Altered Cell Surface N-Glycosylation of Resting and Activated T Cells in Systemic Lupus Erythematosus

Autor: Ákos Hornung, Ágnes Czibula, László Kovács, Enikő Szabó, Márta Bocskai, Éva Monostori
Jazyk: angličtina
Rok vydání: 2019
Předmět:
Male
0301 basic medicine
T-Lymphocytes
Cellular differentiation
Cell
Gene Expression
Lymphocyte Activation
lcsh:Chemistry
chemistry.chemical_compound
0302 clinical medicine
N-linked glycosylation
systemic lupus erythematosus
Lectins
Lupus Erythematosus
Systemic
lcsh:QH301-705.5
Spectroscopy
lectin binding
medicine.diagnostic_test
biology
Chemistry
General Medicine
Middle Aged
Computer Science Applications
medicine.anatomical_structure
Galectin-1
Female
Adult
Glycosylation
glycosylation
Surface Properties
T cell
T cells
Neuraminidase
galectin 1
Article
Catalysis
Flow cytometry
Inorganic Chemistry
Young Adult
03 medical and health sciences
sialylation
Antigens
CD
glycosylation enzymes
medicine
Humans
Physical and Theoretical Chemistry
Molecular Biology
030203 arthritis & rheumatology
Organic Chemistry
Molecular biology
Sialyltransferases
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
biology.protein
Zdroj: International Journal of Molecular Sciences, Vol 20, Iss 18, p 4455 (2019)
International Journal of Molecular Sciences
Volume 20
Issue 18
ISSN: 1422-0067
Popis: Altered cell surface glycosylation in congenital and acquired diseases has been shown to affect cell differentiation and cellular responses to external signals. Hence, it may have an important role in immune regulation
however, T cell surface glycosylation has not been studied in systemic lupus erythematosus (SLE), a prototype of autoimmune diseases. Analysis of the glycosylation of T cells from patients suffering from SLE was performed by lectin-binding assay, flow cytometry, and quantitative real-time PCR. The results showed that resting SLE T cells presented an activated-like phenotype in terms of their glycosylation pattern. Additionally, activated SLE T cells bound significantly less galectin-1 (Gal-1), an important immunoregulatory lectin, while other lectins bound similarly to the controls. Differential lectin binding, specifically Gal-1, to SLE T cells was explained by the increased gene expression ratio of sialyltransferases and neuraminidase 1 (NEU1), particularly by elevated ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1)/NEU1 and ST3 beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6)/NEU1 ratios. These findings indicated an increased terminal sialylation. Indeed, neuraminidase treatment of cells resulted in the increase of Gal-1 binding. Altered T cell surface glycosylation may predispose the cells to resistance to the immunoregulatory effects of Gal-1, and may thus contribute to the pathomechanism of SLE.
Databáze: OpenAIRE
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