Abstract
Improved technology has provided researchers with two automated carbohydrate analysers. One is based on hydrazinolysis and subsequent fractionation of labelled and oligosaccharides (Oxford Glycosystems) and the other is based on high pH anion exchange, coupled with electrochemical detection (Dionex Carbohydrate System), which allows determination of the monosaccharide composition as well as mapping of the oligosaccharide moieties.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abstract Supplement. 2nd Jenner International Glycoimmunology Meeting Ann Rheum Dis. 1992; 1269–1285.
Filley E, Andreoli A, Steele J et al. A transient rise in agalactosyl IgG correlating with free IL-2 receptors during episodes of erythema nodosum leprosum. Clin Exp Immunol 1989; 76: 343–347
Sumar N, Bodman KB, Rademacher TW, Dwek RA, Williams P, Parekh RB, Edge J, Rook GAW, Isenberg DA, Hay FC & Roitt IM. Analysis of glycosylation changes in IgG using lectins. J Imm Meth 1990; 131: 127–136.
Tsuchiya N, Endo T, Shiota M, Kochibe N, Ito K, and Kobata A. Distribution of glycosylation abnormality among serum IgG subclasses from patients with rheumatoid arthritis. Clin. Immunol & Immunopath 1994; 78(1): 47–50
De Graaf TW, Van der Stelt ME, Anbergen MG & Van Dijk W. Inflammation-induced expression of sialyl Lewis X - containing glycan structures on α1-acid glycoprotein (orosomucoid) in human sera. J Exp.Med 1993;177:657–666.
Van Reeth C, Le Moel G, Lasne T, Revenant MC, Agneray J, Kahn MF & Bourgeois P. Serum ferritin and isoferritins are tools for diagnosis of active Adult Still’s Disease. J Rheum 1994; 21(5): 890–895.
Martin K, Davies EG & Axford JS. The use of fluorophore assisted carbohydrate electrophoresis to determine immunoglobulin G associated carbohydrate profiles in rheumatoid arthritis and juvenile chronic arthritis. Clin Exp Rheumatol 1994; 12/5–10 (S-119).
Nose M & Wigzell H. Biological significance of carbohydrate chains on monoclonal antibodies. Proc Natl Acad Sci, USA 1983; 80: 6632–6636.
Lund J, Tanaka T, Takahashi N, Sarmay G, Arata Y & Jefferis R. A protein structural change in aglycosylated IgG3 correlates with a loss of huFcγRII and FcγRIII binding and/or activation. Molec Immunol 1990; 27: 1145–1154.
Furukawa K, and Kobata A. IgG galactosylation-its biological significance and pathology. Mol Immunol 1991; 28: 1333
Wright A, Tao M, Kabat EA & Morrison SL. Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure. The EMBO J 1991; 10: 2717–2723.
Bond A, Jones MG & Hay FC. Human IgG preparations isolated by ion-exchange or protein G affinity chromatography differ in their glycosylation profiles. J Imm Meth 1993; 166: 27–33.
Youinou P, Pennec Y-L, Casburn-Budd R, Dueymes M, Letoux G & Lamour A. Galactose terminating oligosaccharides of IgG in patients with Primary Sjogren’s Syndrome. J Autoimmunity 1992; 5: 393–400.
Axford JS, Alavi A, Bond A & Hay FC. Differential B lymphocyte galactosyltransferase activity in the MRL mouse model of rheumatoid arthritis. Autoimmunity 1994; 17: 157–163.
Natsuka S, Gersten KM, Zenita K, Kannagi R & Lowe JB. Molecular cloning of a cDNA encoding a novel human leukocyte α1,3 fucosyltransferase capable of synthesizing the Sialyl Lewisx determinant. J Biological Chem 1994; 269: 16789–16794.
Bond A, Alavi A, Hay FC, Youinou P & Axford JS. Immunoglobulin G glycosylation changes occur in rheumatoid arthritis and primary Sjögren’s syndrome, but due to different mechanisms. Arth Rheum 1993; 36(9): D66.
Nishiura T, Fujii S, Kanayama Y, Nishikawa A, Tomiyama Y, Iida M, Karasuno T, Nakao H, Yonesawa T, Taniguchi N & Tarui S. Carbohydrate analysis of immunoglobulin G myeloma proteins by lectin and high performance liquid chromatography: Role of glycosyltransferases in the structures. Cancer Research 1990; 50: 5345–5350
Tsuchiya N, Endo T, Matsuta K, Yoshinoya S, Aikawa T, Kosuge E, Takeuchi F, Miyamoto T & Kobata A. Effects of galactose depletion from oligosaccharide chains on immunological activities of human IgG. J Rheum 1989; 16(3); 285–290.
Newkirk K, Rauch J. Binding of human monoclonal IgG rheumatoid factor to Fc is influenced by carbohydrate. J Rheum 1993; 20(5): 776–780.
Soltys AJ, Hay FC, Bond A, Axford JS, Jones MG, Randen I, Thompson K, & Natvig J. The binding of synovial tissue-derived human monoclonal immunoglobulin M rheumatoid factor to immunoglobulin G preparations of differing galactose content. Scand J Immunol 1994; 40: 135–143.
Bond A, Cooke A & Hay FC. Glycosylation of IgG, immune complex and IgG subclasses in the MRL-lpr/lpr mouse model of rheumatoid arthritis. Eur J Immunol 1990; 20: 2229–2233.
Nag B, Passmore D, Kendrick T, Bhayani H & Sharma SD. N-linked oligosaccharides of murine major histocompatibility complex class II molecule. Role in antigenic peptide binding, T cell recognition and clonal non-responsiveness. J Biol Chem 1992; 267: 22624–22629.
Brenner MB, McLean J, Scheft H et al. Two forms of the T cell receptor and protein found on peripheral blood cytotoxic T lymphocytes. Nature 1987; 325: 689–694.
Hanasaki K, Varki A, Stamenkovic I, Bevilocqua P. Cytokine-induced β-galactoside α-2,6 Sialyltransferase in human endothelial cells mediates α2,6-sialylationn of adhesion molecules and CD22 ligands. J Biol Chem 1994; 269(14): 10637–10643.
Thompson S, Dargan E, Griffiths ID, Kelly CA & Turner GA. The glycosylation of haptoglobin in rheumatoid arthritis. Clin Chim Acta 220 1993; 107–114.
Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993; 3(2): 97–130.
Axford JS, Sumar N, Alavi A, Isenberg DA, Young A, Bodman KB & Roitt IM. Changes in normal glycosylation mechanisms in autoimmune rheumatic disease. J Clin Invest 1992; 89: 1021–1031.
Van Dijk W, Turner GA & Mackiewicz A. Changes in glycosylation of acute phase proteins in health and disease: Occurrence, regulation and function. Glycosylation & Dis 1994; 1: 5–14.
Fernandes C, Alarcon-Riguelme ME, Abedi-Valugerdi M, Svenzemazk G & Cortes V. Polyreactivity could be the result of differential glycosylation of immunoglobulins. 12th European Immunology Meeting, 14–17 June 1994, Barcelona.
Sumar N, Colaco CB, Bodman KB, Parekh R, Williams P, Dwek R, Rademacher T, Isenberg DA, Soltys AJ, Hay FC & Roitt IM. Abnormalities in the glycosylation of IgG in spouses of patients with rheumatoid arthritis. A Family Study. J of Autoimmunity 1991; 4: 907–914.
Tomana M, Schrohenloher RE, Bennett PH, del Puente A & Koopman WJ. Occurrence of deficient galactosylation of serum IgG prior to the onset of rheumatoid arthritis. Rheumatol Int 1994; 13: 217–220.
Young A, Sumar N, Bodman KB, Goyal S, Sinclair H, Roitt IM & Isenberg DA. Agalactosyl IgG: An aid to differential diagnosis in early synovitis. Arthritis Rheum 1991; 34(11): 1425–1429.
Van Zeben D, Rook GAW, Hazes JMW, Zwinderman AH, Zhang Y, Ghelani S, Rademacher TW & Breedveld FC. Early agalctosylation of IgG is associated with a more progressive disease course in patients with rheumatoid arthritis: Results of a follow-up study. Br J Rheum 1994; 33: 36–43.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
Axford, J.S., Alavi, A. (1995). An Introduction to Glycosylation and Rheumatic Disease. In: Alavi, A., Axford, J.S. (eds) Glycoimmunology. Advances in Experimental Medicine and Biology, vol 376. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1885-3_17
Download citation
DOI: https://doi.org/10.1007/978-1-4615-1885-3_17
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5768-1
Online ISBN: 978-1-4615-1885-3
eBook Packages: Springer Book Archive