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Reduced sialyl-Lewis(x) on salivary MUC7 from patients with burning mouth syndrome

Journal article
Authors Shikha Acharya
Chunsheng Jin
Johan Bylund
Q. J. Shen
M. Kamali-Moghaddam
Mats Jontell
Anette Carlén
Niclas G. Karlsson
Published in Molecular Omics
Volume 15
Issue 5
Pages 331-339
Publication year 2019
Published at Institute of Odontology
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 331-339
Language en
Links dx.doi.org/10.1039/c9mo00061e
Keywords transcriptional regulation, blood-group, cell, oligosaccharides, glycosylation, association, fractalkine, expression, features, sp1, Biochemistry & Molecular Biology
Subject categories Clinical Medicine

Abstract

We analysed and compared MUC7 O-glycosylation and inflammatory biomarkers in saliva from female patients with burning mouth syndrome (BMS) and gender/age-matched controls. Oligosaccharides from salivary MUC7 from BMS and controls were released. Inflammatory mediators were measured by multiplex proximity extension assay. Presence of sialyl-Lewis(x) (Si-Le(x)) epitope on MUC7 was confirmed using Western blot. MUC7 O-glycans and measured inflammatory biomarkers were found to be similar between BMS and controls. However, oligosaccharides sialyl-Lewis(x) (Si-Le(x)) was found to be reduced in samples from BMS patients. Positive correlation (combined patients and controls) was found between levels of C-C motif chemokine 19 (CCL-19) and the amount of core-2 oligosaccharides on MUC7 as well as fractalkine (CX3CL1) and level of sialylation. Patients with BMS were shown to represent a heterogeneous group in terms of inflammatory biomarkers. This indicates that BMS patients could be further stratified on the basis of low-level inflammation. The results furthermore indicate that reduced sialylation of MUC7, particularly Si-Le(x), may be an important feature in patients with BMS. However, the functional aspects and potential involvement in immune regulation of Si-Le(x) remains unclear. Our data suggests a chemokine driven alteration of MUC7 glycosylation.

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