Glycobiology (Oxford), 2017-09, Vol.27 (9), p.878-887
2017
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- Autor(en) / Beteiligte
- Titel
- Galectin-9 binds to O-glycans on protein disulfide isomerase
- Ist Teil von
- Glycobiology (Oxford), 2017-09, Vol.27 (9), p.878-887
- Ort / Verlag
- England: Oxford University Press
- Erscheinungsjahr
- 2017
- Quelle
- Oxford Journals 2020 Medicine
- Beschreibungen/Notizen
- Changes in the T cell surface redox environment regulate critical cell functions, such as cell migration, viral entry and cytokine production. Cell surface protein disulfide isomerase (PDI) contributes to the regulation of T cell surface redox status. Cell surface PDI can be released into the extracellular milieu or can be internalized by T cells. We have found that galectin-9, a soluble lectin expressed by T cells, endothelial cells and dendritic cells, binds to and retains PDI on the cell surface. While endogenous galectin-9 is not required for basal cell surface PDI expression, exogenous galectin-9 mediated retention of cell surface PDI shifted the disulfide/thiol equilibrium on the T cell surface. O-glycans on PDI are required for galectin-9 binding, and PDI recognition appears to be specific for galectin-9, as galectin-1 and galectin-3 do not bind PDI. Galectin-9 is widely expressed by immune and endothelial cells in inflamed tissues, suggesting that T cells would be exposed to abundant galectin-9, in cis and in trans, in infectious or autoimmune conditions.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0959-6658eISSN: 1460-2423DOI: 10.1093/glycob/cwx065Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5881768
- Format
- –
- Schlagworte
- Binding Sites, Cell Line, Cell Membrane - chemistry, Cell Membrane - drug effects, Cell Membrane - immunology, Cell Membrane - metabolism, Cloning, Molecular, Escherichia coli - genetics, Escherichia coli - metabolism, Galectin 1 - genetics, Galectin 1 - metabolism, Galectin 3 - genetics, Galectin 3 - metabolism, Galectins - antagonists & inhibitors, Galectins - genetics, Galectins - metabolism, Galectins - pharmacology, Gene Expression, Gene Expression Regulation, Glycosylation, Humans, Models, Molecular, Original, Oxidation-Reduction, Polysaccharides - chemistry, Polysaccharides - metabolism, Protein Binding, Protein Disulfide-Isomerases - chemistry, Protein Disulfide-Isomerases - genetics, Protein Disulfide-Isomerases - immunology, Protein Disulfide-Isomerases - metabolism, Protein Transport, Recombinant Fusion Proteins - genetics, Recombinant Fusion Proteins - metabolism, Recombinant Fusion Proteins - pharmacology, RNA, Small Interfering - genetics, RNA, Small Interfering - metabolism, Signal Transduction, T-Lymphocytes - chemistry, T-Lymphocytes - drug effects, T-Lymphocytes - immunology, T-Lymphocytes - metabolism