Cited by 653Glycosylation and Glycoproteins ResearchGalectins and Cancer BiologyT-cell and B-cell Immunology

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Differential glycosylation of TH1, TH2 and TH-17 effector cells selectively regulates susceptibility to cell death

Toscano, Marta A, Bianco, Germán A, Ilarregui, Juan M, Croci, Diego O, Correale, Jorge, Hernandez, Joseph D, Zwirner, Norberto W, Poirier, Francoise, Riley, Eleanor M, Baum, Linda G, Rabinovich, Gabriel A·2007·Nature Immunology

DOI 10.1038/ni1482

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Abstract

Regulated glycosylation controls T cell processes, including activation, differentiation and homing by creating or masking ligands for endogenous lectins. Here we show that stimuli promoting T helper type 1 (TH1), TH2 or interleukin 17-producing T helper (TH-17) differentiation can differentially regulate the glycosylation pattern of T helper cells and modulate their susceptibility to galectin-1, a glycan-binding protein with anti-inflammatory activity. Although TH1- and TH-17-differentiated cells expressed the repertoire of cell surface glycans critical for galectin-1-induced cell death, TH2 cells were protected from galectin-1 through differential sialylation of cell surface glycoproteins. Consistent with those findings, galectin-1-deficient mice developed greater TH1 and TH-17 responses and enhanced susceptibility to autoimmune neuroinflammation. Our findings identify a molecular link among differential glycosylation of T helper cells, susceptibility to cell death and termination of the inflammatory response.

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Authors: Toscano, M. A., Bianco, G. A., Ilarregui, J. M., Croci, D. O., Correale, J., Hernandez, J. D., Zwirner, N. W., Poirier, F., Riley, E. M., Baum, L. G., & Rabinovich, G. A.
Affiliations: Universidad de Buenos Aires (AR)
Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
University of California, Los Angeles (US)
London School of Hygiene & Tropical Medicine (GB)
Corresponding author: Rabinovich, Gabriel A
ORCID: Toscano, Marta A
Ilarregui, Juan M
Croci, Diego O
Correale, Jorge
Hernandez, Joseph D
Zwirner, Norberto W
Riley, Eleanor M
Rabinovich, Gabriel A
Venue: Nature Immunology
Publisher: Springer Science and Business Media LLC
Published: 2007-06-24
Volume: 8
Issue: 8
Pages: 825-834
ISSN: 1529-2908 (ISSN-L)
1529-2916
DOI: 10.1038/ni1482
OpenAlex: W2041659209
Cited by: 653
References: 52
Citations by year: 2026: 22 · 2025: 28 · 2024: 22 · 2023: 22 · 2022: 46 · 2021: 31 · 2020: 35 · 2019: 20 · 2018: 36 · 2017: 25 · 2016: 33 · 2015: 36 · 2014: 37 · 2013: 34 · 2012: 40
FWCI: 18.17
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Immunology (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Funders: Wellcome Trust
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Immunology and Microbiology › Immunology › Galectins and Cancer Biology
Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Keywords: galectin-1, T helper cell differentiation, Th1 cells, Th2 cells, Th17 cells, sialylation, cell death, cell surface glycans, lectin binding, autoimmune neuroinflammation
MeSH terms: Animals, Cell Differentiation, Encephalomyelitis, Autoimmune, Experimental, Flow Cytometry, Glycosylation, T-Lymphocytes, Helper-Inducer, Humans, Inflammation, Membrane Glycoproteins, Polysaccharides, Immunoblotting, T-Lymphocyte Subsets, Apoptosis, Th1 Cells, Th2 Cells, Adoptive Transfer, In Situ Nick-End Labeling, Interleukin-17, Galectin 1, Mice

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Differential glycosylation of TH1, TH2 and TH-17 effector cells selectively regulates susceptibility to cell death

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