The Structure of Protein AA and its Correlation to the Tissue Distribution of Amyloid

  • Gunilla T. Westermark
  • Knut Sletten
  • Per Westermark


Amino acid sequence has been determined in the two major protein AA subspecies 859-8.1 and 798-4.6 derived from two patients with different histological patterns of amyloid deposition. The subspecies 859-8.1 contained 50 residues, corresponding to SAA residues 1–50 with pI 8.1, while subspecies 798-4.6 contained at least 79 residues, corresponding to positions 2-80 of SAA with pI 4.6. Both of these AA proteins were purified from patients with patterns of amyloid deposition different from the common one in which protein AA contains a subspecies with 76 residues. It is concluded that there is a correlation between the size of protein AA and the distribution of amyloid, but the reason for this correlation remains unknown.


Amyloid Deposition Amyloid Fibril Amino Acid Sequence Analysis Cyanogen Bromide Complete Amino Acid Sequence 
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  1. 1.
    P. Westermark, K. Sletten and M. Eriksson, Morphologic and chemical variation of the kidney lesions in amyloidosis secondary to rheumatoid arthritis, Lab. Invest. 41:427 (1979).Google Scholar
  2. 2.
    H.M. Falck, T. Törnroth and O. Wegelius, Predominantly vascular amyloid deposition in the kidney in patients with minimal or no proteinuria, Clin. Nephrol. 19:137 (1983).Google Scholar
  3. 3.
    P. Westermark, The heterogeneity of protein AA in secondary (reactive) systemic amyloidosis, Biochim. Biophys. Acta 701:19 (1982).CrossRefGoogle Scholar
  4. 4.
    P. Westermark and G.T. Nilsson, Vascular AA amyloidosis is characterized by special protein AA subspecies, in: “Amyloidosis”, G.G. Glenner, E.F. Osserman, E.P. Benditt, E. Calkins, A.S. Cohen, D. Zucker-Franklin, eds., Plenum, New York (1986).Google Scholar
  5. 5.
    G.T. Westermark, P. Westermark and K. Sletten, Amyloid fibril protein AA: characterization of different uncommon subspecies from a patient with rheumatoid arthritis, Lab. Invest. 57:57 (1987).Google Scholar
  6. 6.
    D.C. Parmelee, K. Titani, L.H. Ericsson, N. Eriksen, E.P. Benditt and K.A. Walsh, Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein, Biochemistry 21:3298 (1982).CrossRefGoogle Scholar
  7. 7.
    K. Sletten, G. Marhaug and G. Husby, The covalent structure of amyloid-related serum protein SAA from two patients with inflammatory disease, Hoppe-Zeyler’s Z. Physiol. Chem. 364:1039 (1983).CrossRefGoogle Scholar
  8. 8.
    K. Sletten, G. Husby and J.B. Natvig, The complete amino acid sequence of an amyloid fibril protein AA of unusual size (64 residues), Biochem. Biophys. Res. Commun. 69:19 (1976).CrossRefGoogle Scholar
  9. 9.
    M. Levin, E.C. Franklin, B. Frangione and M. Pras, The amino acid sequence of a major non-immunoglobulin component of some amyloid fibrils, J. Clin. Invest. 51:2773 (1972).CrossRefGoogle Scholar
  10. 10.
    D. Ein, S. Kimura, W.D. Terry, J. Magnotta and G.G. Glenner, Amino acid sequence of an amyloid fibril protein of unknown origin, J. Biol. Chem. 247:5653 (1972).Google Scholar
  11. 11.
    K. Sletten and G. Husby, The complete amino acid sequence of non-immunoglobulin amyloid fibril protein AS in rheumatoid arthritis, Eur. J. Biochem. 41:117 (1974).CrossRefGoogle Scholar
  12. 12.
    K. Möyner, K. Sletten, G. Husby and J.B. Natvig, An unusually large (83 amino acid residues) amyloid fibril protein AA from a patient with Waldenström’s macroglobulinaemia and amyloidosis, Scand. J. Immunol. 11:549 (1980).CrossRefGoogle Scholar
  13. 13.
    B. Kluve-Beckerman, G.L. Long and M.D. Benson, DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA), Biochem. Gen. 24:795 (1986).CrossRefGoogle Scholar
  14. 14.
    J. Sipe, H.R. Colten, G. Goldberger, M.D. Edge, B.F. Tack, A.S. Cohen and A.S. Whitehead, Human serum amyloid A (SAA): Biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA, Biochemistry 24:2931 (1985).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Gunilla T. Westermark
    • 1
    • 2
  • Knut Sletten
    • 1
    • 2
  • Per Westermark
    • 1
    • 2
  1. 1.Department of PathologyUniversity HospitalUppsalaSweden
  2. 2.Department of BiochemistryUniversity of OsloOsloNorway

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