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Annals of the Rheumatic Diseases logoLink to Annals of the Rheumatic Diseases
. 1979 Feb;38(1):68–71. doi: 10.1136/ard.38.1.68

Demonstration of protein AA in subcutaneous fat tissue obtained by fine needle biopsy.

P Westermark, B Stenkvist, J B Natvig, E Olding-Stenkvist
PMCID: PMC1000322  PMID: 107869

Abstract

Polarisation microscopy of material obtained by fine needle biopsy of subcutaneous tissue and stained with Congo red is a simple and reliable method for the diagnosis of systemic amyloidosis. It cannot, however, be used to differentiate histologically between different forms of amyloidosis. In the present study extracts of material obtained by fine needle biopsy of subcutaneous fat tissue from 13 patients were examined by double immunodiffusion with an antiserum against protein AA, a unique protein which forms a major part of the fibrils in secondary amyloidosis. Five of the patients showed amyloid deposits round the fat cells by conventional microscopy. In 3 of these, all with rheumatoid arthritis, protein AA was detected. Eight patients without amyloidosis and 2 with myelomatosis and amyloidosis showed no reaction with antiprotein AA antiserum. Thus the material obtained by fine needle biopsy of subcutaneous tissue could be used not only for the histological diagnosis of amyloidosis but also for a classification of systemic amyloidosis into secondary or primary based on the type of amyloid fibril protein involved.

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Selected References

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

  1. Benditt E. P., Eriksen N., Hermodson M. A., Ericsson L. H. The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences. FEBS Lett. 1971 Dec 1;19(2):169–173. doi: 10.1016/0014-5793(71)80506-9. [DOI] [PubMed] [Google Scholar]
  2. Benson M. D., Skinner M., Cohen A. S. Antigenicity and cross-reactivity of denatured fibril proteins of primary, secondary, and myeloma associated amyloids. J Lab Clin Med. 1975 Apr;85(4):650–659. [PubMed] [Google Scholar]
  3. Benson M. D., Skinner M., Lian J., Cohen A. S. "A" protein of amyloidosis. Isolation of a cross-reacting component from serum by affinity chromatography. Arthritis Rheum. 1975 Jul-Aug;18(4):315–322. doi: 10.1002/art.1780180404. [DOI] [PubMed] [Google Scholar]
  4. Cornwell G. G., 3rd, Husby G., Westermark P., Natvig J. B., Michaelsen T. E., Skogen B. Identification and characterization of different amyloid fibril proteins in tissue sections. Scand J Immunol. 1977;6(11):1071–1080. doi: 10.1111/j.1365-3083.1977.tb00344.x. [DOI] [PubMed] [Google Scholar]
  5. Glenner G. G., Terry W., Harada M., Isersky C., Page D. Amyloid fibril proteins: proof of homology with immunoglobulin light chains by sequence analyses. Science. 1971 Jun 11;172(3988):1150–1151. doi: 10.1126/science.172.3988.1150. [DOI] [PubMed] [Google Scholar]
  6. Husby G., Natvig J. B. A serum component related to nonimmunoglobulin amyloid protein AS, a possible precursor of the fibrils. J Clin Invest. 1974 Apr;53(4):1054–1061. doi: 10.1172/JCI107642. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Husby G., Natvig J. B., Michaelsen T. E., Sletten K., Höst H. Unique amyloid protein subunit common to different types of amyloid fibril. Nature. 1973 Aug 10;244(5415):362–364. doi: 10.1038/244362a0. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Pras M., Schubert M., Zucker-Franklin D., Rimon A., Franklin E. C. The characterization of soluble amyloid prepared in water. J Clin Invest. 1968 Apr;47(4):924–933. doi: 10.1172/JCI105784. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. Rosenthal C. J., Franklin E. C. Variation with age and disease of an amyloid A protein-related serum component. J Clin Invest. 1975 Apr;55(4):746–753. doi: 10.1172/JCI107985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Westermark P., Stenkvist B. A new method for the diagnosis of systemic amyloidosis. Arch Intern Med. 1973 Oct;132(4):522–523. [PubMed] [Google Scholar]

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