Skip to main content
Clinical and Experimental Immunology logoLink to Clinical and Experimental Immunology
. 1981 Jul;45(1):90–96.

Characterization of an amyloid fibril protein from localized amyloidosis of the skin as lambda immunoglobulin light chains of variable subgroup I (A lambda I).

G Husby, K Sletten, N Blumenkrantz, L Danielsen
PMCID: PMC1537258  PMID: 6796317

Abstract

Amyloid fibrils obtained from a case (Hud) of localized, tumorous amyloidosis of the skin were investigated by immunological and biochemical methods including amino acid sequence studies. Evidence was obtained that a lambda immunoglobulin light chain protein, A lambda I, and differently sized N terminal fragments (mol. wt 14,000 and 10,000) of the same protein comprised a major component of the fibrils. The chemical nature of this protein suggested that this case of cutaneous amyloidosis belonged to the idiopathic form of amyloidosis, probably as a special type of systemic, idiopathic amyloid disease.

Full text

PDF
90

Selected References

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

  1. Brownstein M. H., Helwig E. B. The cutaneous amyloidoses. I. Localized forms. Arch Dermatol. 1970 Jul;102(1):8–19. [PubMed] [Google Scholar]
  2. 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]
  3. Danielsen L., Christensen H. E., Wanstrup J. Cutaneous amyloidosis. Classification, pathogenesis and relation to "collagen disease". Acta Pathol Microbiol Scand A. 1970;78(3):335–344. [PubMed] [Google Scholar]
  4. Danielsen L., Kobayasi T. An ultrastructural study of cutaneous amyloidosis. Acta Derm Venereol. 1973;53(1):13–21. [PubMed] [Google Scholar]
  5. Engelhard M., Hilschmann N. Zur Strukturregel der Antikörper. Die Aminosäuresequenz einer monoklonalen immunglobulin-L-Kette vom lambde-Typ, Subgruppe I (Bence-Jones-Protein Vor.) Ein Beitrag zur Aufklärung der Entsthung der Antikörperspezifitäten. Hoppe Seylers Z Physiol Chem. 1975 Sep;356(9):1413–1444. [PubMed] [Google Scholar]
  6. 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]
  7. Glenner G. G., Page D. L. Amyloid, amyloidosis, and amyloidogenesis. Int Rev Exp Pathol. 1976;15:1–92. [PubMed] [Google Scholar]
  8. Harada M., Isersky C., Cuatrecasas P., Page D., Bladen H. A., Eanes E. D., Keiser H. R., Glenner G. G. Human amyloid protein: chemical variability and homogeneity. J Histochem Cytochem. 1971 Jan;19(1):1–15. doi: 10.1177/19.1.1. [DOI] [PubMed] [Google Scholar]
  9. Husby G. A chemical classification of amyloid. Correlation with different clinical types of amyloidosis. Scand J Rheumatol. 1980;9(1):60–64. doi: 10.1080/03009748009098131. [DOI] [PubMed] [Google Scholar]
  10. Husby G., Lindström F. D., Natvig J. B., Dahlström U. Occurrence of amyloid-related serum proteins in patients with benign monoclonal gammopathy. Scand J Immunol. 1977;6(6-7):659–663. doi: 10.1111/j.1365-3083.1977.tb02146.x. [DOI] [PubMed] [Google Scholar]
  11. Husby G., Sletten K., Michaelsen T. E., Natvig J. B. Amyloid fibril protein subunit, "protein AS": distribution in tissue and serum in different clinical types of amyloidosis including that associated with myelomatosis and Waldenström's macroglobulinamia. Scand J Immunol. 1973;2(4):395–404. doi: 10.1111/j.1365-3083.1973.tb02048.x. [DOI] [PubMed] [Google Scholar]
  12. Husby G., Sletten K., Michaelsen T. E., Natvig J. B. Antigenic and chemical characterization of non-immunoglobulin amyloid proteins. Scand J Immunol. 1972;1(4):393–400. doi: 10.1111/j.1365-3083.1972.tb03305.x. [DOI] [PubMed] [Google Scholar]
  13. Husby G., Sletten K. Structural similarities between a protein extracted from normal human tissues and a component of amyloid fibrils. Acta Pathol Microbiol Scand C. 1977 Jun;85(3):153–160. doi: 10.1111/j.1699-0463.1977.tb03625.x. [DOI] [PubMed] [Google Scholar]
  14. Isersky C., Ein D., Page D. L., Harada M., Glenner G. G. Immunochemical cross-reactions of human amyloid proteins with human immunoglobulin light polypeptide chains. J Immunol. 1972 Feb;108(2):486–493. [PubMed] [Google Scholar]
  15. Møyner K., Sletten K., Husby G., Natvig J. B. An unusually large (83 amino acid residues) amyloid fibril protein AA from a patient with Waldenström's macroglobulinaemia and amyloidosis. Scand J Immunol. 1980;11(5):549–554. doi: 10.1111/j.1365-3083.1980.tb00023.x. [DOI] [PubMed] [Google Scholar]
  16. Page D. L., Isersky C., Harada M., Glenner G. G. Immunoglobulin origin of localized nodular pulmonary amyloidosis. Res Exp Med (Berl) 1972;159(2):75–86. doi: 10.1007/BF01856034. [DOI] [PubMed] [Google Scholar]
  17. Pras M., Glynn L. E. Isolation of a non-collagenous reticulin component and its primary characterization. Br J Exp Pathol. 1973 Aug;54(4):449–456. [PMC free article] [PubMed] [Google Scholar]
  18. 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]
  19. Sletten K., Dus K., De Klerk H., Kamen M. D. Cytochrome c2 of Rhodospirillum rubrum. 1. Molecular properties of the protein and amino acid sequences of its peptides derived by the action of trypsin and thermolysin. J Biol Chem. 1968 Oct 25;243(20):5492–5506. [PubMed] [Google Scholar]
  20. Sletten K., Husby G., Natvig J. B. N-terminal amino acid sequence of amyloid fibril protein AR, prototype of a new lambda-variable subgroup, V lambda V. Scand J Immunol. 1974;3(6):833–836. doi: 10.1111/j.1365-3083.1974.tb01319.x. [DOI] [PubMed] [Google Scholar]
  21. 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]
  22. Waalen K., Sletten K., Husby G., Nordstoga K. The primary structure of amyloid fibril protein AA in endotoxin-induced amyloidosis of the mink. Eur J Biochem. 1980 Mar;104(2):407–412. doi: 10.1111/j.1432-1033.1980.tb04441.x. [DOI] [PubMed] [Google Scholar]
  23. Westermark P., Natvig J. B., Anders R. F., Sletten K., Husby G. Coexistence of protein AA and immunoglobulin light-chain fragments in amyloid fibrils. Scand J Immunol. 1976;5(1-2):31–36. doi: 10.1111/j.1365-3083.1976.tb02989.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES