Evidence map›Paper›PMID 36729338›Full record

ArticleCellular and molecular life sciences : CMLS2023

"Glyco-sulfo barcodes" regulate chemokine receptor function.

Lisa Verhallen, Jarkko J Lackman, Rikke Wendt, Martin Gustavsson, Zhang Yang, Yoshiki Narimatsu, Daniel M Sørensen, Kato Mac Lafferty, Mieke Gouwy, Pedro E Marques and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
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  7. The role of glycosylation in clinical allergy and immunology.The Journal of allergy and clinical immunology · 2024
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

14 authors at 2 institutions in 2 countries.

Lisa VerhallenLaboratory for Molecular Pharmacology, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Panum Building 185. Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Jarkko J LackmanLaboratory for Molecular Pharmacology, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Panum Building 185. Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Rikke WendtLaboratory for Molecular Pharmacology, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Panum Building 185. Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Martin GustavssonLaboratory for Molecular Pharmacology, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Panum Building 185. Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Zhang YangCopenhagen Center for Glycomics, Department of Molecular and Cellular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Yoshiki NarimatsuCopenhagen Center for Glycomics, Department of Molecular and Cellular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Daniel M SørensenCopenhagen Center for Glycomics, Department of Molecular and Cellular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Kato Mac LaffertyLaboratory of Molecular Immunology, Department of Microbiology, Immunology and Transplantation, KU Leuven, Louvain, Belgium.
Mieke GouwyLaboratory of Molecular Immunology, Department of Microbiology, Immunology and Transplantation, KU Leuven, Louvain, Belgium.
Pedro E MarquesLaboratory of Molecular Immunology, Department of Microbiology, Immunology and Transplantation, KU Leuven, Louvain, Belgium.
Gertrud M HjortøLaboratory for Molecular Pharmacology, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Panum Building 185. Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Mette M RosenkildeLaboratory for Molecular Pharmacology, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Panum Building 185. Blegdamsvej 3B, 2200, Copenhagen, Denmark.
Paul ProostLaboratory of Molecular Immunology, Department of Microbiology, Immunology and Transplantation, KU Leuven, Louvain, Belgium.
Christoffer K GothLaboratory for Molecular Pharmacology, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, University of Copenhagen, Panum Building 185. Blegdamsvej 3B, 2200, Copenhagen, Denmark. goth@sund.ku.dk.ORCID http://orcid.org/0000-0002-5766-1411
University of Copenhagen · DKKU Leuven · BE

Funding

Fonds Wetenschappelijk Onderzoek G080818NH2020 Marie Skłodowska-Curie Actions ESA-D6247-MSCA-IF-2018Lundbeckfonden R322-2019-2171Onderzoeksraad, KU Leuven (C16/17/010)
6 · The paper itself

Abstract

Chemokine ligands and receptors regulate the directional migration of leukocytes. Post-translational modifications of chemokine receptors including O-glycosylation and tyrosine sulfation have been reported to regulate ligand binding and resulting signaling. Through in silico analyses, we determined potential conserved O-glycosylation and sulfation sites on human and murine CC chemokine receptors. Glyco-engineered CHO cell lines were used to measure the impact of O-glycosylation on CC chemokine receptor CCR5, while mutation of tyrosine residues and treatment with sodium chlorate were performed to determine the effect of tyrosine sulfation. Changing the glycosylation or tyrosine sulfation on CCR5 reduced the receptor signaling by the more positively charged CCL5 and CCL8 more profoundly compared to the less charged CCL3. The loss of negatively charged sialic acids resulted only in a minor effect on CCL3-induced signal transduction. The enzymes GalNAc-T1 and GalNAc-T11 were shown to be involved in the process of chemokine receptor O-glycosylation. These results indicate that O-glycosylation and tyrosine sulfation are involved in the fine-tuning and recognition of chemokine interactions with CCR5 and the resulting signaling.

Indexed as

ChemokinesSignal TransductionAnimalsCHO CellsCricetinaeHumansMiceProtein BindingProtein Processing, Post-TranslationalReceptors, CCR5TyrosineChemokinesReceptors, CCR5TyrosineChemokine receptorG protein-coupled receptorO-glycosylationTyrosine sulfation

Identifiers

PMID36729338
PMCPMC9894980
OpenAlexW4318934232

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.