An Integrated Glycosylation Signature of Rheumatoid Arthritis.


Journal

Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414

Informations de publication

Date de publication:
12 07 2023
Historique:
received: 24 05 2023
revised: 27 06 2023
accepted: 29 06 2023
medline: 31 7 2023
pubmed: 29 7 2023
entrez: 29 7 2023
Statut: epublish

Résumé

Rheumatoid arthritis (RA) Is a highly prevalent autoimmune disease that affects the joints but also various other organs. The disease is characterized by autoantibodies that are often already observed pre-disease. Since the 1980s, it has been known that antibody glycosylation is different in RA as compared to control individuals. While the literature on glycosylation changes in RA is dominated by reports on serum or plasma immunoglobulin G (IgG), our recent studies have indicated that the glycosylation changes observed for immunoglobulin A (IgA) and total serum

Identifiants

pubmed: 37509142
pii: biom13071106
doi: 10.3390/biom13071106
pmc: PMC10377307
pii:
doi:

Substances chimiques

Autoantibodies 0
Immunoglobulin G 0
Immunoglobulin A 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Références

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Auteurs

Oleg A Mayboroda (OA)

Center for Proteomics and Metabolomics, Leiden University Medical Center, 2333 ZA Leiden, The Netherlands.

Guinevere S M Lageveen-Kammeijer (GSM)

Center for Proteomics and Metabolomics, Leiden University Medical Center, 2333 ZA Leiden, The Netherlands.
Analytical Biochemistry, University of Groningen, 9700 RB Groningen, The Netherlands.

Manfred Wuhrer (M)

Center for Proteomics and Metabolomics, Leiden University Medical Center, 2333 ZA Leiden, The Netherlands.

Radboud J E M Dolhain (RJEM)

Department of Rheumatology, Erasmus Medical Center, 3015 CN Rotterdam, The Netherlands.

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Classifications MeSH