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Fucosylation and Galactosylation of IgG Heavy Chains Differ in Acute and Remittent Phases of Juvenile Chronic Arthritis

Oligosaccharide structures are attached to nearly all membrane and serum proteins, and due to their sensitive biosynthetic machinery, change significantly in many diseases. We have analyzed glycosylation of IgG heavy chains in 34 juvenile chronic arthritis patients and 13 control individuals. IgG was purified from 0.7 ml of serum, separated by electrophoresis and transferred onto PVDF membrane. RCA, BSA II and UEA I lectins were used to measure galactose, N-acetyglucosamine and fucose, respectively. While there was no significant difference in average levels of galactose and N-acetylglucosamine, juvenile chronic arthritis patients had 2.4 times more fucose attached to IgG heavy chains than control individuals. Different picture emerged when patients were divided into acute and remittent groups. Patients in which juvenile chronic arthritis was currently active had significantly lower levels of galactose than the remittent group which had galactose levels comparable to control group. Fucose levels in both groups was significantly higher than in the control group. These results indicate that while degalactosylation is a good measure to detect activity of juvenile chronic arthritis, increased fucosylation is much better measure to identify the disease itself.

Fucosylation of IgG; Immunoglobulin G; Galactosylation of igG; Arthritis; IgG heavy chain structure

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