively lignifying zones of plant tissues. The first step consists in the metabolic incorporation of two independent chemical reporters, surrogates of the two native monolignols that give rise to lignin H- and G-units. After incorporation into growing lignin polymers, each reporter is then specifically labeled with its own fluorescent probe via a sequential combination of bioorthogonal SPAAC/CuAAC click reactions. Combined with lignin autofluorescence, this approach leads to the generation of three-color localization maps of lignin within plant cell walls by confocal fluorescence microscopy and provides precise spatial information on the presence or absence of active lignification machinery at the scale of plant tissues, cells and different cell wall layers.

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Section: Discussionmentioning

confidence: 99%

Visualizing Lignification Dynamics in Plants with Click Chemistry: Dual Labeling is BLISS!

Simon

Spriet

Hawkins

et al. 2018

JoVE

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“…Individual sialic acid derivatives were quantified by integration of fluorescence signals after HPLC separation, plotted against standard curves of corresponding authentic standards. In parallel, the nature of sialic acids was confirmed by analyzing MS and MS/MS fragmentation patterns by LC/MS based on known patterns 73 , 74 .…”

Section: Methodsmentioning

confidence: 99%

Systems glycomics of adult zebrafish identifies organ-specific sialylation and glycosylation patterns

et al. 2018

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The emergence of zebrafish Danio rerio as a versatile model organism provides the unique opportunity to monitor the functions of glycosylation throughout vertebrate embryogenesis, providing insights into human diseases caused by glycosylation defects. Using a combination of chemical modifications, enzymatic digestion and mass spectrometry analyses, we establish here the precise glycomic profiles of eight individual zebrafish organs and demonstrate that the protein glycosylation and glycosphingolipid expression patterns exhibits exquisite specificity. Concomitant expression screening of a wide array of enzymes involved in the synthesis and transfer of sialic acids shows that the presence of organ-specific sialylation motifs correlates with the localized activity of the corresponding glycan biosynthesis pathways. These findings provide a basis for the rational design of zebrafish lines expressing desired glycosylation profiles.

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“…In individuals of South Asian ancestry, ST6GAL1 has also been associated with type 2 diabetes . ST6GAL1 encodes an N‐glycosylation pathway protein responsible for the transfer of α2,6‐linked sialic acid to galactose‐containing substrates . Identified type 2 diabetes risk allele in European‐descent individuals was associated with an increase in ST6GAL1 expression in islets .…”

Section: Type 2 Diabetesmentioning

confidence: 99%

Altered N‐glycosylation profiles as potential biomarkers and drug targets in diabetes

2019

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N‐glycosylation is a ubiquitous protein modification, and N‐glycosylation profiles are emerging as both biomarkers and functional effectors in various types of diabetes. Genome‐wide association studies identified glycosyltransferase genes as candidate causal genes for type 1 and type 2 diabetes. Studies focused on N‐glycosylation changes in type 2 diabetes demonstrated that patients can be distinguished from healthy controls based on N‐glycome composition. In addition, individuals at an increased risk of future disease development could be identified based on N‐glycome profiles. Moreover, accumulating evidence indicates that N‐glycans have a major role in preventing the impairment of glucose‐stimulated insulin secretion by maintaining the glucose transporter in proper orientation, indicating that interindividual variation in protein N‐glycosylation might be a novel risk factor contributing to diabetes development. Defective N‐glycosylation of T cells has been implicated in type 1 diabetes pathogenesis. Furthermore, studies of N‐glycan alterations have successfully been used to identify individuals with rare types of diabetes (such as the HNF1A‐MODY), and also to evaluate functional significance of novel diabetes‐associated mutations. In conclusion, both N‐glycans and glycosyltransferases emerge as potential therapeutic targets in diabetes.

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Probing the CMP‐Sialic Acid Donor Specificity of Two Human β‐d‐Galactoside Sialyltransferases (ST3Gal I and ST6Gal I) Selectively Acting on O‐ and N‐Glycosylproteins

Cited by 42 publications

References 58 publications

Visualizing Lignification Dynamics in Plants with Click Chemistry: Dual Labeling is BLISS!

Visualizing Lignification Dynamics in Plants with Click Chemistry: Dual Labeling is BLISS!

Systems glycomics of adult zebrafish identifies organ-specific sialylation and glycosylation patterns

Altered N‐glycosylation profiles as potential biomarkers and drug targets in diabetes

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