Skip to main content
PMC home page
Immunology logoLink to Immunology
. 1971 Jun;20(6):945–954.

Immunogenicity of amyloid*

E S Cathcart, Martha Skinner, A S Cohen
PMCID: PMC1455945  PMID: 4104285

Abstract

Human amyloid appears to contain two immunogenic components, the P (plasma) component and the F (fibril) component. Antisera to P component react with both autologous and homologous antigens by immunodiffusion and fluorescent antibody techniques; antisera to F component react with autologous antigens by immunodiffusion and fluorescent antibody techniques, but react with homologous antigens only by the fluorescent antibody method. Antisera to both P component and F component fail to react with non-amyloid human tissues as well as amyloid deposits in guinea-pig tissues. These results point to heterogeneity in the antigenic determinants of human amyloid and possibly greater inter-species heterogeneity of amyloid.

Full text

PDF
954

Images in this article

949FIG. 1
on p.949
950FIG. 2
on p.950
951FIG. 3
on p.951
951FIG. 4
on p.951
952FIG. 5
on p.952

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bladen H. A., Nylen M. U., Glenner G. G. The ultrastructure of human amyloid as revealed by the negative staining technique. J Ultrastruct Res. 1966 Mar;14(5):449–459. doi: 10.1016/s0022-5320(66)80075-8. [DOI] [PubMed] [Google Scholar]
  2. CATHCART E. S., COMERFORD F. R., COHEN A. S. IMMUNOLOGIC STUDIES ON A PROTEIN EXTRACTED FROM HUMAN SECONDARY AMYLOID. N Engl J Med. 1965 Jul 15;273:143–146. doi: 10.1056/NEJM196507152730306. [DOI] [PubMed] [Google Scholar]
  3. COHEN A. S., CALKINS E. Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature. 1959 Apr 25;183(4669):1202–1203. doi: 10.1038/1831202a0. [DOI] [PubMed] [Google Scholar]
  4. COHEN A. S., CALKINS E. THE ISOLATION OF AMYLOID FIBRILS AND A STUDY OF THE EFFECT OF COLLAGENASE AND HYALURONIDASE. J Cell Biol. 1964 Jun;21:481–486. doi: 10.1083/jcb.21.3.481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cathcart E. S., Cohen A. S. The relation between isolated human amyloid fibrils and human gamma-globulin and its subunits. J Immunol. 1966 Feb;96(2):239–244. [PubMed] [Google Scholar]
  6. Cathcart E. S., Wollheim F. A., Cohen A. S. Plasma protein constituents of amyloid fibrils. J Immunol. 1967 Aug;99(2):376–385. [PubMed] [Google Scholar]
  7. DIXON F. J., VAZQUEZ J. J. Immunohistochemical analysis of amyloid by the fluorescence technique. J Exp Med. 1956 Nov 1;104(5):727–736. doi: 10.1084/jem.104.5.727. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Franklin E. C., Pras M. Immunologic studies of water-soluble human amyloid fibrils. Comparative studies of eight amyloid preparations. J Exp Med. 1969 Oct 1;130(4):797–808. doi: 10.1084/jem.130.4.797. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. HOROWITZ R. E., STUYVESANT V. W., WIGMORE W., TATTER D. FIBRINOGEN AS A COMPONENT OF AMYLOID. Arch Pathol. 1965 Mar;79:238–244. [PubMed] [Google Scholar]
  10. LACHMANN P. J., MULLER-EBERHARD H. J., KUNKEL H. G., PARONETTO F. The localization of in vivo bound complement in tissue section. J Exp Med. 1962 Jan 1;115:63–82. doi: 10.1084/jem.115.1.63. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LETTERER E., CAESAR R., VOGT A. [Studies on electronoptic and immunomorphological structure of amyloid]. Dtsch Med Wochenschr. 1960 Oct 28;85:1909–1910. doi: 10.1055/s-0028-1112672. [DOI] [PubMed] [Google Scholar]
  12. MCDEVITT H. O., PETERS J. H., POLLARD L. W., HARTER J. G., COONS A. H. PURIFICATION AND ANALYSIS OF FLUORESCEIN-LABELED ANTISERA BY COLUMN CHROMATOGRAPHY. J Immunol. 1963 Apr;90:634–642. [PubMed] [Google Scholar]
  13. MELLORS R. C., ORTEGA L. G. Analytical pathology. III. New observations on the pathogenesis of glomerulonephritis, lipid nephrosis, periarteritis nodosa, and secondary amyloidosis in man. Am J Pathol. 1956 May-Jun;32(3):455–499. [PMC free article] [PubMed] [Google Scholar]
  14. OSSERMAN E. F., TAKATSUKI K., TALAL N. MULTIPLE MYELOMA I. THE PATHOGENESIS OF "AMYLOIDOSIS. Semin Hematol. 1964 Jan;1:3–85. [PubMed] [Google Scholar]
  15. OVARY Z. Immediate reactions in the skin of experimental animals provoked by antibody-antigen interaction. Prog Allergy. 1958;5:459–508. [PubMed] [Google Scholar]
  16. Pras M., Schubert M., Zucker-Franklin D., Rimon A., Franklin E. C. The characterization of soluble amyloid prepared in water. J Clin Invest. 1968 Apr;47(4):924–933. doi: 10.1172/JCI105784. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Pras M., Zucker-Franklin D., Rimon A., Franklin E. C. Physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations. J Exp Med. 1969 Oct 1;130(4):777–796. doi: 10.1084/jem.130.4.777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. RINDERKNECHT H. Ultra-rapid fluorescent labelling of proteins. Nature. 1962 Jan 13;193:167–168. doi: 10.1038/193167b0. [DOI] [PubMed] [Google Scholar]
  19. SCHEIDEGGER J. J. Une micro-méthode de l'immuno-electrophorèse. Int Arch Allergy Appl Immunol. 1955;7(2):103–110. [PubMed] [Google Scholar]
  20. Schultz R. T., Calkins E., Milgrom F., Witebsky E. Association of gamma globulin with amyloid. Am J Pathol. 1966 Jan;48(1):1–17. [PMC free article] [PubMed] [Google Scholar]
  21. Sellin D., Haferkamp O. Bence Jones Protein und Amyloid. Untersuchungen zum Zusammenhang von natürlicherweise aufretendem menschlichem Antikörper gegen Bence Jones Protein und von Bence Jones Protein mit Amyloid. Z Gesamte Exp Med. 1968;147(3):173–189. [PubMed] [Google Scholar]
  22. Sri Ram J., DeLellis R. A., Glenner G. G. Amyloid. IV. Is human amyloid immunogenic? Int Arch Allergy Appl Immunol. 1968;34(3):269–282. [PubMed] [Google Scholar]
  23. VOGT A., KOCHEM H. G. [Histo-serological studies with fluorescein-labeled anticomplement. Demonstration of complement-binding substances in amyloid]. Z Zellforsch Mikrosk Anat. 1960;52:640–652. [PubMed] [Google Scholar]

Articles from Immunology are provided here courtesy of British Society for Immunology

RESOURCES