An Integrated Glycosylation Signature of Rheumatoid Arthritis
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 c...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2023-07-01
|
| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/13/7/1106 |
| _version_ | 1797590104503484416 |
|---|---|
| author | Oleg A. Mayboroda Guinevere S. M. Lageveen-Kammeijer Manfred Wuhrer Radboud J. E. M. Dolhain |
| author_facet | Oleg A. Mayboroda Guinevere S. M. Lageveen-Kammeijer Manfred Wuhrer Radboud J. E. M. Dolhain |
| author_sort | Oleg A. Mayboroda |
| collection | DOAJ |
| description | 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 <i>N</i>-glycome (TSNG) may be similarly prominent, and useful in differentiating between the RA patients and controls, or as a proxy of the disease activity. In this study, we integrated and compared the RA glycosylation signatures of IgG, IgA and TSNG, all determined in the pregnancy-induced amelioration of rheumatoid arthritis (PARA) cohort. We assessed the association of the altered glycosylation patterns with the disease, autoantibody positivity and disease activity. Our analyses indicated a common, composite glycosylation signature of RA that was independent of the autoantibody status. |
| first_indexed | 2024-03-11T01:15:41Z |
| format | Article |
| id | doaj.art-79a86f34bd434b6e81166a0faf03f613 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-11T01:15:41Z |
| publishDate | 2023-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-79a86f34bd434b6e81166a0faf03f6132023-11-18T18:31:31ZengMDPI AGBiomolecules2218-273X2023-07-01137110610.3390/biom13071106An Integrated Glycosylation Signature of Rheumatoid ArthritisOleg A. Mayboroda0Guinevere S. M. Lageveen-Kammeijer1Manfred Wuhrer2Radboud J. E. M. Dolhain3Center for Proteomics and Metabolomics, Leiden University Medical Center, 2333 ZA Leiden, The NetherlandsCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2333 ZA Leiden, The NetherlandsCenter for Proteomics and Metabolomics, Leiden University Medical Center, 2333 ZA Leiden, The NetherlandsDepartment of Rheumatology, Erasmus Medical Center, 3015 CN Rotterdam, The NetherlandsRheumatoid 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 <i>N</i>-glycome (TSNG) may be similarly prominent, and useful in differentiating between the RA patients and controls, or as a proxy of the disease activity. In this study, we integrated and compared the RA glycosylation signatures of IgG, IgA and TSNG, all determined in the pregnancy-induced amelioration of rheumatoid arthritis (PARA) cohort. We assessed the association of the altered glycosylation patterns with the disease, autoantibody positivity and disease activity. Our analyses indicated a common, composite glycosylation signature of RA that was independent of the autoantibody status.https://www.mdpi.com/2218-273X/13/7/1106glycosylationrheumatoid arthritisantibody |
| spellingShingle | Oleg A. Mayboroda Guinevere S. M. Lageveen-Kammeijer Manfred Wuhrer Radboud J. E. M. Dolhain An Integrated Glycosylation Signature of Rheumatoid Arthritis Biomolecules glycosylation rheumatoid arthritis antibody |
| title | An Integrated Glycosylation Signature of Rheumatoid Arthritis |
| title_full | An Integrated Glycosylation Signature of Rheumatoid Arthritis |
| title_fullStr | An Integrated Glycosylation Signature of Rheumatoid Arthritis |
| title_full_unstemmed | An Integrated Glycosylation Signature of Rheumatoid Arthritis |
| title_short | An Integrated Glycosylation Signature of Rheumatoid Arthritis |
| title_sort | integrated glycosylation signature of rheumatoid arthritis |
| topic | glycosylation rheumatoid arthritis antibody |
| url | https://www.mdpi.com/2218-273X/13/7/1106 |
| work_keys_str_mv | AT olegamayboroda anintegratedglycosylationsignatureofrheumatoidarthritis AT guineveresmlageveenkammeijer anintegratedglycosylationsignatureofrheumatoidarthritis AT manfredwuhrer anintegratedglycosylationsignatureofrheumatoidarthritis AT radboudjemdolhain anintegratedglycosylationsignatureofrheumatoidarthritis AT olegamayboroda integratedglycosylationsignatureofrheumatoidarthritis AT guineveresmlageveenkammeijer integratedglycosylationsignatureofrheumatoidarthritis AT manfredwuhrer integratedglycosylationsignatureofrheumatoidarthritis AT radboudjemdolhain integratedglycosylationsignatureofrheumatoidarthritis |