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. 1987 Feb 15;242(1):301–303. doi: 10.1042/bj2420301

Acute-phase high-density lipoprotein in the rat does not contain serum amyloid A protein.

M L Baltz, I F Rowe, D Caspi, W G Turnell, M B Pepys
PMCID: PMC1147699  PMID: 2439069

Abstract

Serum amyloid A protein (SAA) is an acute-phase apolipoprotein of high-density lipoprotein (HDL). Its N-terminal sequence is identical with that of amyloid A protein (AA), the subunit of AA amyloid fibrils. However, rats do not develop AA amyloidosis, and we report here that neither normal nor acute-phase rat HDL contains a protein corresponding to SAA of other species. mRNA coding for a sequence homologous with the C-terminal but not with the N-terminal part of human SAA is synthesized in greatly increased amounts in acute-phase rat liver. These observations indicate that the failure of rats to develop AA amyloid results from the absence of most of the AA-like part of their SAA-like protein, and that the N-terminal portion of SAA probably contains the lipid-binding sequences.

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Selected References

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  1. 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]
  2. Benditt E. P., Eriksen N., Hanson R. H. Amyloid protein SAA is an apoprotein of mouse plasma high density lipoprotein. Proc Natl Acad Sci U S A. 1979 Aug;76(8):4092–4096. doi: 10.1073/pnas.76.8.4092. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. 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]
  4. Eriksen N., Benditt E. P. Trauma, high density lipoproteins, and serum amyloid protein A. Clin Chim Acta. 1984 Jul 16;140(2):139–149. doi: 10.1016/0009-8981(84)90338-3. [DOI] [PubMed] [Google Scholar]
  5. 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]
  6. Glenner G. G. Amyloid deposits and amyloidosis: the beta-fibrilloses (second of two parts). N Engl J Med. 1980 Jun 12;302(24):1333–1343. doi: 10.1056/NEJM198006123022403. [DOI] [PubMed] [Google Scholar]
  7. Green C. J. Amyloidosis as an incidental finding in rats on experiment. Lab Anim. 1974 Jan;8(1):99–101. doi: 10.1258/002367774780943850. [DOI] [PubMed] [Google Scholar]
  8. Gruys E. A comparative approach to secondary amyloidosis: minireview. Dev Comp Immunol. 1979 Winter;3(1):23–36. doi: 10.1016/s0145-305x(79)80003-8. [DOI] [PubMed] [Google Scholar]
  9. HAVEL R. J., EDER H. A., BRAGDON J. H. The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum. J Clin Invest. 1955 Sep;34(9):1345–1353. doi: 10.1172/JCI103182. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Jakob W. Spontaneous amyloidosis of mammals. Vet Pathol. 1971;8(4):292–306. doi: 10.1177/030098587100800402. [DOI] [PubMed] [Google Scholar]
  11. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  12. Lasser N. L., Roheim P. S., Edelstein D., Eder H. A. Serum lipoproteins of normal and cholesterol-fed rats. J Lipid Res. 1973 Jan;14(1):1–8. [PubMed] [Google Scholar]
  13. Marhaug G., Børresen A. L., Husby G., Nordstoga K. A comparative study of serum amyloid a protein (SAA) from mink and man. Comp Biochem Physiol B. 1984;78(2):401–406. doi: 10.1016/0305-0491(84)90049-x. [DOI] [PubMed] [Google Scholar]
  14. Parmelee D. C., Titani K., Ericsson L. H., Eriksen N., Benditt E. P., Walsh K. A. Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein. Biochemistry. 1982 Jul 6;21(14):3298–3303. doi: 10.1021/bi00257a008. [DOI] [PubMed] [Google Scholar]
  15. Pepys M. B., Baltz M. L. Acute phase proteins with special reference to C-reactive protein and related proteins (pentaxins) and serum amyloid A protein. Adv Immunol. 1983;34:141–212. doi: 10.1016/s0065-2776(08)60379-x. [DOI] [PubMed] [Google Scholar]
  16. Pepys M. B. Isolation of serum amyloid P-component (protein SAP) in the mouse. Immunology. 1979 Jul;37(3):637–641. [PMC free article] [PubMed] [Google Scholar]
  17. Skogen B., Børresen A. L., Natvig J. B., Berg K., Michaelsen T. E. High-density lipoprotein as carrier for amyloid-related protein SAA in rabbit serum. Scand J Immunol. 1979;10(1):39–45. doi: 10.1111/j.1365-3083.1979.tb01332.x. [DOI] [PubMed] [Google Scholar]
  18. Swaney J. B., Reese H., Eder H. A. Polypeptide composition of rat high density lipoprotein: characterization by SDS-gel electrophoresis. Biochem Biophys Res Commun. 1974 Jul 24;59(2):513–519. doi: 10.1016/s0006-291x(74)80010-0. [DOI] [PubMed] [Google Scholar]
  19. Vargas K. J., Stephens L. C. Resistance of Rowett athymic (nude) rats to casein-induced amyloidosis. Am J Vet Res. 1983 Aug;44(8):1597–1599. [PubMed] [Google Scholar]
  20. Yamamoto K., Migita S. Complete primary structures of two major murine serum amyloid A proteins deduced from cDNA sequences. Proc Natl Acad Sci U S A. 1985 May;82(9):2915–2919. doi: 10.1073/pnas.82.9.2915. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. de Beer F. C., Baltz M. L., Munn E. A., Feinstein A., Taylor J., Bruton C., Clamp J. R., Pepys M. B. Isolation and characterization of C-reactive protein and serum amyloid P component in the rat. Immunology. 1982 Jan;45(1):55–70. [PMC free article] [PubMed] [Google Scholar]

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