Skip to main content
The Journal of Clinical Investigation logoLink to The Journal of Clinical Investigation
. 1975 Apr;55(4):746–753. doi: 10.1172/JCI107985

Variation with age and disease of an amyloid A protein-related serum component.

C J Rosenthal, E C Franklin
PMCID: PMC301811  PMID: 47333

Abstract

Using the radioactively-labeled alkaline-degraded acid-soluble fraction of amyloid ([ 125I ]DAA), we developed a radioimmunoassay for the previously described amyloid-related component of the human serum (SAA). Screening the sera of 228 normal individuals and of 297 patients with a variety of illnesses, we found that SAA is a component of all human sera, including cord blood (mean 94 plus or minus 57 ng/ml). The concentration of this component increases significantly with the aging process, reaching very high levels in the eighth and nine decades. It is also elevated in all cases of amyloidosis (except for those associated with nephrotic syndrome) as well as in many patients with myeloma, macroglobulinemia, lymphoma, carcinoma, rheumatoid arthritis, and tuberculosis. A marked increase was noted in the early stages of a variety of acute inflammatory and infectious states with a return to normal levels paralleling clinical improvement and faster than the erythrocyte sedimentation rate. The possible implications of this component in the genesis of amyloid and in the immune process are discussed.

Full text

PDF
751

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. Chemical classes of amyloid substance. Am J Pathol. 1971 Oct;65(1):231–252. [PMC free article] [PubMed] [Google Scholar]
  2. Desbuquois B., Aurbach G. D. Use of polyethylene glycol to separate free and antibody-bound peptide hormones in radioimmunoassays. J Clin Endocrinol Metab. 1971 Nov;33(5):732–738. doi: 10.1210/jcem-33-5-732. [DOI] [PubMed] [Google Scholar]
  3. EHRLICH J. C., RATNER I. M. Amyloidosis of the islets of Langerhans. A restudy of islet hyalin in diabetic and non-diabetic individuals. Am J Pathol. 1961 Jan;38:49–59. [PMC free article] [PubMed] [Google Scholar]
  4. Ein D., Kimura S., Terry W. D., Magnotta J., Glenner G. G. Amino acid sequence of an amyloid fibril protein of unknown origin. J Biol Chem. 1972 Sep 10;247(17):5653–5655. [PubMed] [Google Scholar]
  5. Franklin E. C., Pras M., Levin M., Frangione B. The partial amino acid sequence of the major low molecular weight component of two human amyloid fibrils. FEBS Lett. 1972 Apr 15;22(1):121–123. doi: 10.1016/0014-5793(72)80235-7. [DOI] [PubMed] [Google Scholar]
  6. GREENWOOD F. C., HUNTER W. M., GLOVER J. S. THE PREPARATION OF I-131-LABELLED HUMAN GROWTH HORMONE OF HIGH SPECIFIC RADIOACTIVITY. Biochem J. 1963 Oct;89:114–123. doi: 10.1042/bj0890114. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Hermodson M. A., Kuhn R. W., Walsh K. A., Neurath H., Eriksen N., Benditt E. P. Amino acid sequence of monkey amyloid protein A. Biochemistry. 1972 Aug 1;11(16):2934–2938. doi: 10.1021/bi00766a002. [DOI] [PubMed] [Google Scholar]
  9. Hunter W. M. Radioimmunoassay and saturation analysis. Preparation and assessment of radioactive tracers. Br Med Bull. 1974 Jan;30(1):18–23. doi: 10.1093/oxfordjournals.bmb.a071161. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. 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]
  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. 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]
  14. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  15. Levin M., Franklin E. C., Frangione B., Pras M. The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest. 1972 Oct;51(10):2773–2776. doi: 10.1172/JCI107098. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Levin M., Pras M., Franklin E. C. Immunologic studies of the major nonimmunoglobulin protein of amyloid. I. Identification and partial characterization of a related serum component. J Exp Med. 1973 Aug 1;138(2):373–380. doi: 10.1084/jem.138.2.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Marchalonis J. J. An enzymic method for the trace iodination of immunoglobulins and other proteins. Biochem J. 1969 Jun;113(2):299–305. doi: 10.1042/bj1130299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. OUCHTERLONY O. Diffusion-in-gel methods for immunological analysis. Prog Allergy. 1958;5:1–78. [PubMed] [Google Scholar]
  19. Pras M., Reshef T. The acid-soluble fraction of amyloid--a fibril forming protein. Biochim Biophys Acta. 1972 Jun 22;271(1):193–203. doi: 10.1016/0005-2795(72)90147-x. [DOI] [PubMed] [Google Scholar]
  20. SCHEIDEGGER J. J. Une micro-méthode de l'immuno-electrophorèse. Int Arch Allergy Appl Immunol. 1955;7(2):103–110. [PubMed] [Google Scholar]
  21. TERRY R. D. THE FINE STRUCTURE OF NEUROFIBRILLARY TANGLES IN ALZHEIMER'S DISEASE. J Neuropathol Exp Neurol. 1963 Oct;22:629–642. doi: 10.1097/00005072-196310000-00005. [DOI] [PubMed] [Google Scholar]
  22. Thorell J. I., Johansson B. G. Enzymatic iodination of polypeptides with 125I to high specific activity. Biochim Biophys Acta. 1971 Dec 28;251(3):363–369. doi: 10.1016/0005-2795(71)90123-1. [DOI] [PubMed] [Google Scholar]
  23. YALOW R. S., BERSON S. A. Immunoassay of endogenous plasma insulin in man. J Clin Invest. 1960 Jul;39:1157–1175. doi: 10.1172/JCI104130. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Clinical Investigation are provided here courtesy of American Society for Clinical Investigation

RESOURCES