Evaluation of ?1,4-galactosyltransferase in rheumatoid arthritis and its role in the glycosylation network associated with this disease
Autor: | John S. Axford, Azita Alavi |
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Rok vydání: | 1995 |
Předmět: |
Glycosylation
Arthritis Disease Biochemistry Arthritis Rheumatoid Pathogenesis chemistry.chemical_compound Immune system Reference Values N-Acetyllactosamine Synthase medicine Humans Molecular Biology Galactosyltransferase biology Chemistry Cell Biology medicine.disease Isoenzymes carbohydrates (lipids) Evaluation Studies as Topic Rheumatoid arthritis Immunology biology.protein Regression Analysis Antibody |
Zdroj: | Glycoconjugate Journal. 12:206-210 |
ISSN: | 1573-4986 0282-0080 |
DOI: | 10.1007/bf00731321 |
Popis: | Evidence indicating an important link between glycosylation changes and autoimmune rheumatic disease is presented. Attention is especially focused on the interrelationship between reduced galactosylation of the oligosaccharides of IgG, auto-sensitization which is thought to be of central importance in the pathogenesis of rheumatoid arthritis (RA), and the enzyme beta 1,4-galactosyltransferase (GTase) that catalyses the addition of galactose to the oligosaccharide chains on this molecule. Data are presented to indicate that GTase undergoes a variety of normal and disease associated changes. These variations are believed to contribute to the pathological processes in rheumatoid disease, and a hypothesis is suggested, whereby disease is associated with the dysregulation of an integrated glycosylation network, comprising IgG galactosylation, lymphocytic GTase and anti-GTase antibodies, that is a component of the normal immune system. |
Databáze: | OpenAIRE |
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