Acta Neuropathologica

, Volume 77, Issue 4, pp 337–342 | Cite as

Sulfated glycosaminoglycans in amyloid plaques of prion diseases

  • A. D. Snow
  • R. Kisilevsky
  • J. Willmer
  • S. B. Prusiner
  • S. J. DeArmond
Regular Papers


Brain sections from cases of human Creutzfeldt-Jakob disease, Gerstmann-Sträussler syndrome, kuru, and hamster scrapie containing amyloid were examined for the presence of sulfated glycosaminoglycans (GAGs), the anionic component of proteoglycans, using the sulfated Alcian blue method and Alcian blue technique with 0.3 M and 0.7 M magnesium chloride. These studies suggest that sulfated glycosaminoglycans are part of the CNS amyloid plaques in each of the above human prion disorders as well as in experimental scrapie. All the amyloid plaques stained positively with Alcian blue at 0.3 M, and less so at 0.7 M magnesium chloride indicating the presence of sulfated GAGs. Therefore, the amyloid plaques of prion diseases possess similar histochemical features to those found in Alzheimer's disease.

Key words

Amyloid Alzheimer's disease Glycosaminoglycans Proteoglycans Priom diseases 


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Copyright information

© Springer-Verlag 1989

Authors and Affiliations

  • A. D. Snow
    • 1
  • R. Kisilevsky
    • 1
  • J. Willmer
    • 1
  • S. B. Prusiner
    • 3
    • 4
  • S. J. DeArmond
    • 2
    • 3
  1. 1.Departments of Pathology and BiochemistryQueen's University and Kingston General HospitalKingstonCanada
  2. 2.Department of PathologyUniversity of CaliforniaSan Francisco
  3. 3.Department of NeurologyUniversity of CaliforniaSan Francisco
  4. 4.Department of Biochemistry and BiophysicsUniversity of CaliforniaSan Francisco

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