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
Rok vydání: 1995
Předmět:
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