Acta Neuropathologica

, Volume 58, Issue 4, pp 275–278 | Cite as

Permanganate oxidation of senile cerebral amyloid and its relationship to AA protein

  • J. M. Powers
  • L. Sullivan
  • C. J. Rosenthal
Original Works


Immunoreactivity for AA protein was rarely detected in briefly fixed amyloid of senile plaques and dyshoric angiopathy, but was not observed in Congophilic angiopathy. Plaque and dyshoric amyloid exhibited variable sensitivity to permanganate oxidation; Congophilic angiopathy was resistant to oxidation. In contrast to systemic amyloid composed of AA protein, the rare immunoreactivity of senile cerebral amyloid was lost with prolonged fixation. This study demonstrates that the fibrillar protein of senile cerebral amyloid differs from that of systemic amyloid of AA type.

Key words

AA protein Amyloid Oxidation Immunoperoxidase Senile brain 


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  1. Glenner GG (1979) Congophilic microangiopathy in the pathogenesis of Alzheimer's syndrome (pre-senile dementia). Med Hypothes 5:1231–1236Google Scholar
  2. Husby G, Natvig JB (1974) A serum component related to non-immunoglobulin amyloid protein AS, a possible precursor of the fibrils. J Clin Invest 53:1054–1061Google Scholar
  3. Ishii T, Haga S, Shimizu F (1975) Identification of components of immunoglobulins in senile plaques by means of fluorescent antibody technique. Acta Neuropathol (Berl) 32:157–162Google Scholar
  4. Levin M, Pras M, Franklin EC (1973) Immunologic studies of the major non-immunoglobulin amyloid protein of amyloid. J Exp Med 138:373–380Google Scholar
  5. Mason TE, Phifer RF, Spicer SS, Swallow RA, Dreskin RB (1969) An immunoglobulin enzyme bridge method for localizing tissue antigens. J Histochem Cytochem 17:563–569Google Scholar
  6. Morel F, Wildi E (1952) General and cellular pathochemistry of senile and presenile alterations of the brain. In: First international congress of neuropathology proceedings. Rosenberg and Sellier, Turin, pp 347–374Google Scholar
  7. Nikaido T, Austin J, Rinehart R, Trueb L, Hutchinson J, Stukenbrok H, Miles B (1971) Studies in aging of the brain. Isolation and preliminary characterization of Alzheimer plaques and cores. Arch Neurol 25:198–211Google Scholar
  8. Powers JM, Spicer SS (1977) Histochemical similarity of senile plaque amyloid to apudamyloid. Virchows Arch [Pathol Anat] 376:107–115Google Scholar
  9. Powers JM, Skeen JT (1980) An immunoperoxidase study of neuritic plaques. J Neuropathol Exp Neurol 39:385AGoogle Scholar
  10. Powers JM, Schlaepfer WW, Willingham MC, Hall BJ (1981) An immunoperoxidase study of senile cerebral amyloidosis with pathogenetic considerations. J Neuropathol Exp Neurol 40:592–612Google Scholar
  11. Probst A, Heitz PhU, Ulrich J (1980) Histochemical analysis of senile plaque amyloid and amyloid angiopathy. Virchows Arch [Pathol Anat] 388:327–334Google Scholar
  12. Puchtler H, Sweat F, Levine M (1962) On the binding of Congo red by amyloid. J Histochem Cytochem 10:355–364Google Scholar
  13. Rosenthal CJ, Franklin EC (1975) Variation with age and disease of an amyloid A protein-related serum component. J Clin Invest 55:746–753Google Scholar
  14. Schlaepfer WW, Hasler MB (1979) The persistence and possible externalization of axonal debris during Wallerian degeneration. J Neuropathol Exp Neurol 38:242–252Google Scholar
  15. Shirahama T, Skinner M, Cohen AS (1981) Immunocytochemical identification of amyloid in formalin-fixed paraffin sections. Histochemistry 72:161–171Google Scholar
  16. Shtrasburg S, Pras M, Langevitch P, Gal R (1982) Demonstration of AA-protein in formalin-fixed, paraffin-embedded tissues. Am J Pathol 106:141–144Google Scholar
  17. Sipe JD, Ignaczak TF, Pollock PS, Glenner GG (1976) Amyloid fibril protein AA: Purification and properties of the antigenically related serum component as determined by solid phase radioimmunoassay. J Immunol 116:1151–1156Google Scholar
  18. Stam FC (1965) Histochemistry of the senile involution of the brain. In: Luthy F, Bischoff A (eds) Fifth international congress of neuropathology proceedings. Excerpta Medica, Zürich, pp 513–517Google Scholar
  19. Stiller D, Katenkamp D (1975) Histochemistry of amyloid. Exp Pathol [Suppl] 1:7–116Google Scholar
  20. Torack RM, Lynch RG (1981) Cytochemistry of brain amyloid in adult dementia. Acta Neuropathol (Berl) 53:189–196Google Scholar
  21. Wright JR, Calkins E, Humphrey RL (1977) Potassium permanganate reaction in amyloidosis. A histologic method to assist in differentiating forms of this disease. Lab Invest 36:274–281Google Scholar
  22. van Rijswijk MH, van Heusden CWGJ (1979) The potassium permanganate method. A reliable method for differentiating amyloid AA from other forms of amyloid in routine laboratory practice. Am J Pathol 97:43–58Google Scholar

Copyright information

© Springer-Verlag 1982

Authors and Affiliations

  • J. M. Powers
    • 1
  • L. Sullivan
    • 2
  • C. J. Rosenthal
    • 3
  1. 1.Dept. of Pathology (Neuropathology)Medical University of South CarolinaCharlestonUSA
  2. 2.Dept. of Basic and Clinical Immunology and MicrobiologyMedical University of South CarolinaCharlestonUSA
  3. 3.Dept. of Medicine, Downstate Medical CenterState University of New YorkBrooklynUSA

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