Induced AA Amyloid in Hamster: On the Amyloid Enhancing Factor and Protein AA-Cross Reacting Components of Intermediate Molecular Weight

  • Th. A. Niewold
  • P. C. J. Tooten
  • A. C. J. van Andel
  • E. Gruys


In the pathogenesis of AA-amyloidosis serum amyloid protein A (SAA) and the amyloid enhancing factor (AEF) are thought to play essential roles1. SAA is an acute phase reactant produced in hepatocytes stimulated by cytokines released by inflammatory cells2,3. SAA is present in the bloodstream mainly as a part of high density lipoprotein. of its structure, amino acid composition and DNA sequence in several species a great deal is known already. In contrast, it is not known where the AEF is produced or by what cells. Furthermore, its exact chemical nature is unknown. In the experimental murine model AEF has been described as a (glyco-) protein, because of its inactivation by proteolytic enzymes4,5. However, upto now the AEF resists every attempt to ascribe its activity to one specific protein5. Moreover, regarding the molecular size of the AEF, different data are given in the literature, depending on varying research groups and the source of the AEF, ranging from 10,000 to over 400,000 dalton4,5,6,7,8. The suggestion was made that AEF could be a small molecule that is easily complexing with itself or normal tissue components1,8.


Liver Homogenate Amyloid Fibril Mesocricetus Auratus Intermediate Molecular Weight Amyloid Enhance Factor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    R. Kisilevsky, A. D. Snow, L. Subrahmanyan, L. Boudreau, and R. Tan, What factors are necessary for the induction of AA amyloidosis?, in: Amyloidosis, edited by J. Marrink, and M. H. van Rijswijk, p301. Martinus Nijhoff Publishers, Dordrecht (1986)CrossRefGoogle Scholar
  2. 2.
    P. R. Hol, F. W. J. J. Snel, and E. Gruys, Hamster SAA-stimulating factor and lymphocyte activating factor are different factors, in: IVth International Symposium of Veterinary Laboratory Diagnosticians, edited by G. H. A. Borst et al, pl32. The Royal Netherlands Veterinary Association, Utrecht (1986)Google Scholar
  3. 3.
    K. P. W. J. McAdam, J. Li, J. Knowles, N. T. Foss, C. A. Dinarello, L. J. Rosenwasser, M. J. Selinger, M. M. Kaplan, R. Goodman, P. N. Herbert, L. L. Baussermann, and L. M. Nadler, The biology of SAA: identification of the inducer, in vitro synthesis, and heterogeneity demonstrated with monoclonal antibodies. Ann. N. Y. Acad. Sc. 389:127 (1982)CrossRefGoogle Scholar
  4. 4.
    M. A. Axelrad, and R. Kisilevsky, Biological characterization of amyloid enhancing factor, in: Amyloid and Amyloidosis, edited by G. G. Glenner, P. P. Costa, A. F. de Freitas, p 527. Excerpta Medica, Amsterdam (1980)Google Scholar
  5. 5.
    M. L. Baltz, D. Caspi, C. R. K. Hind, A. Feinstein, and M. B. Pepys, Isolation and characterization of amyloid enhancing factor (AEF), in: Amyloidosis, edited by G. G. Glenner, E. F. Ossermann, E. P. Benditt, E. Calkins, A. S. Cohen, D. Zucker-Franklin, pll5. Plenum Press, New York (1986)Google Scholar
  6. 6.
    P. R. Hol, A. C. J. van Andel, A. M. van Ederen, J. Draaijer, and E. Gruys, Amyloid enhancing factor in hamster, Br. J. Exp. Pathol. 66:689 (1985)Google Scholar
  7. 7.
    K. Kedar, I. Keizman, J. Bleiberg, and E. Sohar, Stimulation of murine amyloidosis by a dialyzable product from pre-treated donors, Br. J. Exp. Pathol. 56:244 (1975)Google Scholar
  8. 8.
    Th.A. Niewold, P. R. Hol, A. C. J. van Andel, E. T. G. Lutz, and E. Gruys, Enhancement of amyloid induction by amyloid fibril fragments in hamster, Lab. Invest. 56:544 (1987)Google Scholar
  9. 9.
    P. R. Hol, F. W. J. J. Snel, Th. A. Niewold, and E. Gruys, Amyloid-enhancing factor (AEF) in the pathogenesis of AA-amyloidosis in the hamster, Virchows Arch. B. 52:273 (1986)CrossRefGoogle Scholar
  10. 10.
    J. Varga, M. S. M. Flinn, T. Shirahama, O. G. Rodgers, and A. S. Cohen, The induction of accelerated murine amyloid with human splenic extract, Virchows Arch. B. 51:177 (1986)CrossRefGoogle Scholar
  11. 11.
    M. Pras, M. Schubert, D. Zucker-Franklin, A. Rimon, and E. C. Franklin, The characterization of soluble amyloid in water, J. Clin. Invest. 47:924 (1968)CrossRefGoogle Scholar
  12. 12.
    P. R. Hol, J. P. M. Langeveld, E. W. van Beuningen-Jansen, J. H. Veerkamp, and E. Gruys, A second component in bovine AA amyloid fibrils not identical with protein AA is essential for AA amyloid fibrillogenesis, Scand. J. Immunol. 20:53 (1984)CrossRefGoogle Scholar
  13. 13.
    G. Stokes, An improved Congo red method for amyloid, Med. Lab. Sci. 33:79 (1976)Google Scholar
  14. 14.
    N. Eriksen, and E. P. Benditt, Protein AA and associated proteins in type-AA amyloid substance, in: Amyloidosis, edited by G. G. Glenner, E. F. Ossermann, E. P. Benditt, E. Calkins, A. S. Cohen, and D. Zucker-Franklin, p3. Plenum Press, New York (1986)CrossRefGoogle Scholar
  15. 15.
    D. L. Scott, G. Marhaug, and G. Husby, Comparative studies of the high molecular weight amyloid fibril proteins and similar components from normal tissues, Clin. Exp. Immunol. 52: 693 (1983)Google Scholar
  16. 16.
    D. L. Scott, A. Husebekk, and G. Husby, Comparison of a reticulin extract of normal tissue and AA-amyloid fibrils. IRCS Med. Sci. 13:378 (1985)Google Scholar
  17. 17.
    A. C. J. van Andel, P. R. Hol, J. H. van der Maas, E. T. G. Lutz, H. Krabbendam, and E. Gruys, Reaggregation of bovine amyloid A fibril components to ß-pleated sheet fibrillar structures, in: Amyloidosis, edited by G. G. Glenner, E. F. Ossermann, E. P. Benditt, E. Calkins, A. S. Cohen, and D. Zucker-Franklin, p39. Plenum Press, New York (1986)CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Th. A. Niewold
    • 1
  • P. C. J. Tooten
    • 1
  • A. C. J. van Andel
    • 1
  • E. Gruys
    • 1
  1. 1.Department of Veterinary PathologyUniversity of UtrechtUtrechtThe Netherlands

Personalised recommendations