Deposition of Amyloid a Fibrils in Spleen is Accompanied by Decreased Hepatic and Splenic and Increased Macrophage Serum Amyloid a Expression

  • Jean D. Sipe
  • Hanna Rokita
  • Tsuranobu Shirahama
  • Alan S. Cohen


Amyloidosis is an occasional sequela to long standing inflammation. The origin of the disorder is multifactorial; the etiology and the duration of inflammation, structure of the serum amyloid A (SAA) precursor, and genetic background of the host are all thought to contribute to amyloid deposition (1-4).


Peritoneal Macrophage Serum Amyloid Guanidinium Isothiocyanate Amyloid Enhance Factor Acute Phase Serum Amyloid 
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  1. 1.
    G. G. Glenner, Amyloid deposits and amyloidosis: The Bfibrilloses. N. Eng. J. Med. 302:1283 (1980).CrossRefGoogle Scholar
  2. 2.
    A. S. Cohen, General introduction and a brief history of amyloidosis, In “Amyloidosis” J. Marrink and M. H. van Rijswijk, ed., Martinus Nijhoff Publishers Dordrecht, The Netherlands, pp. 3–19(1986).CrossRefGoogle Scholar
  3. 3.
    E. P. Benditt, N. Eriksen, M.A. Hermodson, and L.H. Ericcson, The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences. FEBS Lett. 19:169 (1971).CrossRefGoogle Scholar
  4. 4.
    J. R. Wohlgethan and E. S. Cathcart, Amyloid resistance in A/J mice is determined by a single gene. Nature 278:453 (1979).CrossRefGoogle Scholar
  5. 5.
    R. Kisilevsky, Amyloidosis: A familiar problem in the light of current pathogenetic developments. Lab. Invest. 49:381 (1983).Google Scholar
  6. 6.
    J. D. Sipe, K. P. W. J. McAdam, and F. Uchino, Biochemical evidence for the biphasic development of experimental amyloidosis. Lab. Invest. 38:110 (1978).Google Scholar
  7. 7.
    G. Teilung Pathogenesis of amyloidosis: the two phase cellular theory of local secretion, Acta Pathol. Microbiol. Scand. 61:21 (1964).Google Scholar
  8. 8.
    M. A. Axelrad, R. Kisilevsky, J. Willmer, S.J. Chen and M. Skinner, Further characterization of amyloidenhancing factor. Lab. Invest. 47:139 (1982).Google Scholar
  9. 9.
    F. Hardt and P. Ranlovf Transfer amyloidosis. Internat. Rev. Exp. Pathol. 16:273, 1976.Google Scholar
  10. 10.
    C. L. Deal, J. D. Sipe, E. Tatsuta, M. Skinner and A. S. Cohen, The effect of amyloid enhancing factor (AEF) on the acute phase serum amyloid A (SAA) and serum amyloid P (SAP) response to silver nitrate. Ann. N.Y. Acad. Sci. 389:439, (1982).CrossRefGoogle Scholar
  11. 11.
    G. Ramadori, J. D. Sipe, and H.R. Colten, Expression and regulation of the murine serum amyloid A (SAA) gene in extrahepatic sites. J. Immunol. 135:3645 (1985).Google Scholar
  12. 12.
    R. L. Meek and E. P. Benditt, Amyloid A gene family expression in different mouse tissues, J. Exp. Med. 164:2006 (1986).CrossRefGoogle Scholar
  13. 13.
    H. Rokita, T. Shirahama, A.S. Cohen, R.L. Meek, E.P. Benditt and J.D. Sipe, Differential expression of the amyloid SAA 3 gene in liver and peritoneal macrophages of mice undergoing dissimilar inflammatory episodes, J. Immunol. In press, (1987).Google Scholar
  14. 14.
    H. Puchtler, F. Sweat, and M. Levine, On the binding of Congo red by amyloid, J. Histochem. Cytochem. 10:355, (1962).CrossRefGoogle Scholar
  15. 15.
    J. D. Sipe, T. F. Ignaczak, P. S. Pollock, and G.G. Glenner, Amyloid fibril protein AA: Purification and properties of the antigenically related serum component as determined by solid phase radioimmunoassay, J. Immunol. 116:1151, (1976).Google Scholar
  16. 16.
    J. M. Chirgwin, A. E. Przybyla, R. J. MacDonald, and W. J. Rutter, Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease, Biochemistry 18:5294 (1979).CrossRefGoogle Scholar
  17. 17.
    J. D. Sipe, H. R. Colten, G. Goldberger, M. D. Edge, B. F. Tack, A. S. Cohen, and A. S. Whitehead, Human serum amyloid A (SAA): Biosynthesis and post synthetic processing of preSAA and structural variants defined by complementary DNA, Biochemistry 24:2931, (1985).Google Scholar
  18. 18.
    A. D. Snow, J. Willmer and R. Kisilevsky, Sulfated glycosaminoglycans: A common constituent of all amyloids, Lab. Invest. 56:120, (1987).Google Scholar
  19. 19.
    J. D. Sipe, H. Rokita, T. Shirahama, A. Cohen and A. Koj, Analysis of SAA gene expression during acute inflammation and accelerated amyloidogenesis. Coll. Protides Biol. Fluids 34:331 (1986).Google Scholar
  20. 20.
    G. Ramadori, H. Rieder, A. Mitch, J. Sipe, Synthesis and secretion of serum amyloid A (SAA) by mouse hepatocytes and Kupffer cells, Coll. Protides Biol. Fluids 34:383 (1986).Google Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Jean D. Sipe
    • 1
  • Hanna Rokita
    • 1
  • Tsuranobu Shirahama
    • 1
  • Alan S. Cohen
    • 1
  1. 1.Arthritis CenterBoston University School of MedicineBostonUSA

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