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. 1988 May 1;167(5):1731–1736. doi: 10.1084/jem.167.5.1731

Age-related galactosylation of the N-linked oligosaccharides of human serum IgG

PMCID: PMC2188930  PMID: 3367097

Abstract

In a study of 151 normal, healthy individuals of both sexes varying in age from 1-70 yr, it was found that the relative incidence of agalactosyl (with both outer arms terminating in N-acetylglucosamine) N- linked oligosaccharides on total serum IgG decreased from birth to a minimum (at 25 yr of age) and then increased with age. The relative incidence of digalactosyl structures varied inversely to this, and the relative incidence of monogalactosyl structures was constant. Galactosylation of the N-linked oligosaccharides of the human serum IgG of normal individuals is therefore an age-related molecular parameter. Several reports have suggested that rheumatoid arthritis is associated with a decreased galactosylation of serum IgG (3-5). The normal variation in galactosylation with age as described here allows a true assessment of disease-associated changes in this parameter, and raises the possibility that one of the lesions in rheumatoid arthritis is an accelerated aging of the immune system. In addition, heterogeneity within age groups may be due to intrinsic differences in genetic endowment, or may reflect the impact of extrinsic factors (8).

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Selected References

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  1. Ashford D., Dwek R. A., Welply J. K., Amatayakul S., Homans S. W., Lis H., Taylor G. N., Sharon N., Rademacher T. W. The beta 1----2-D-xylose and alpha 1----3-L-fucose substituted N-linked oligosaccharides from Erythrina cristagalli lectin. Isolation, characterisation and comparison with other legume lectins. Eur J Biochem. 1987 Jul 15;166(2):311–320. doi: 10.1111/j.1432-1033.1987.tb13516.x. [DOI] [PubMed] [Google Scholar]
  2. Cerami A. Accumulation of advanced glycosylation endproducts on proteins and nucleic acids: role in ageing. Prog Clin Biol Res. 1985;195:79–90. [PubMed] [Google Scholar]
  3. Doria G., D'Agostaro G., Poretti A. Age-dependent variations of antibody avidity. Immunology. 1978 Oct;35(4):601–611. [PMC free article] [PubMed] [Google Scholar]
  4. Duvall E., Wyllie A. H., Morris R. G. Macrophage recognition of cells undergoing programmed cell death (apoptosis). Immunology. 1985 Oct;56(2):351–358. [PMC free article] [PubMed] [Google Scholar]
  5. Goidl E. A., Innes J. B., Weksler M. E. Immunological studies of aging. II. Loss of IgG and high avidity plaque-forming cells and increased suppressor cell activity in aging mice. J Exp Med. 1976 Oct 1;144(4):1037–1048. doi: 10.1084/jem.144.4.1037. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hallgren H. M., Buckley C. E., 3rd, Gilbertsen V. A., Yunis E. J. Lymphocyte phytohemagglutinin responsiveness, immunoglobulins and autoantibodies in aging humans. J Immunol. 1973 Oct;111(4):1101–1107. [PubMed] [Google Scholar]
  7. Jalkanen S., Steere A. C., Fox R. I., Butcher E. C. A distinct endothelial cell recognition system that controls lymphocyte traffic into inflamed synovium. Science. 1986 Aug 1;233(4763):556–558. doi: 10.1126/science.3726548. [DOI] [PubMed] [Google Scholar]
  8. Leatherbarrow R. J., Rademacher T. W., Dwek R. A., Woof J. M., Clark A., Burton D. R., Richardson N., Feinstein A. Effector functions of a monoclonal aglycosylated mouse IgG2a: binding and activation of complement component C1 and interaction with human monocyte Fc receptor. Mol Immunol. 1985 Apr;22(4):407–415. doi: 10.1016/0161-5890(85)90125-7. [DOI] [PubMed] [Google Scholar]
  9. Parekh R. B., Dwek R. A., Sutton B. J., Fernandes D. L., Leung A., Stanworth D., Rademacher T. W., Mizuochi T., Taniguchi T., Matsuta K. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature. 1985 Aug 1;316(6027):452–457. doi: 10.1038/316452a0. [DOI] [PubMed] [Google Scholar]
  10. Parekh R. B., Tse A. G., Dwek R. A., Williams A. F., Rademacher T. W. Tissue-specific N-glycosylation, site-specific oligosaccharide patterns and lentil lectin recognition of rat Thy-1. EMBO J. 1987 May;6(5):1233–1244. doi: 10.1002/j.1460-2075.1987.tb02359.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Podskalny J. M., Rouiller D. G., Grunberger G., Baxter R. C., McElduff A., Gorden P. Glycosylation defects alter insulin but not insulin-like growth factor I binding to Chinese hamster ovary cells. J Biol Chem. 1986 Oct 25;261(30):14076–14081. [PubMed] [Google Scholar]
  12. Rademacher T. W., Homans S. W., Parekh R. B., Dwek R. A. Immunoglobulin G as a glycoprotein. Biochem Soc Symp. 1986;51:131–148. [PubMed] [Google Scholar]
  13. Rowe J. W., Kahn R. L. Human aging: usual and successful. Science. 1987 Jul 10;237(4811):143–149. doi: 10.1126/science.3299702. [DOI] [PubMed] [Google Scholar]
  14. Wareham K. A., Lyon M. F., Glenister P. H., Williams E. D. Age related reactivation of an X-linked gene. 1987 Jun 25-Jul 1Nature. 327(6124):725–727. doi: 10.1038/327725a0. [DOI] [PubMed] [Google Scholar]

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