Replacement of SAA from the HDL-SAA Complex by APO AI and APO AII: HDL has Higher Binding Capacity for SAA than for AA

  • Anne Husebekk
  • Bjørn Skogen
  • Gunnar Husby


When purified apo-AI or apo-AII was added to human SAA-HDL in vitro, some of the apoproteins were incorporated in the complexes. On the other hand, SAA was displaced from HDL. Apo A-II had a higher SAA “displacing activity” than apo-AI. We also observed that SAA had a higher binding affinity for HDL than protein AA. Essentially the same was observed when human apoprotein AII was added to mouse SAA-HDL. Our results also indicate that mouse SAA2 has lower affinity for HDL than SAA1.


High Density Lipoprotein Amyloid Fibril Serum Amyloid Secondary Amyloidosis Small Intestinal Wall 
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.
    D. C. Parmelee, K. Titani, L. H, Ericsson, N. Eriksen, E. F. Benditt and K. A. Walsh, Amino acid sequence of amyloid-related apoprotein (apo SAA1 ) from human high-density lipoprotein, Biochemistry, 21:3298 (1982).CrossRefGoogle Scholar
  2. 2.
    M. J. Selinger, K. F. W. J. McAdam, M. M. Kaplan, J. D. Sipe, S. N. Vogel and D. L. Rosenstreich, Monokine-induced synthesis of serum amyloid A protein by hepatocytes, Nature, 285:498 (1980).CrossRefGoogle Scholar
  3. 3.
    E. P. Benditt and N. Eriksen, Amyloid protein SAA is associ ated with high density lipoprotein from human serurn, Proc. Natn. Acad. Sci. (USA), 74:4025 (1977).CrossRefGoogle Scholar
  4. 4.
    A. Husebekk, B. Skogen, G. Husby and G. Marhaug, Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo, Scand. J. Immunol., 21:283 (1985).CrossRefGoogle Scholar
  5. 5.
    M. Levin, E. C. Franklin, B. Frangione and M. Pras, The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils, J. Clin. Invest., 51:2773 (1972).CrossRefGoogle Scholar
  6. 6.
    A. Husebekk, B. Skogen and G. Husby, Characterization of amyloid proteins AA and SAA as apolipoproteins of high density lipoprotein (HDL). Displacement of SAA from the HDL-SAA complex by apo AI and apo AII, Scand. J. Immunol., 25:375 (1987).CrossRefGoogle Scholar
  7. 7.
    G. A. Coetzee, A. F. Strachan, D. R. van der Westhuysen, H. C. Hoppe, M. S. Jeenah and F. C. de Beer, Serum amyloid A-contairiing human high density lipoprotein J. Density, size, and apolipoprotein composition, J. Biol. Chenu, 261:9644 (1986).Google Scholar
  8. 8.
    G. Marhaug, Three assays for the characterization and quantitation of human serum amyloid A, Scand. J. Immunol., 18:329 (1983).CrossRefGoogle Scholar
  9. 9.
    P. A. Lagocki and A. M. Scanu, In vitro modulation of the apolipoprotein composition of high density lipoprotein, J. Biol. Chern., 255:3701 (1980).Google Scholar
  10. 10.
    R. L. Meek, J. S. Hoffman and E. P. Benditt, Arnyloidogenesis. One serum amyloid A isotype is selectively removed from the circulation, J. Exp. Med., 163:499 (1986).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Anne Husebekk
    • 1
  • Bjørn Skogen
    • 1
  • Gunnar Husby
    • 1
    • 2
  1. 1.Departments of ImmunologyUniversity Hospital of TromsøTromsøNorway
  2. 2.Departments of RheumatologyUniversity Hospital of TromsøTromsøNorway

Personalised recommendations