Abstract
We previously reported a decrease in the content of galactose residues in oligosaccharide chains of serum IgG from patients with rheumatoid arthritis, which was presumed to affect the 3 dimensional structure of CH2 domain. In the present study, we prepared the galactose depleted IgG (agalacto IgG) and characterized its immunological activities. Significant reduction in Clq binding and Fc receptor binding was observed in agalacto IgG. However, IgM rheumatoid factor binding and protein A binding were the same as with intact IgG. Our results implied the biological function of the carbohydrate moiety of human IgG.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Arthritis, Rheumatoid / immunology*
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Carrier Proteins
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Complement Activation
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Galactose
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Humans
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Hyaluronan Receptors*
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Immunoglobulin G / immunology*
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Immunoglobulin Heavy Chains / immunology
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Membrane Glycoproteins*
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Mitochondrial Proteins
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Oligosaccharides*
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Receptors, Complement / immunology
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Receptors, Fc / immunology
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Rheumatoid Factor / immunology
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Staphylococcal Protein A / immunology
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Structure-Activity Relationship
Substances
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C1QBP protein, human
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Carrier Proteins
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Hyaluronan Receptors
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Immunoglobulin G
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Immunoglobulin Heavy Chains
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Membrane Glycoproteins
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Mitochondrial Proteins
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Oligosaccharides
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Receptors, Complement
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Receptors, Fc
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Staphylococcal Protein A
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complement 1q receptor
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Rheumatoid Factor
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Galactose