Polymorphism and expression of the galactosyltransferase‐associated protein kinase gene in normal individuals and galactosylation‐defective rheumatoid arthritis patients

Delves, Peter J.; Lund, Torben; Axford, John S.; Alavi-Sadrieh, A; Lydyard, Peter M.; Mackenzie, Lorna; Smith, Mark D.; Kidd, Vincent J.

doi:10.1002/art.1780331108

Cited by 24 publications

(8 citation statements)

References 37 publications

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“…GTase activity has been shown to be reduced in B lymphocytes of patients with rheumatoid arthritis (18), but this does not appear to be due to gross structural changes in either the GTase activator gene (19), the GTase gene itself, or to the presence of a soluble intracellular inhibitor (20).…”

Section: Introductionmentioning

confidence: 99%

Changes in normal glycosylation mechanisms in autoimmune rheumatic disease.

Axford¹,

Sumar²,

Alavi³

et al. 1992

J. Clin. Invest.

109

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To investigate potential mechanisms controlling protein glycosylation we have studied the interrelationship between lymphocytic galactosyltransferase (GTase) activity and serum agalactosylated immunoglobulin G levels (G(0)) in healthy individuals and patients with rheumatoid arthritis and non-autoimmune arthritis. In RA there was reduced GTase activity and increased G(0). A positive linear correlation between B and T cell GTase was found in all individuals. The relationship between GTase and G(0) was found to be positive and linear in the control population and negative and linear in the RA population. Sulphasalazine therapy maintained normal levels of GTase and caused a reduction in G(0) in the RA population. IgG anti-GTase antibodies (abs) were significantly increased in the RA population, whereas IgM anti-GTase abs were significantly decreased in both the RA and the non-autoimmune arthritis groups. These data describe a defect in RA lymphocytic

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Section: Introductionmentioning

confidence: 99%

Changes in normal glycosylation mechanisms in autoimmune rheumatic disease.

Axford¹,

Sumar²,

Alavi³

et al. 1992

J. Clin. Invest.

109

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“…The %G() was found to be higher in synovial fluid than in scrum, supporting the idea that agalactosyl IgG is produced in the joint in RA patients [10,11]. This change is associated with a down-regulation in B cell galactosyltransferase activity which in turn is controlled by the action of an associated protein kinasc [12]. Agalactosy!…”

Section: Introductionmentioning

confidence: 55%

Agalactosyl IgG in pristane-induced arthritis. Pregnancy affects the incidence and severity of arthritis and the glycosylation status of IgG

Thompson

Hitsumoto²,

Zhang

et al. 1992

Clinical and Experimental Immunology

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SUMMARYThe effecl of pregnancy on Ihe incidence and severity of pristane-induced arlhrilis was examined along with the glycosylation status of IgG during the ante-natal and post-partum periods. Il was found that pristane-induced arthritis is prevented by pregnancy. In addition, the levels of agalactosyl IgG fall during pregnancy but rise lo greater than normal wilhin a few days of parturition, before resetting towards Ihe norm shortly afterwards. Interestingly, the level of agalactosyl igG correlates with the severity of arthritis. As previously reported iL-6may bean important factor, not necessarily the only one, in the production of agalactosyl IgG. Here it is clearly demonstrated that llic kinetics of lL-6 activity posl-prislane injection parallels the kinetics of agalactosyl IgG production. In addition, the overshoot in agalactosyl IgG levels immediately post-partum coincides with a burst in IL-6 activity. It is considered that these changes in IgG glycoform levels, or the factors which control them, may be related to the mechanisms underlying prevention/remission of arthritis during pregnancy.

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“…In experiments using MRL mouse RA model, Axford et al reported a low Ga1T activity in peripheral lymphocytes [21]; and Jeddi et al a reduced expression of GaIT mRNA in spleen [22]. Taken together, the data suggest that it is more likely that the reduction in Ga1T activity in RA is due to an aberrant regulation of Ga1T mRNA expression through a variety of transcription factors and their phosphorylations by protein kinases such as GaIT-associated protein kinase [23]. The final proof must await the demonstration of a molecular mechanism that regulates the GaIT activity and its expression in RA patients.…”

Section: Discussionmentioning

confidence: 98%

Abnormal Glycosylation of IgG as a Clinical Parameter in Patients with Rheumatoid Arthritis: Its Constitutional Analysis by HPLC.

Yuka

Otsuka

Waguri

et al. 1998

J. Clin. Biochem. Nutr.

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SummaryTo determine the abnormal glycosylation patterns of IgG in patients with rheumatoid arthritis (RA), we analyzed these oligosaccharide profiles using a recently established high-performance liquid chromatography (HPLC) method. Oligosaccharides of IgG proteins purified from sera of RA patients were labeled with a fluorescent reagent, 2-aminopyridine. The oligosaccharide derivatives were separated into 12 peaks by HPLC, and compared with those of age-matched controls. Serum IgG from patients with RA (RA-IgG) contained a higher content of oligosaccharides with bisecting GlcNAc than normal IgG, which was accompanied by an increase in the glycosylation of the bisected oligosaccharides. The ratio of the glycosylation of bisected to nonbisected oligosaccharides correlated with RA disease activity as well as with its clinical markers. This ratio reflecting the balance of glycosylation between bisected and nonbisected oligosaccharides may be a useful clinical parameter to monitor RA activity.

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Polymorphism and expression of the galactosyltransferase‐associated protein kinase gene in normal individuals and galactosylation‐defective rheumatoid arthritis patients

Cited by 24 publications

References 37 publications

Changes in normal glycosylation mechanisms in autoimmune rheumatic disease.

Changes in normal glycosylation mechanisms in autoimmune rheumatic disease.

Agalactosyl IgG in pristane-induced arthritis. Pregnancy affects the incidence and severity of arthritis and the glycosylation status of IgG

Abnormal Glycosylation of IgG as a Clinical Parameter in Patients with Rheumatoid Arthritis: Its Constitutional Analysis by HPLC.

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