Immunolocalization of Heparan Sulfate Proteoglycans to AA Amyloid Deposition Sites in Spleen and Liver During Experimental Amyloidosis

  • Alan D. Snow
  • Robert Kisilevsky
  • Thomas N. Wight


Our previous histochemical studies have demonstrated that during experimental AA amyloidosis a close time relationship exists between initial amyloid and glycosaminoglycan (GAG) accumulation, regardless of the induction protocol used, tissue concerned or length of induction (13). Use of the Alcian blue — magnesium chloride staining technique (11) additionally suggested that highly sulfated GAGs were involved (13), Recent qualitative and quantitative biochemical investigations (14) have confirmed the close temporal relationship between initial amyloid and GAG deposition, and have identified heparan sulfate and heparin as the two major GAGs which accumulate in mouse spleen during experimental AA amyloidosis, a process which did not occur during acute inflammation.


Heparan Sulfate Alcian Blue Amyloid Fibril Heparan Sulfate Proteoglycan Sulfated GAGs 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    M.A. Axelrad, R. Kisilevsky, J. Willmer, S.J. Chen, and M. Skinner, Further characterization of amyloid-enhancing factor, Lab Invest 47:139 (1982).Google Scholar
  2. 2.
    J.R. Hassel1, P.G. Robey, H. Barrach, J. Wilczek, S. Rennard and G.R. Martin, Isolation of a heparan sulfate-containing proteoglycan from basement membrane, Proc Natl Acad Sc 77:4494 (1980).CrossRefGoogle Scholar
  3. 3.
    J.R. Hassell, U.C. Leyshon, S.R. Ledbetter, B. Tyree, S. Suzukil, M. Kato, K. Kimata, and K. Kleinman, Isolation of two forms of basement membrane proteoglycans, J Biol Chem 260:8098 (1985).Google Scholar
  4. 4.
    D.T. Janigan and R.L. Druet, Experimental amyloidosis. Role of antigenicity and rapid induction, Am J Path 48:1013 (1966).Google Scholar
  5. 5.
    E.P. Katz, E.J. Watchel, and A. Marovdas, Extrafibrillar proteoglycans osmotically regulate the molecular packing of collagen in cartilage, Bioch Biophys Acta 882:136 (1986).CrossRefGoogle Scholar
  6. 6.
    A. Linker and H.C. Carney, Presence and role of glycosaminoglycans in amyloidosis, Lab Invest 57:297 (1987).Google Scholar
  7. 7.
    M.B. Mathews, and L. Decker, The effect of acid mucopolysaccharides on fibril formation from collagen solutions, Biochem J 109:517 (1968).Google Scholar
  8. 8.
    D.B. Myers, T.C. Highton, and D.G. Ryans, Acid mucopolysaccharides closely associated with collagen fibrils in normal human synovium, Ultrastr Res 28:203 (1969).CrossRefGoogle Scholar
  9. 9.
    B. Obrink, The influence of glycosarainoglycans on the formation of fibers from monomeric tropocollagen in vitro, Eur J Biochem 31:129 (1973).CrossRefGoogle Scholar
  10. 10.
    H. Puchtler, F. Sweat, and M. Levine, On the binding of Congo red by amyloid, J Histochem Cytochem 10:355 (1962).CrossRefGoogle Scholar
  11. 11.
    J.E. Scott and J. Dorling, Differential staining of acid glycosaminoglycans (mucopolysaccharides) by alcian blue in salt solutions, Histochem 5:221 (1965).CrossRefGoogle Scholar
  12. 12.
    J.E. Scott, Collagen-proteoglycan interactions. Localization of proteoglycans in tendon by electron microscopy, Biochem J 187:887 (1980).Google Scholar
  13. 13.
    A.D. Snow and R. Kisilevsky, Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis. A histochemical study, Lab Invest 53:37 (1985).Google Scholar
  14. 14.
    A.D. Snow, R. Kisilevsky, C. Stephens and T. Anastassiades, Characterization of tissue and plasma glycosaminoglycans during experimental AA amyloidosis and acute inflammation. Qualitative and quantitative analysis, Lab Invest 56:665 (1987).Google Scholar
  15. 15.
    A.D. Snow, J. Willmer and R. Kisilevsky, Sulfated glycosaminoglycans: a common constituent of all amyloids? Lab Invest 56:120 (1987).Google Scholar
  16. 16.
    A.D. Snow, J. Willmer and R. Kisilevsky, A close ultrastructural relationship between sulfated proteoglycans and AA amyloid fibrils, Lab Invest 57:687 (1987).Google Scholar
  17. 17.
    L.A. Sternberger. Immunohistochemistry, in: “Immunohistochemistry”, Third Edition, John Wiley & Sons, N.Y. (1986).Google Scholar
  18. 18.
    A.L. Stone, Optical conformation of heparin and heparin complexes with cationic dyes, amines and protein models. Fed Proc 36:101 (1977).Google Scholar
  19. 19.
    P Whitaker, D.R. Roughner, D.G. Perkins, and P.B. Canham, Quantitative structural analysis of collagen in chordae tendineae and its relation to floppy mitral valves and proteoglycan infiltration. Br Heart J 57:264 (1987).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Alan D. Snow
    • 1
  • Robert Kisilevsky
    • 1
    • 2
  • Thomas N. Wight
    • 1
  1. 1.Department of PathologyUniversity of WashingtonSeattleUSA
  2. 2.Department of PathologyQueen’s UniversityKingstonCanada

Personalised recommendations