The Role of B Cell and T Cell Glycosylation in Systemic Lupus Erythematosus
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Published:2023-01-03
Issue:1
Volume:24
Page:863
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ISSN:1422-0067
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Container-title:International Journal of Molecular Sciences
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language:en
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Short-container-title:IJMS
Author:
Ramos-Martínez IvanORCID, Ramos-Martínez EdgarORCID, Cerbón Marco, Pérez-Torres ArmandoORCID, Pérez-Campos Mayoral LauraORCID, Hernández-Huerta María Teresa, Martínez-Cruz Margarito, Pérez-Santiago Alma Dolores, Sánchez-Medina Marco Antonio, García-Montalvo Iván AntonioORCID, Zenteno EdgarORCID, Matias-Cervantes Carlos AlbertoORCID, Ojeda-Meixueiro Víctor, Pérez-Campos EduardoORCID
Abstract
Glycosylation is a post-translational modification that affects the stability, structure, antigenicity and charge of proteins. In the immune system, glycosylation is involved in the regulation of ligand–receptor interactions, such as in B-cell and T-cell activating receptors. Alterations in glycosylation have been described in several autoimmune diseases, such as systemic lupus erythematosus (SLE), in which alterations have been found mainly in the glycosylation of B lymphocytes, T lymphocytes and immunoglobulins. In immunoglobulin G of lupus patients, a decrease in galactosylation, sialylation, and nucleotide fucose, as well as an increase in the N-acetylglucosamine bisector, are observed. These changes in glycoisolation affect the interactions of immunoglobulins with Fc receptors and are associated with pericarditis, proteinuria, nephritis, and the presence of antinuclear antibodies. In T cells, alterations have been described in the glycosylation of receptors involved in activation, such as the T cell receptor; these changes affect the affinity with their ligands and modulate the binding to endogenous lectins such as galectins. In T cells from lupus patients, a decrease in galectin 1 binding is observed, which could favor activation and reduce apoptosis. Furthermore, these alterations in glycosylation correlate with disease activity and clinical manifestations, and thus have potential use as biomarkers. In this review, we summarize findings on glycosylation alterations in SLE and how they relate to immune system defects and their clinical manifestations.
Subject
Inorganic Chemistry,Organic Chemistry,Physical and Theoretical Chemistry,Computer Science Applications,Spectroscopy,Molecular Biology,General Medicine,Catalysis
Reference103 articles.
1. Varki, A., Cummings, R., Esko, J., Stanley, P., Hart, G., Aebi, M., Mohnen, D., Kinoshita, T., Packer, N., and Prestegard, J. (2022). Essentials of Glycobiology, Cold Spring Harbor Laboratory Press. 2. Varki, A., Cummings, R.D., Esko, J.D., Freeze, H.H., Stanley, P., Bertozzi, C.R., Hart, G.W., and Etzler, M.E. (2022). Essentials of Glycobiology, Cold Spring Harbor. 3. The role of the carbohydrates in plasmatic membrane;Sprovieri;Physiol. Res.,2018 4. Glycans in the immune system and The Altered Glycan Theory of Autoimmunity: A critical review;Maverakis;J. Autoimmun.,2015 5. N-glycosylation bidirectionally extends the boundaries of thymocyte positive selection by decoupling Lck from Ca2+ signaling;Zhou;Nat. Immunol.,2014
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