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. 1979 Sep 19;150(3):597–606. doi: 10.1084/jem.150.3.597

Detection of a mediator derived from endotoxin-stimulated macrohpages that induces the acute phase serum amyloid A response in mice

PMCID: PMC2185651  PMID: 479763

Abstract

The mechanism by which LPS stimulates an acute phase serum amyloid A (SAA) response in C3H mice has been studied. A factor (SAA inducer) appears in the blood of C3H/HeN (lipopolysaccharide [LPS]-sensitive) mice approximately 1 h after administration of LPS, which, when passively administered, can induce C3H/HeJ mice to produce SAA although they are resistant to the LPS itself. SAA inducer has been detected in the culture medium of LPS treated C3H/HeN macrophages but not spleen cells. Thus, two stages in the induction of the acute phase SAA response are now recognized: a latent period of 2-3 h during which the SAA concentration remains at baseline values and in which SAA inducer appears, and the period of synthesis of SAA which lasts for approoximately 24 h past induction. It is proposed that a macrophage response to LPS is responsible for production of the serum mediator which induces SAA synthesis.

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Selected References

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  1. 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]
  2. Baumal R., Sklar S., Wilson B., Laskov R. Casein-induced murine amyloidosis: amyloidogenesis in vitro by monolayer spleen explants of casein-injected mice. Lab Invest. 1978 Dec;39(6):632–639. [PubMed] [Google Scholar]
  3. 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]
  4. 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]
  5. 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]
  6. Goodrum K. J., Berry L. J. The effect of glucocorticoid antagonizing factor on hepatoma cells. Proc Soc Exp Biol Med. 1978 Dec;159(3):359–363. doi: 10.3181/00379727-159-40348. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Ignaczak T. F., Sipe J. D., Linke F. P., Glenner G. G. Immunochemical studies on the nature of the serum component (SAA) related to secondary amyloidosis. J Lab Clin Med. 1977 May;89(5):1092–1104. [PubMed] [Google Scholar]
  9. Isersky C., Page D. L., Cuatrecasas P., DeLellis R. A., Glenner G. G. Murine amyloidosis: immunologic characterization of amyloid fibril protein. J Immunol. 1971 Dec;107(6):1690–1698. [PubMed] [Google Scholar]
  10. Kushner I., Feldmann G. Control of the acute phase response. Demonstration of C-reactive protein synthesis and secretion by hepatocytes during acute inflammation in the rabbit. J Exp Med. 1978 Aug 1;148(2):466–477. doi: 10.1084/jem.148.2.466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Lavie G., Zucker-Franklin D., Franklin E. C. Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes. J Exp Med. 1978 Oct 1;148(4):1020–1031. doi: 10.1084/jem.148.4.1020. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Linder E., Lehto V. P., Virtanen I., Stenman S., Natvig J. B. Localization of amyloid-related serum protein SAA-like material to intermediate (10 nm) filaments of cultured human embryonal fibroblasts. J Exp Med. 1977 Oct 1;146(4):1158–1163. doi: 10.1084/jem.146.4.1158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Linke R. P., Sipe J. D., Pollock P. S., Ignaczak T. F., Glenner G. G. Isolation of a low-molecular-weight serum component antigenically related to an amyloid fibril protein of unknown origin. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1473–1476. doi: 10.1073/pnas.72.4.1473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. McAdam K. P., Elin R. J., Sipe J. D., Wolff S. M. Changes in human serum amyloid A and C-reactive protein after etiocholanolone-induced inflammation. J Clin Invest. 1978 Feb;61(2):390–394. doi: 10.1172/JCI108949. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. McIntire F. C., Sievert H. W., Barlow G. H., Finley R. A., Lee A. Y. Chemical, physical, biological properties of a lipopolysaccharide from Escherichia coli K-235. Biochemistry. 1967 Aug;6(8):2363–2372. doi: 10.1021/bi00860a011. [DOI] [PubMed] [Google Scholar]
  18. Rosenstreich D. L., McAdam K. P. Lymphoid cells in endotoxin-induced production of the amyloid-related serum amyloid A protein. Infect Immun. 1979 Jan;23(1):181–183. doi: 10.1128/iai.23.1.181-183.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. 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]
  20. Rosenthal C. J., Sullivan L. Serum amyloid A: evidence for its origin in polymorphonuclear leukocytes. J Clin Invest. 1978 Dec;62(6):1181–1186. doi: 10.1172/JCI109237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Sipe J. D., Ignaczak T. F., Pollock P. S., Glenner G. G. Amyloid fibril protein AA: purification and properties of the antigenically related serum component as determined by solid phase radioimmunoassay. J Immunol. 1976 Apr;116(4):1151–1156. [PubMed] [Google Scholar]
  22. Sipe J. D. Induction of the acute-phase serum protein SAA requires both RNA and protein synthesis. Br J Exp Pathol. 1978 Jun;59(3):305–310. [PMC free article] [PubMed] [Google Scholar]
  23. Sipe J. D., McAdam K. P., Uchino F. Biochemical evidence for the biphasic development of experimental amyloidosis. Lab Invest. 1978 Jan;38(1):110–114. [PubMed] [Google Scholar]

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