Structural changes in the N-linked sugar chains of serum immunoglobulin G of HTLV-I transgenic mice.
IgGs were purified from the sera of HTLV-I transgenic and nontransgenic mice. Comparative studies of the N-linked sugar chains released by hydrazinolysis revealed that their structures of transgenic IgG are quite different from those of nontransgenic IgG. Although both IgGs contained biantennary complex-type oligosaccharides, transgenic IgG had more agalactosylated forms (45%) than those from nontransgenic IgG (28%), just as was found in patients with rheumatoid arthritis (RA). Since these transgenic mice express arthritis similar to RA, it will be a useful model to investigate the relationship between the galactosylation of IgG and the development of RA.
Department of Biochemistry, University of Tokyo, Japan.
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Endo
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Iwakura
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Kobata
D000818:Animals; D002240:Carbohydrate Sequence; D002850:Chromatography, Gel; D015752:Genes, env; D016355:Genes, pX; D015368:Human T-lymphotropic virus 1 / Q000235:genetics* / Q000276:immunology*; D007074:Immunoglobulin G / Q000097:blood* / Q000737:chemistry; D051379:Mice; D008822:Mice, Transgenic; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry* / Q000302:isolation & purification
D007074:Immunoglobulin G; D009844:Oligosaccharides