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The heterogeneity of the glycosylation of alpha-1-acid glycoprotein between the sera and synovial fluid in rheumatoid arthritis

Smith, Kevin D. and Pollacchi, Aileen and Field, Max and Watson, John (2002) The heterogeneity of the glycosylation of alpha-1-acid glycoprotein between the sera and synovial fluid in rheumatoid arthritis. Biomedical Chromatography, 16 (4). pp. 261-266. ISSN 0269-3879

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Abstract

Alpha-1-acid glycoprotein (AGP) is a plasma glycoprotein produced by the liver that undergoes increased production and altered glycosylation in several physiological and pathological conditions including rheumatoid arthritis. To date, although present in the synovial fluid of rheumatoid arthritis patients, there has been no evidence for the separate extra-hepatic production of AGP. This study indicates that there could be a localized production of AGP in rheumatoid synovial fluid by demonstrating that the glycosylation patterns of AGP differed between the serum and synovial fluid in the same rheumatoid patient. Serum AGP was largely composed of fucosylated tri- and tetra-antennary oligosaccharide chains while the synovial fluid contained mainly bi-antennary chains that were fucosylated to a lesser extent. This structural heterogeneity of glycosylation resulted in functional diversity; serum but not synovial AGP is able to inhibit binding to the cell adhesion molecule E-selectin through expression of antigen sialyl Lewis X.

Item type: Article
ID code: 23427
Keywords: epithelial cells, microheterogeneity, modulation, expression, binding, disease, Pharmacy and materia medica, Biochemistry, Drug Discovery, Molecular Biology, Analytical Chemistry, Pharmacology, Clinical Biochemistry
Subjects: Medicine > Pharmacy and materia medica
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Faculty of Education > Curricular Studies
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    Depositing user: Strathprints Administrator
    Date Deposited: 08 Jul 2010 16:57
    Last modified: 05 Sep 2014 04:36
    URI: http://strathprints.strath.ac.uk/id/eprint/23427

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