Skip to main content
NCBI home page
Clinical and Experimental Immunology logoLink to Clinical and Experimental Immunology
. 1987 Sep;69(3):695–701.

Prealbumin variants in the amyloid fibrils of Swedish familial amyloidotic polyneuropathy.

P Westermark 1, K Sletten 1, B O Olofsson 1
PMCID: PMC1542365  PMID: 3117463

Abstract

Amino-acid sequence analysis of an amyloid fibril protein from a patient with Swedish familial amyloidotic polyneuropathy showed homology with prealbumin but with heterogeneous N-terminal deletions. One-third of the molecules had the same amino acid substitution, methionine for valine in position 30, as in familial amyloidosis of Portuguese, Japanese and Swedish-American type. A protein with the same antigenic properties and size was found in the fibrils of two other patients with Swedish FAP while the amyloid fibrils in two further patients predominantly contained a smaller prealbumin-derived protein. Cyanogen bromide cleavage of this protein revealed no evidence for a methionine residue in position 30.

Full text

PDF
695

Images in this article

697Fig. 1
on p.697
697Fig. 2
on p.697

Selected References

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

  1. Blake C. C., Geisow M. J., Oatley S. J., Rérat B., Rérat C. Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 A. J Mol Biol. 1978 May 25;121(3):339–356. doi: 10.1016/0022-2836(78)90368-6. [DOI] [PubMed] [Google Scholar]
  2. Blobel G., Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol. 1975 Dec;67(3):835–851. doi: 10.1083/jcb.67.3.835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  4. Cornwell G. G., 3rd, Murdoch W. L., Kyle R. A., Westermark P., Pitkänen P. Frequency and distribution of senile cardiovascular amyloid. A clinicopathologic correlation. Am J Med. 1983 Oct;75(4):618–623. doi: 10.1016/0002-9343(83)90443-6. [DOI] [PubMed] [Google Scholar]
  5. Cornwell G. G., 3rd, Westermark P., Natvig J. B., Murdoch W. Senile cardiac amyloid: evidence that fibrils contain a protein immunologically related to prealbumin. Immunology. 1981 Nov;44(3):447–452. [PMC free article] [PubMed] [Google Scholar]
  6. Dwulet F. E., Benson M. D. Characterization of a transthyretin (prealbumin) variant associated with familial amyloidotic polyneuropathy type II (Indiana/Swiss). J Clin Invest. 1986 Oct;78(4):880–886. doi: 10.1172/JCI112675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Dwulet F. E., Benson M. D. Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin. Proc Natl Acad Sci U S A. 1984 Feb;81(3):694–698. doi: 10.1073/pnas.81.3.694. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Eanes E. D., Glenner G. G. X-ray diffraction studies on amyloid filaments. J Histochem Cytochem. 1968 Nov;16(11):673–677. doi: 10.1177/16.11.673. [DOI] [PubMed] [Google Scholar]
  9. Felding P., Fex G., Westermark P., Olofsson B. O., Pitkänen P., Benson L. Prealbumin in Swedish patients with senile systemic amyloidosis and familial amyloidotic polyneuropathy. Scand J Immunol. 1985 Feb;21(2):133–140. doi: 10.1111/j.1365-3083.1985.tb01412.x. [DOI] [PubMed] [Google Scholar]
  10. Glenner G. G. Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts). N Engl J Med. 1980 Jun 5;302(23):1283–1292. doi: 10.1056/NEJM198006053022305. [DOI] [PubMed] [Google Scholar]
  11. Kanda Y., Goodman D. S., Canfield R. E., Morgan F. J. The amino acid sequence of human plasma prealbumin. J Biol Chem. 1974 Nov 10;249(21):6796–6805. [PubMed] [Google Scholar]
  12. Nakazato M., Kangawa K., Minamino N., Tawara S., Matsuo H., Araki S. Identification of a prealbumin variant in the serum of a Japanese patient with familial amyloidotic polyneuropathy. Biochem Biophys Res Commun. 1984 Jul 31;122(2):712–718. doi: 10.1016/s0006-291x(84)80092-3. [DOI] [PubMed] [Google Scholar]
  13. Nakazato M., Kangawa K., Minamino N., Tawara S., Matsuo H., Araki S. Revised analysis of amino acid replacement in a prealbumin variant (SKO-III) associated with familial amyloidotic polyneuropathy of Jewish origin. Biochem Biophys Res Commun. 1984 Sep 28;123(3):921–928. doi: 10.1016/s0006-291x(84)80222-3. [DOI] [PubMed] [Google Scholar]
  14. Pras M., Prelli F., Franklin E. C., Frangione B. Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin. Proc Natl Acad Sci U S A. 1983 Jan;80(2):539–542. doi: 10.1073/pnas.80.2.539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. Saraiva M. J., Birken S., Costa P. P., Goodman D. S. Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin). J Clin Invest. 1984 Jul;74(1):104–119. doi: 10.1172/JCI111390. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Sletten K., Husby G. The complete amino-acid sequence of non-immunoglobulin amyloid fibril protein AS in rheumatoid arthritis. Eur J Biochem. 1974 Jan 3;41(1):117–125. doi: 10.1111/j.1432-1033.1974.tb03251.x. [DOI] [PubMed] [Google Scholar]
  18. Sletten K., Natvig J. B., Husby G., Juul J. The complete amino acid sequence of a prototype immunoglobulin-lambda light-chain-type amyloid-fibril protein AR. Biochem J. 1981 Jun 1;195(3):561–572. doi: 10.1042/bj1950561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sletten K., Westermark P., Natvig J. B. Senile cardiac amyloid is related to prealbumin. Scand J Immunol. 1980;12(6):503–506. doi: 10.1111/j.1365-3083.1980.tb00098.x. [DOI] [PubMed] [Google Scholar]
  20. Sundelin J., Melhus H., Das S., Eriksson U., Lind P., Trägårdh L., Peterson P. A., Rask L. The primary structure of rabbit and rat prealbumin and a comparison with the tertiary structure of human prealbumin. J Biol Chem. 1985 May 25;260(10):6481–6487. [PubMed] [Google Scholar]
  21. Tawara S., Nakazato M., Kangawa K., Matsuo H., Araki S. Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type). Biochem Biophys Res Commun. 1983 Nov 15;116(3):880–888. doi: 10.1016/s0006-291x(83)80224-1. [DOI] [PubMed] [Google Scholar]
  22. Wallace M. R., Dwulet F. E., Conneally P. M., Benson M. D. Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis. J Clin Invest. 1986 Jul;78(1):6–12. doi: 10.1172/JCI112573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Westermark P., Natvig J. B., Johansson B. Characterization of an amyloid fibril protein from senile cardiac amyloid. J Exp Med. 1977 Aug 1;146(2):631–636. doi: 10.1084/jem.146.2.631. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Clinical and Experimental Immunology are provided here courtesy of British Society for Immunology

RESOURCES