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Clinical and Experimental Immunology logoLink to Clinical and Experimental Immunology
. 1990 Aug;81(2):325–328. doi: 10.1111/j.1365-2249.1990.tb03339.x

A primed state exists in vivo following histological regression of amyloidosis.

P N Hawkins 1, M B Pepys 1
PMCID: PMC1535055  PMID: 2387095

Abstract

Using a sensitive, quantitative, and non-invasive in vivo method, based on the specific binding of serum amyloid P component to amyloid fibrils, we have directly documented the spontaneous resolution of AA amyloid deposits in mice, and the prolonged existence thereafter of a primed state of enhanced susceptibility to further amyloid deposition. These results may have important implications for understanding and management of amyloidosis in humans.

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Selected References

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

  1. Axelrad M. A., Kisilevsky R., Willmer J., Chen S. J., Skinner M. Further characterization of amyloid-enhancing factor. Lab Invest. 1982 Aug;47(2):139–146. [PubMed] [Google Scholar]
  2. Baltz M. L., Caspi D., Evans D. J., Rowe I. F., Hind C. R., Pepys M. B. Circulating serum amyloid P component is the precursor of amyloid P component in tissue amyloid deposits. Clin Exp Immunol. 1986 Dec;66(3):691–700. [PMC free article] [PubMed] [Google Scholar]
  3. Caspi D., Zalzman S., Baratz M., Teitelbaum Z., Yaron M., Pras M., Baltz M. L., Pepys M. B. Imaging of experimental amyloidosis with 131I-labeled serum amyloid P component. Arthritis Rheum. 1987 Nov;30(11):1303–1306. doi: 10.1002/art.1780301115. [DOI] [PubMed] [Google Scholar]
  4. Coria F., Castaño E., Prelli F., Larrondo-Lillo M., van Duinen S., Shelanski M. L., Frangione B. Isolation and characterization of amyloid P component from Alzheimer's disease and other types of cerebral amyloidosis. Lab Invest. 1988 Apr;58(4):454–458. [PubMed] [Google Scholar]
  5. De Beer F. C., Pepys M. B. Isolation of human C-reactive protein and serum amyloid P component. J Immunol Methods. 1982;50(1):17–31. doi: 10.1016/0022-1759(82)90300-3. [DOI] [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. Hawkins P. N., Myers M. J., Epenetos A. A., Caspi D., Pepys M. B. Specific localization and imaging of amyloid deposits in vivo using 123I-labeled serum amyloid P component. J Exp Med. 1988 Mar 1;167(3):903–913. doi: 10.1084/jem.167.3.903. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hawkins P. N., Myers M. J., Lavender J. P., Pepys M. B. Diagnostic radionuclide imaging of amyloid: biological targeting by circulating human serum amyloid P component. Lancet. 1988 Jun 25;1(8600):1413–1418. doi: 10.1016/s0140-6736(88)92235-0. [DOI] [PubMed] [Google Scholar]
  9. JANIGAN D. T. EXPERIMENTAL AMYLOIDOSIS: STUDIES WITH A MODIFIED CASEIN METHOD, CASEIN HYDROLYSATE AND GELATIN. Am J Pathol. 1965 Jul;47:159–171. [PMC free article] [PubMed] [Google Scholar]
  10. Mather S. J., Ward B. G. High efficiency iodination of monoclonal antibodies for radiotherapy. J Nucl Med. 1987 Jun;28(6):1034–1036. [PubMed] [Google Scholar]
  11. Pepys M. B., Dyck R. F., de Beer F. C., Skinner M., Cohen A. S. Binding of serum amyloid P-component (SAP) by amyloid fibrils. Clin Exp Immunol. 1979 Nov;38(2):284–293. [PMC free article] [PubMed] [Google Scholar]

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