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. 1980 Feb;39(2):355–360.

Differences in the acute phase responses of serum amyloid P-component (SAP) and C3 to injections of casein or bovine serum albumin in amyloid-susceptible and -resistant mouse strains.

M L Baltz, K Gomer, A J Davies, D J Evans, G G Klaus, M B Pepys
PMCID: PMC1538052  PMID: 7389204

Abstract

In CBA/Ca and C57Bl/Cbi mice, which are susceptible to casein-induced amyloidosis, daily injections of casein caused a marked rise in the level of circulating serum amyloid P-component (SAP), which was sustained while injections continued. In contrast, mice given bovine serum albumin (BSA) injections showed only a small, transient increase in SAP levels. A/J mice, which are relatively resistant to casein-induced amyloidosis, also developed high SAP levels initially, but the increase was not maintained despite continued administration of casein. A/J mice receiving BSA had a slowly progressive rise in SAP which reached the same level as in the casein-treated animals. Administration of colchicine, which prevents casein-induced amyloidosis, suppressed the SAP response to casein in CBA mice. The serum level of the C3 component of complement, which is not an amyloid protein but is an acute phase reactant, also increased following casein injection. The rise in C3 was, however, proportionately less than that of SAP, was less sustained and was scarcely affected by colchicine. The present results therefore demonstrate different patterns in the acute phase response of different proteins in different mouse strains, and suggest that there may be a relationship between sustained high levels of SAP and the deposition of amyloid.

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Selected References

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

  1. Benson M. D., Scheinberg M. A., Shirahama T., Cathcart E. S., Skinner M. Kinetics of serum amyloid protein A in casein-induced murine amyloidosis. J Clin Invest. 1977 Mar;59(3):412–417. doi: 10.1172/JCI108654. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Britton S. Experimental amyloidosis: the inducer is a polyclonal B-cell activator to which susceptibility is under genetic control. J Exp Med. 1975 Dec 1;142(6):1564–1569. doi: 10.1084/jem.142.6.1564. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cathcart E. S., Wollheim F. A., Cohen A. S. Plasma protein constituents of amyloid fibrils. J Immunol. 1967 Aug;99(2):376–385. [PubMed] [Google Scholar]
  4. Cohen A. S., Shirahama T. Animal model for human disease: spontaneous and induced amyloidosis. Am J Pathol. 1972 Aug;68(2):441–444. [PMC free article] [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. HORNUNG M., ARQUEMBOURG R. C. BETA-1-C-GLOBULIN: AN "ACUTE PHASE" SERUM REACTANT OF HUMAN SERUM. J Immunol. 1965 Feb;94:307–316. [PubMed] [Google Scholar]
  7. Hartveit F., Borve W., Thunold S. Serum complement levels and response to turpentine inflammation in mice. Acta Pathol Microbiol Scand Suppl. 1973;236(0):54–59. [PubMed] [Google Scholar]
  8. 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]
  9. Janigan D. T., Druet R. L. Experimental amyloidosis. Role of antigenicity and rapid induction. Am J Pathol. 1966 Jun;48(6):1013–1025. [PMC free article] [PubMed] [Google Scholar]
  10. Kedar I., Ravid M., Sohar E., Gafni J. Colchicine inhibition of casein-induced amyloidosis in mice. Isr J Med Sci. 1974 Jul;10(7):787–789. [PubMed] [Google Scholar]
  11. Kushner I., Edgington T. S., Trimble C., Liem H. H., Muller-Eberhard U. Plasma hemopexin homeostasis during the acute phase response. J Lab Clin Med. 1972 Jul;80(1):18–25. [PubMed] [Google Scholar]
  12. 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]
  13. 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]
  14. Natsuume-Sakai S., Motonishi K., Takahashi M. Quantitation of beta 1c/1A globulin (C3) in inbred mice: variation dependent upon strain, age, sex and environment. Int Arch Allergy Appl Immunol. 1977;53(3):269–278. doi: 10.1159/000231762. [DOI] [PubMed] [Google Scholar]
  15. Pepys M. B., Baltz M., Gomer K., Davies A. J., Doenhoff M. Serum amyloid P-component is an acute-phase reactant in the mouse. Nature. 1979 Mar 15;278(5701):259–261. doi: 10.1038/278259a0. [DOI] [PubMed] [Google Scholar]
  16. Pepys M. B., Dash A. C., Fielder A. H., Mirjah D. D. Isolation and study of murine C3. Immunology. 1977 Oct;33(4):491–499. [PMC free article] [PubMed] [Google Scholar]
  17. Pepys M. B., Dash A. C., Markham R. E., Thomas H. C., Williams B. D., Petrie A. Comparative clinical study of protein SAP (amyloid P component) and C-reactive protein in serum. Clin Exp Immunol. 1978 Apr;32(1):119–124. [PMC free article] [PubMed] [Google Scholar]
  18. 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]
  19. Ram J. S., DeLellis R. A., Glenner G. G. Amyloid. 8. On strain variability in experimental murine amyloidosis. Proc Soc Exp Biol Med. 1969 Feb;130(2):462–464. doi: 10.3181/00379727-130-33580. [DOI] [PubMed] [Google Scholar]
  20. Shirahama T., Cohen A. S. Blockage of amyloid induction by colchicine in an animal model. J Exp Med. 1974 Oct 1;140(4):1102–1107. doi: 10.1084/jem.140.4.1102. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Skinner M., Shirahama T., Benson M. D., Cohen A. S. Murine amyloid protein AA in casein-induced experimental amyloidosis. Lab Invest. 1977 Apr;36(4):420–427. [PubMed] [Google Scholar]
  22. Westermark P., Skinner M., Cohen A. S. The P-component of amyloid of human islets of langerhans. Scand J Immunol. 1975;4(1):95–97. doi: 10.1111/j.1365-3083.1975.tb02604.x. [DOI] [PubMed] [Google Scholar]
  23. Zurier R. B., Hoffstein S., Weissmann G. Mechanisms of lysosomal enzyme release from human leukocytes. I. Effect of cyclic nucleotides and colchicine. J Cell Biol. 1973 Jul;58(1):27–41. doi: 10.1083/jcb.58.1.27. [DOI] [PMC free article] [PubMed] [Google Scholar]

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