Liberation of Protein-Specific Glycosylation Information for Glycan Analysis by Exonuclease III-Aided Recycling Hybridization

Chen, Yunlong; Ding, Lin; Song, Wanyao; Yang, Min; Ju, Huangxian

doi:10.1021/acs.analchem.5b04883

Cited by 28 publications

(15 citation statements)

References 31 publications

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“…In addition to selective labeling, the relatively low sensitivity of FRET-based methods is another challenge to overcome. , The background signals derived from thousands of other proteins carrying the same glycans require an efficient strategy to yield high signal-to-noise. , To this end, several amplification strategies have been reported to enhance the sensitivity, such as proximity ligation assay, , rolling-circle amplification, and exonuclease III-aided recycling hybridization . Nevertheless, all of these methods are highly enzyme-dependent, thereby impeding their application under living conditions.…”

Section: Introductionmentioning

confidence: 99%

“…22,23 To this end, several amplification strategies have been reported to enhance the sensitivity, such as proximity ligation assay, 24,25 rolling-circle amplification, 26 and exonuclease III-aided recycling hybridization. 27 Nevertheless, all of these methods are highly enzymedependent, thereby impeding their application under living conditions. For this reason, it is still highly desired to develop sensitive imaging strategies for visualizing protein-specific glycosylation in vivo.…”

Section: ■ Introductionmentioning

confidence: 99%

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Amplified Visualization of Protein-Specific Glycosylation in Zebrafish via Proximity-Induced Hybridization Chain Reaction

et al. 2018

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The visualization of glycosylation states of specific proteins in vivo is of great importance for uncovering their roles in disease development. However, the ubiquity of glycosylation makes probing the glycans on a certain protein as difficult as looking for a needle in a haystack. Herein, we demonstrate a proximity-induced hybridization chain reaction (HCR) strategy for amplified visualization of protein-specific glycosylation. The strategy relies on designing two kinds of DNA probes, glycan conversion probes and protein recognition probes, which are attached to glycans and target proteins, respectively. Upon sequential binding to the targets, the proximity-induced hybridization between two probes occurs, which leads to the structure-switching of protein recognition probes, followed by triggering of HCR assembly. This strategy has been used to visualize tyrosine-protein kinase 7-specific sialic acid in living CEM cells and zebrafish and to monitor its variation during drug treatment. It provides a potential tool for investigating protein-specific glycosylation and researching the relation between dynamic glycans state and disease process.

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Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Amplified Visualization of Protein-Specific Glycosylation in Zebrafish via Proximity-Induced Hybridization Chain Reaction

et al. 2018

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“…Thus, by combining confocal FRET microscopy with an RCA reaction, researchers can conveniently and clearly image glycosylation of a specific protein. Compared with previous work, which developed a strategy for information liberation of protein specific glycosylation via an exonuclease III-aided recycling, 42 our work has two obvious advantages. First, unlike the RCA process, the reported work relies on the recycling “hybridization and cleavage” process of the protein probe with other adjacent glycan probes.…”

Section: Resultsmentioning

confidence: 93%

Applying DNA rolling circle amplification in fluorescence imaging of cell surface glycans labeled by a metabolic method

Zhang

Chen

et al. 2016

Chem. Sci.

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“…We detected this molecule in MCF7 cells. Chen et al found that EpCAM is sialylated in MCF7 and that its degree of sialylation may be changed by drugs [91].…”

Section: Cell Adhesion Moleculesmentioning

confidence: 99%

Insight in Adhesion Protein Sialylation and Microgravity Dependent Cell Adhesion—An Omics Network Approach

Bauer

Gombocz²,

Wehland

et al. 2020

IJMS

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The adhesion behavior of human tissue cells changes in vitro, when gravity forces affecting these cells are modified. To understand the mechanisms underlying these changes, proteins involved in cell-cell or cell-extracellular matrix adhesion, their expression, accumulation, localization, and posttranslational modification (PTM) regarding changes during exposure to microgravity were investigated. As the sialylation of adhesion proteins is influencing cell adhesion on Earth in vitro and in vivo, we analyzed the sialylation of cell adhesion molecules detected by omics studies on cells, which change their adhesion behavior when exposed to microgravity. Using a knowledge graph created from experimental omics data and semantic searches across several reference databases, we studied the sialylation of adhesion proteins glycosylated at their extracellular domains with regards to its sensitivity to microgravity. This way, experimental omics data networked with the current knowledge about the binding of sialic acids to cell adhesion proteins, its regulation, and interactions in between those proteins provided insights into the mechanisms behind our experimental findings, suggesting that balancing the sialylation against the de-sialylation of the terminal ends of the adhesion proteins’ glycans influences their binding activity. This sheds light on the transition from two- to three-dimensional growth observed in microgravity, mirroring cell migration and cancer metastasis in vivo.

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Liberation of Protein-Specific Glycosylation Information for Glycan Analysis by Exonuclease III-Aided Recycling Hybridization

Cited by 28 publications

References 31 publications

Amplified Visualization of Protein-Specific Glycosylation in Zebrafish via Proximity-Induced Hybridization Chain Reaction

Amplified Visualization of Protein-Specific Glycosylation in Zebrafish via Proximity-Induced Hybridization Chain Reaction

Applying DNA rolling circle amplification in fluorescence imaging of cell surface glycans labeled by a metabolic method

Insight in Adhesion Protein Sialylation and Microgravity Dependent Cell Adhesion—An Omics Network Approach

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