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/anie.201100265

Cited by 84 publications

(60 citation statements)

References 24 publications

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“…Interestingly, the periarteriolar lymphoid sheaths (PALS) of the white pulp of the spleen, where naïve T cells reside, had lower LacNAc expression (Figure 4, Figure S7). This result is consistent with our previous findings, obtained by flow cytometry, which show that activated T cells bear higher levels of LacNAc as compared to their naïve counterparts [25] . This pattern, however, was not distinguishable using the direct labeling method.…”

supporting

confidence: 94%

CHoMP: A Chemoenzymatic Histology Method Using Clickable Probes

Rouhanifard

López-Aguilar

2014

ChemBioChem

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The characterization of aberrant glycosylation patterns in biopsied patient samples represents a remarkable challenge for scientists and medical doctors due to the lack of specific methods for their detection. Here, we report the development of a histological method, dubbed CHoMP—Chemoenzymatic Histology of Membrane Polysaccharides—for analyzing glycosylation patterns in mammalian tissues. This method exploits a recombinant glycosyltransferase to transfer a monosaccharide analog equipped with a chemical handle to a specific cell-surface glycan target, which can then be derivatized with imaging probes using bioorthogonal click chemistry for visualization. We applied CHoMP to survey changes in expression of N-acetyllactosamine (LacNAc) in human samples from patients afflicted with lung adenocarcinoma and observed a sharp decrease in expression levels between normal and early grade tumors, suggestion a potential application of this technique in early cancer diagnosis.

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supporting

confidence: 94%

CHoMP: A Chemoenzymatic Histology Method Using Clickable Probes

Rouhanifard

López-Aguilar

2014

ChemBioChem

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“…S2A). Fucose modification can also be achieved by directly adding fucose using in vitro fucosylation assays (Zheng et al, 2011)(Fig. S2A).…”

Section: Resultsmentioning

confidence: 99%

“…To control for potential differential responses between cell lines, we performed in vitro fucosylation assays as described (Zheng et al, 2011). Since both CHO and LEC30 lines have endogenous Wnt activity, we normalized all data to untreated CHO or LEC30 lines, which we set as 100%.…”

Section: Methodsmentioning

confidence: 99%

Negative feedback regulation of Wnt signaling via N-linked fucosylation in zebrafish

Feng

Jiang

et al. 2014

Developmental Biology

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Summary L-fucose, a monosaccharide widely distributed in eukaryotes and certain bacteria, is a determinant of many functional glycans that play central roles in numerous biological processes. The molecular mechanism, however, by which fucosylation mediates these processes remains largely elusive. To study how changes in fucosylation impact embryonic development, we up-regulated N-linked fucosylation via over-expression of a key GDP-Fucose transporter, Slc35c1, in zebrafish. We show that Slc35c1 overexpression causes elevated N-linked fucosylation and disrupts embryonic patterning in a transporter activity dependent manner. We demonstrate that patterning defects associated with enhanced N-linked fucosylation are due to diminished canonical Wnt signaling. Chimeric analyses demonstrate that elevated Slc35c1 expression in receiving cells decreases the signaling range of Wnt8a during zebrafish embryogenesis. Moreover, we provide biochemical evidence that this decrease is associated with degradation of Wnt8 ligand and elevated Lrp6 coreceptor, which we show are both substrates for N-linked fucosylation in zebrafish embryos. Strikingly, slc35c1 expression is regulated by canonical Wnt signaling. These results suggest that Wnt limits its own signaling activity in part via up-regulation of a transporter, slc35c1 that promotes terminal fucosylation and thereby limits Wnt activity.

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“…[18] Furthermore, it has been shown that GDP-6-azidofucose is readily accepted by a recombinant H. pylori a(1,3)-fucosyltransferase, and this has been successfully employed to image glycans in the enveloping layer of zebrafish embryos. [19] The attraction of enzymatic labeling is that it affords near quantitative labeling, does not perturb signaling pathways, and is amenable to all cell types.…”

mentioning

confidence: 99%

Selective Exo‐Enzymatic Labeling of N‐Glycans on the Surface of Living Cells by Recombinant ST6Gal I

Mbua

Flanagan-Steet

et al. 2013

Angewandte Chemie

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Mit Sternchen: Die selektive Markierung von N‐Glykanen auf der Oberfläche lebender Zellen gelingt mittels exogener rekombinanter ST6Gal‐I‐Sialyltransferase und azidmodifiziertem CMP‐Neu5Ac und anschließender spannungsvermittelter Cycloaddition mit einem biotinmodifizierten Dibenzylcyclooctinol (siehe Schema; roter Stern=Biotin). Mithilfe dieser Methode können die Mechanismen krankheitsbedingt veränderter Glykokonjugat‐Speicherung und ‐Rezyklierung aufgeklärt werden.

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Tracking N‐Acetyllactosamine on Cell‐Surface Glycans In Vivo

Cited by 84 publications

References 24 publications

CHoMP: A Chemoenzymatic Histology Method Using Clickable Probes

CHoMP: A Chemoenzymatic Histology Method Using Clickable Probes

Negative feedback regulation of Wnt signaling via N-linked fucosylation in zebrafish

Selective Exo‐Enzymatic Labeling of N‐Glycans on the Surface of Living Cells by Recombinant ST6Gal I

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