Affiliations: [a] NIBRT Complete Process and Product Characterisation Group, National Institute for Bioprocessing, Research and Training, Dublin, Ireland | [b] Veterinary Sciences Centre, University College Dublin, Dublin, Ireland | [c] Conway Institute of Biomolecular and Biomedical Science, University College Dublin, Dublin, Ireland | Biochemistry and Bio-related Chemistry Branch Pharmacology, Physiology, and Biological Chemistry Division NIGMS, NIH
Correspondence:
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Corresponding author: Pauline M. Rudd, Conway Institute of Biomolecular and Biomedical Science, University College Dublin, Belfield, Dublin 4, Ireland. Tel.: +353 12158 142; Fax: +353 12158 116; E-mail: pauline.rudd@nibrt.ie.
Abstract: Changes in serum protein glycosylation play an important role in inflammatory arthritis. Altered galactosylation of immunoglobulin G (IgG) in rheumatoid arthritis attracts special attention due to the devastating nature of the disease. Studying glycosylation changes of serum proteins has been recognized as a potential strategy to provide added value regarding diagnostics, aetiopathology and therapy of inflammatory arthritic diseases. Key questions, which are approached in these fields of research, are whether or not glycosylation can be used as a complementary pre-clinical and clinical marker for disease differentiation, diagnosis, the prediction of disease course and severity as well as for the evaluation of disease therapies. These studies mainly focus on TNF antagonists, which present a new and promising way of treating inflammatory arthritis. The recent availability of new high-throughput glycoanalytical tools enables a more profound and efficient investigation in large patient cohorts and helps to gain new insights in the complex mechanism of the underlying disease pathways.
Keywords: Inflammatory arthritis, serum protein glycosylation, diagnostics, aetiopathology, therapy
