Tracking <i>N</i>‐Acetyllactosamine on Cell‐Surface Glycans In Vivo

Zheng, Tianqing; Jiang, Hao; Gros, Marilyn; Amo, David Soriano del; Sundaram, Subha; Lauvau, Grégoire; Marlow, Florence; Liu, Yi; Stanley, Pamela; Wu, Peng

doi:10.1002/ange.201100265

Cited by 34 publications

(42 citation statements)

References 23 publications

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“…257 In another approach by Wu and co-workers, the authors demonstrated that wild-type α -1,3-fucosyltransferase from H. pylori could transfer fucose analogues (e.g., 6-azido-fucose) onto LacNAc residues. 258 Finally, to target Fuc- α -1,2-Gal, Hsieh-Wilson and co-workers demonstrated that the bacterial glycosyltransferase BgtA could transfer GalNAc analogues (e.g., 2-keto-Gal or GalNAz) onto the Gal residue within the Fuc- α -1,2-Gal motif. In the future, we anticipate that these new chemoenzymatic tagging strategies will be coupled with enrichment tags to help identify glycoprotein substrates containing higher-order glycans.…”

Section: Enrichment Of Glycoproteins and Glycopeptidesmentioning

confidence: 99%

Chemical Glycoproteomics

Palaniappan

Bertozzi²

2016

Chem. Rev.

227

205

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Chemical tools have accelerated progress in glycoscience, reducing experimental barriers to studying protein glycosylation, the most widespread and complex form of posttranslational modification. For example, chemical glycoproteomics technologies have enabled the identification of specific glycosylation sites and glycan structures that modulate protein function in a number of biological processes. This field is now entering a stage of logarithmic growth, during which chemical innovations combined with mass spectrometry advances could make it possible to fully characterize the human glycoproteome. In this review, we describe the important role that chemical glycoproteomics methods are playing in such efforts. We summarize developments in four key areas: enrichment of glycoproteins and glycopeptides from complex mixtures, emphasizing methods that exploit unique chemical properties of glycans or introduce unnatural functional groups through metabolic labeling and chemoenzymatic tagging; identification of sites of protein glycosylation; targeted glycoproteomics; and functional glycoproteomics, with a focus on probing interactions between glycoproteins and glycan-binding proteins. Our goal with this survey is to provide a foundation on which continued technological advancements can be made to promote further explorations of protein glycosylation.

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Section: Enrichment Of Glycoproteins and Glycopeptidesmentioning

confidence: 99%

Chemical Glycoproteomics

Palaniappan

Bertozzi²

2016

Chem. Rev.

227

205

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“…Robust labeling of the enveloping layer, the embryos’ outermost layer of cells, was achieved within 2–3 min. Using this bioorthogonal reaction, we also developed a chemoenzymatic approach for labeling cell surface glycans bearing the LacNAc disaccharide for imaging and glycomic analysis (Zheng et al ., 2011). …”

Section: Bioorthogonal Chemistry In Glycan Labeling: Merits and LImentioning

confidence: 99%

“…α-1,3-FucTM can be generated using our established protocol (Zheng et al ., 2011). The enzyme can be store at high concentration (>5 mg/mL) with 10% glycerol at 4 ° C and is stable for 3 months.…”

Section: Labeling Cell Surface Glycans Bearing the Lacnac Disacchamentioning

confidence: 99%

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Imaging the Glycome in Living Systems

Mock

2012

Methods in Enzymology

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The glycome, the full complement of glycans that cells produce, is an attractive target for molecular imaging. Imaging of the glycome in living systems has recently been enabled via bioorthogonal chemical reporter-based approaches. In this chapter, we describe two approaches to introduce bioorthogonal chemical reporters (tags) onto cell surface fucosylated glycans and glycans bearing LacNAc disaccharides, respectively. The tagged glycans can then be conjugated to imaging probes via bioorthogonal click chemistry. Similar approaches can be extended to image other sectors of the glycome in living systems.

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“…5 To identify proteins that are posttranslationally modified, azide or alkyne tags are introduced into the target protein pools either metabolically 6,7,8 or via enzymatic approaches. 9,10 In the second step, affinity probes, e.g. biotin, functionalized in a complementary fashion, are ligated, allowing for affinity capture, e.g.…”

mentioning

confidence: 99%

Single-Stranded DNA as a Cleavable Linker for Bioorthogonal Click Chemistry-Based Proteomics

Zheng

Jiang

2013

Bioconjugate Chem.

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In this report, we present a new class of cleavable linker based on automatically synthesized, single-stranded DNAs. We incorporated a DNA oligo into an azide-functionalized biotin (biotin-DNA-N3) and used the probe to enrich alkyne-tagged glycoproteins from mammalian cell lysates. Highly efficient and selective release of the captured proteins from streptavidin agarose resins was achieved using DNase treatment under very mild conditions. A total of 36 sialylated glycoproteins were identified from the lysates of HL60 cells, an acute human promyeloid leukemia cell line. These sialylated glycoproteins were involved in many different biological processes ranging from glycan biosynthesis to cell adhesion events.

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Tracking N‐Acetyllactosamine on Cell‐Surface Glycans In Vivo

Cited by 34 publications

References 23 publications

Chemical Glycoproteomics

Chemical Glycoproteomics

Imaging the Glycome in Living Systems

Single-Stranded DNA as a Cleavable Linker for Bioorthogonal Click Chemistry-Based Proteomics

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