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Amyloid Fibril Protein in Finnish Hereditary Amyloidosis

  • C. P. J. Maury
  • A-M. Teppo
  • A-L. Kariniemi
  • A. H. Koeppen
Chapter

Abstract

Immunocytochemical methods were used to study the nature of the amyloid deposits in the Finnish form of familial amyloidosis, FAP type IV. Commercial antisera to human plasma transthyretin (prealbumin) did not stain the amyloid deposits, but positive staining was obtained with antibodies raised against transthyretin-related amyloid fibril whole protein. The amyloid deposits also stained with antiserum to serum amyloid P component, but did not stain with antisera to retinol-binding protein, amyloid A protein, γ-trace protein, β2-microglobulin, or immunoglobulin light chains. The serum level of serum transthyretin was significantly decreased in the Finnish FAP patients. The results suggest that the amyloid fibril protein in Finnish hereditary amyloidosis is related to transthyretin.

Keywords

Amyloid Deposit Amyloid Fibril Cerebral Amyloid Angiopathy Corneal Dystrophy Immunoglobulin Light Chain 
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.

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References

  1. 1.
    J. Meretoja, Familial systemic paramyloidosis with lattice dystrophy of the cornea, progressive cranial neuropathy, skin changes and various internal symptoms. A previously unrecongnized heritable syndrome, Ann. Clin. Res. 1: 314 (1969).Google Scholar
  2. 2.
    P. P. Costa, A. S. Figuieira, and F. R. Bravo, Amyloid fibril protein related to prealbumin in familial amyloidotic polyneuropathy, Proc. Natl. Acad. Sci. USA 75: 4499 (1978).CrossRefGoogle Scholar
  3. 3.
    F. E. Dwulet, and M. D. Benson, Polymorphism of human plasma thyroxine binding prealbumin, Biochem. Biophys. Res. Commun. 114: 657 (1983).CrossRefGoogle Scholar
  4. 4.
    S. Tawara, M. Nakazato, K. Kangawa, H. Matsuo, and S. Araki, Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type), Biochem. Biophys. Res. Commun. 116: 880 (1983).CrossRefGoogle Scholar
  5. 5.
    M. J. M. Saraiva, S. Birken, P. P. Costa, and D. S. Goodman, Amyloid fibril protein in familial amyloidotic polyneuropathy Portuguese type, J. Clin. Invest. 74: 109 (1984).CrossRefGoogle Scholar
  6. 6.
    F. E. Dwulet, and M. D. Benson, Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin, Proc.Natl.Acad.Sei. 81:694 (1984).CrossRefGoogle Scholar
  7. 7.
    M. Nakazato, K. Kangawa, N. Minamino, S. Tawara, H. Matsuo, and S. Araki, Revised analysis of amino acid replacement in a prealbumin variant (SKO-III) associated with familial amyloidotic polyneuropathy of Jewish origin, Biochem. Biophys. Res. Commun. 123: 921 (1984).CrossRefGoogle Scholar
  8. 8.
    F. E. Dwulet, and M. D. Benson, Characterization of a transthyretin (prealbumin) variant associated with familial amyloidotic polyneuropathy type II (Indiana/Swiss), J. Clin. Invest. 78: 880 (1986).CrossRefGoogle Scholar
  9. 9.
    M. R. Wallace, F. E. Dwulet, P. M. Conneally, and M. D. Benson, Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis, J. Clin. Invest. 78: 6 (1986).CrossRefGoogle Scholar
  10. 10.
    M. R. Wallace, F. E. Dwulet, E. C. Williams, P. M. Conneally, and M. D. Benson, Identification of a new hereditary amyloid prealbumin variant, Tyr-77, associated with autosomal dominant amyloidosis, Am. J. Hum. Genet. 39: A 22 (1986).Google Scholar
  11. 11.
    W. C. Nichols, F. E. Dwulet, and M. D. Benson, Apolipoprotein A I in Iowa type hereditary amyloidosis, Clin. Res. 35: 595A (1987).Google Scholar
  12. 12.
    J. Ghiso, B. Pons-Estel, and B. Frangione, Hereditary cerebral amyloid angiopathy: the amyloid fibrils contain a protein which is a variant of cystatin C., an inhibitor of lysosomal cysteine proteases, Biochem. Biophys. Res. Commun. 136: 548 (1986).CrossRefGoogle Scholar
  13. 13.
    A. H. Koeppen, E. J. Mitzen, M. B. Hans, S-K. Peng, and R. O. Bailey, Familial amyloid polyneuropathy, Muscle & Nerve 8: 733 (1985).CrossRefGoogle Scholar
  14. 14.
    D. M. Livingston, Immunoaffinity chromatography of proteins, in: “Methods in Enzymology (Affinity Techniques; Enzyme purification, Part B) vol 34, W. B. Jakoby, and M. Wilchek, eds, Academic Press, Orlando FL (1974).Google Scholar
  15. 15.
    C. Ehnholm, A-M. Teppo, J. J. Ohisalo, and C. P. J. Maury, Human high-density lipoprotein associated amyloid A protein. Structural characteristics, relation to apoAI and AII concentrations and plasma clearance characteristics in the rat, Scand. J. Rheumatol. 14: 221 (1984).Google Scholar
  16. 16.
    J. Meretoja, T. Hollmen, T. Meretoja, and R. Penttinen, Partial characterization of amyloid proteins in inherited amyloidosis with lattice corneal dystrophy and in secondary amyloidosis, Med. Biol. 56: 17 (1978).Google Scholar
  17. 17.
    H. M. Falck, and P. Westermark, Immunohistochemical studies on amyloidosis of the Finnish type, in.: “Amyloidosis”, G. G. Glenner et al., eds, Plenum Press, New York, 375 (1986).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • C. P. J. Maury
    • 1
    • 2
  • A-M. Teppo
    • 1
    • 2
  • A-L. Kariniemi
    • 1
    • 2
  • A. H. Koeppen
    • 1
    • 2
  1. 1.Fourth Department of Medicine and Department of DermatologyUniversity of HelsinkiHelsinkiFinland
  2. 2.Neurology ServiceV.A. Medical CenterAlbanyUSA

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