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. 1979 Aug;76(8):4092–4096. doi: 10.1073/pnas.76.8.4092

Amyloid protein SAA is an apoprotein of mouse plasma high density lipoprotein.

E P Benditt, N Eriksen, R H Hanson
PMCID: PMC383984  PMID: 226994

Abstract

Mouse plasma contains a protein antigenically related to mouse protein AA, the principal protein derived from tissue deposits of amyloid substance in mice. In this work the plasma antigen, SAA, was found mainly as a high molecular weight form (2 x 10(5)) residing for the most part in the density interval 1.063-1.21 g/cm3 (high density lipoprotein, HDL); the largest amount of SAA, absolute and relative to total protein, was found in the density interval 1.125-12.1 g/cm3 (HDL3). When apoproteins of the mouse HDL obtained by delipidation of the lipoprotein particles were chromatographed in acid/urea, the antigenic activity appeared in the 10,000- to 15,000-dalton portion of the apoprotein complex. In these characteristics mouse SAA closely resembles human SAA and the behavior of the protein related to amyloid protein AA indicates that is one of the apoproteins of the HDL complex in both species. Therefore we suggest that it be named apoSAA.

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Selected References

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  1. Allain C. C., Poon L. S., Chan C. S., Richmond W., Fu P. C. Enzymatic determination of total serum cholesterol. Clin Chem. 1974 Apr;20(4):470–475. [PubMed] [Google Scholar]
  2. Anders R. F., Natvig J. B., Michaelsen T. E., Husby G. Isolation and characterization of amyloid-related serum protein SAA as a low molecular weight protein. Scand J Immunol. 1975;4(4):397–401. doi: 10.1111/j.1365-3083.1975.tb02642.x. [DOI] [PubMed] [Google Scholar]
  3. Anders R. F., Natvig J. B., Sletten K., Husby G., Nordstoga K. Amyloid-related serum protein SAA from three animal species: comparison with human SAA. J Immunol. 1977 Jan;118(1):229–234. [PubMed] [Google Scholar]
  4. Benditt E. P., Eriksen N. Amyloid protein SAA is associated with high density lipoprotein from human serum. Proc Natl Acad Sci U S A. 1977 Sep;74(9):4025–4028. doi: 10.1073/pnas.74.9.4025. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. Benditt E. P., Eriksen N. Chemical similarity among amyloid substances associated with long standing inflammation. Lab Invest. 1972 Jun;26(6):615–625. [PubMed] [Google Scholar]
  7. 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]
  8. 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]
  9. Eriksen N., Ericsson L. H., Pearsall N., Lagunoff D., Benditt E. P. Mouse amyloid protein AA: Homology with nonimmunoglobulin protein of human and monkey amyloid substance. Proc Natl Acad Sci U S A. 1976 Mar;73(3):964–967. doi: 10.1073/pnas.73.3.964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fainaru M., Glangeaud M. C., Eisenberg S. Radioimmunoassay of human high density lipoprotein apo-protein A-1. Biochim Biophys Acta. 1975 Apr 29;386(2):432–443. doi: 10.1016/0005-2795(75)90286-x. [DOI] [PubMed] [Google Scholar]
  11. Goldstein J. L., Brown M. S., Stone N. J. Genetics of the LDL receptor: evidence that the mutations affecting binding and internalization are allelic. Cell. 1977 Nov;12(3):629–641. doi: 10.1016/0092-8674(77)90263-x. [DOI] [PubMed] [Google Scholar]
  12. Gorevic P. D., Levo Y., Frangione B., Franklin E. C. Polymorphism of tissue and serum amyloid A (AA and SAA) proteins in the mouse. J Immunol. 1978 Jul;121(1):138–140. [PubMed] [Google Scholar]
  13. Herbert P. N., Windmueller H. G., Bersot T. P., Shulman R. S. Characterization of the rat apolipoproteins. I. The low molecular weight proteins of rat plasma high density lipoproteins. J Biol Chem. 1974 Sep 25;249(18):5718–5724. [PubMed] [Google Scholar]
  14. Hijmans W., Sipe J. D. Levels of the serum amyloid A protein (SAA) in normal persons of different age groups. Clin Exp Immunol. 1979 Jan;35(1):96–100. [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. Husby G., Natvig J. B., Sletten K., Nordstoga K., Anders R. F. An experimental model in mink for studying the relation between amyloid fibril protein AA and the related serum protein SAA. Scand J Immunol. 1975;4(8):811–816. doi: 10.1111/j.1365-3083.1975.tb03721.x. [DOI] [PubMed] [Google Scholar]
  17. 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]
  18. Johansson M. B., Karlsson B. W. Lipoproteins in serum of rat, mouse, gerbil, rabbit, pig and man studied by electrophoretical and immunological methods. Comp Biochem Physiol B. 1976;54(4):495–500. doi: 10.1016/0305-0491(76)90128-0. [DOI] [PubMed] [Google Scholar]
  19. Karlin J. B., Juhn D. J., Starr J. I., Scanu A. M., Rubenstein A. H. Measurement of human high density lipoprotein apolipoprotein A-1 in serum by radioimmunoassay. J Lipid Res. 1976 Jan;17(1):30–37. [PubMed] [Google Scholar]
  20. 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]
  21. 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]
  22. McAdam K. P., Sipe J. D. Murine model for human secondary amyloidosis: genetic variability of the acute-phase serum protein SAA response to endotoxins and casein. J Exp Med. 1976 Oct 1;144(4):1121–1127. doi: 10.1084/jem.144.4.1121. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Osborne J. C., Jr, Brewer H. B., Jr The plasma lipoproteins. Adv Protein Chem. 1977;31:253–337. doi: 10.1016/s0065-3233(08)60220-x. [DOI] [PubMed] [Google Scholar]
  24. Rosenthal C. J., Franklin E. C., Frangione B., Greenspan J. Isolation and partial characterization of SAA-an amyloid-related protein from human serum. J Immunol. 1976 May;116(5):1415–1418. [PubMed] [Google Scholar]
  25. Schacterle G. R., Pollack R. L. A simplified method for the quantitative assay of small amounts of protein in biologic material. Anal Biochem. 1973 Feb;51(2):654–655. doi: 10.1016/0003-2697(73)90523-x. [DOI] [PubMed] [Google Scholar]
  26. Schaefer E. J., Eisenberg S., Levy R. I. Lipoprotein apoprotein metabolism. J Lipid Res. 1978 Aug;19(6):667–687. [PubMed] [Google Scholar]
  27. Segrest J. P., Pownall H. J., Jackson R. L., Glenner G. G., Pollock P. S. Amyloid A: amphipathic helixes and lipid binding. Biochemistry. 1976 Jul 27;15(15):3187–3191. doi: 10.1021/bi00660a005. [DOI] [PubMed] [Google Scholar]
  28. Shore V. G., Shore B., Lewis S. B. Isolation and characterization of two threonine-poor apolipoproteins of human plasma high density lipoproteins. Biochemistry. 1978 May 30;17(11):2174–2179. doi: 10.1021/bi00604a023. [DOI] [PubMed] [Google Scholar]
  29. Sipe J. D., McAdam K. P., Torain B. F., Glenner G. G. Conformational flexibility of the serum amyloid precursor SAA. Br J Exp Pathol. 1976 Oct;57(5):582–592. [PMC free article] [PubMed] [Google Scholar]
  30. Sipe J. D., McAdam K. P., Torain B. F., Pollock P. S. Isolation and structural properties of murine SAA--the acute phase serum precursor of amyloid AA. Immunol Commun. 1977;6(1):1–12. doi: 10.3109/08820137709055799. [DOI] [PubMed] [Google Scholar]
  31. Skinner M., Cathcart E. S., Cohen A. S., Benson M. D. Isolation and identification by sequence analysis of experimentally induced guinea pig amyloid fibrils. J Exp Med. 1974 Sep 1;140(3):871–876. doi: 10.1084/jem.140.3.871. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Skogen B., Natvig J. B., Michaelsen T. E., Anders R. F. A high molecular weight serum protein is the carrier for amyloid-related protein SAA. Scand J Immunol. 1977;6(12):1363–1368. doi: 10.1111/j.1365-3083.1977.tb00379.x. [DOI] [PubMed] [Google Scholar]
  33. Swank R. T., Munkres K. D. Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate. Anal Biochem. 1971 Feb;39(2):462–477. doi: 10.1016/0003-2697(71)90436-2. [DOI] [PubMed] [Google Scholar]
  34. Tall A. R., Deckelbaum R. J., Small D. M., Shipley G. G. Thermal behavior of human plasma high density lipoprotein. Biochim Biophys Acta. 1977 Apr 26;487(1):145–133. doi: 10.1016/0005-2760(77)90051-0. [DOI] [PubMed] [Google Scholar]
  35. Tall A. R., Small D. M., Shipley G. G., Lees R. S. Apoprotein stability and lipid-protein interactions in human plasma high density lipoproteins. Proc Natl Acad Sci U S A. 1975 Dec;72(12):4940–4942. doi: 10.1073/pnas.72.12.4940. [DOI] [PMC free article] [PubMed] [Google Scholar]

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