Hydrated autoclave pretreatment enhancement of prion protein immunoreactivity in formalin-fixed bovine spongiform encephalopathy-affected brain
- 103 Downloads
The efficacy of three pretreatment techniques for the detection of prion protein (PrP) in formalin-fixed, paraffin-embedded bovine spongiform encephalopathy (BSE)-affected brain tissue were compared using automated image analysis. The most abundant immunostaining was in the form of particulate expression observed in sections pretreated with hydrated autoclaving for 30 min. Considerably less immunostaining occurred in sections pretreated with formic acid and no specific particulate immunostaining was detected in sections pretreated with hydrolytic autoclaving. Hydrated autoclaving pretreatment of sections prior to PrP immunolabelling gives visualisation of widespread sites of abnormal PrP deposition in the brain, allowing detailed study of the form and distribution of the protein in routinely fixed bovine central nervous system affected with BSE.
Key wordsImmunohistochemistry Medulla oblongata Prion protein (PrP) Bovine spongiform encephalopathy Formalin-fixed tissue
Unable to display preview. Download preview PDF.
- 1.Bell JE, Ironside JW (1993) Neuropathology of spongiform encephalopathies in humans. Br Med Bull (in press)Google Scholar
- 2.Bradley R, Matthews D (1992) Sub-acute, transmissible spongiform encephalopathies: current concepts and future needs. Rev Sci Tech Off Int Epiz 11: 605–634Google Scholar
- 4.Dawson M, Mansley LM, Hunter AR, Stack MJ, Scott AC (1987) Comparison of scrapie associated fibril detection and histology in diagnosis of natural sheep scrapie. Vet Rec 121: 591Google Scholar
- 12.Kimberlin RH (1992) Bovine spongiform encephalopathy. Rev Sci Tech Off Int Epiz 11: 347–390Google Scholar
- 26.Sternberger LA, Hardy PH Jr, Cuculis JJ, Meyer HG (1970) The unlabelled antibody enzyme method of immunohistochemistry preparation and properties of soluble antigen-antibody complex horseradish-D peroxidase anti-horseradish-D peroxidase and its use in the identification of spirochetes. J Histochem Cytochem 18: 315–333PubMedGoogle Scholar
- 31.Wells GAH, Hawkins SAC, Hadlow WJ, Spencer YI (1992) The discovery of bovine spongiform encephalopathy and observations on the vacuolar changes. In: Prusiner SB, Collinge J, Powell J, Anderton B (eds) Prion disease of humans and animals. Ellis-Horwood, Chichester, pp 256–274Google Scholar