In Situ Detection of Cellular and Abnormal Isoforms of Prion Protein in Brains of Cattle with Bovine Spongiform Encephalopathy and Sheep with Scrapie by Use of a Histoblot Technique
Free accessRapid communicationFirst published online May, 2002
In Situ Detection of Cellular and Abnormal Isoforms of Prion Protein in Brains of Cattle with Bovine Spongiform Encephalopathy and Sheep with Scrapie by Use of a Histoblot Technique
To detect prion protein, brains from 5 cattle naturally affected with bovine spongiform encephalopathy (BSE) and 3 sheep naturally affected with scrapie were examined and compared with brains of normal cattle and sheep using a histoblot technique. The technique enabled the in situ distinctive detection of the cellular (PrPC) and abnormal (PrPSc) isoforms of the prion protein. In BSE- or scrapie-affected brains, the PrPC signal decreased, especially in those areas where the PrPSc signal was detected.
References
1.
HeggebøRPressCMGunnesG: 2000, Distribution of prion protein in the ileal Peyer's patch of scrapie-free lambs and lambs naturally and experimentally exposed to the scrapie agentJ Gen Virol81:2327–2337
2.
McBridePAEikelenboomPKraalGBruceME: 1992, PrP protein is associated with follicular dendritic cells of spleens and lymph nodes in uninfected and scrapie-infected miceJ Pathol168:413–418
3.
PrusinerSB: 1991, Molecular biology of prion diseasesScience252:1515–1522
4.
TaraboulosAJendroskaKSerbanD: 1992, Regional mapping of prion proteins in brainProc Natl Acad Sci USA89:7620–7624
5.
van KeulenLJMSchreuderBECMeloenRH: 1995, Immunohistochemical detection and localization of prion protein in brain tissue of sheep with natural scrapieVet Pathol32:299–308
6.
YokoyamaTKimuraKMUshikiY: 2001, In vivo conversion of cellular prion protein to pathogenic isoforms, as monitored by conformation-specific antibodiesJ Biol Chem276:11265–11271
