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 (PrP(C)) and abnormal (PrP(Sc)) isoforms of the prion protein. In BSE- or scrapie-affected brains, the Prp(C) signal decreased, especially in those areas where the PrP(Sc) signal was detected.
Kimura
Kumiko M
KM
National Institute of Animal Health, Tsukuba, Ibaraki, Japan.
Yokoyama
Takashi
T
Haritani
Makoto
M
Narita
Minoru
M
Belleby
Peter
P
Smith
Julie
J
Spencer
Yvonne I
YI
D000818:Animals; D001921:Brain / Q000473:pathology; D002417:Cattle; D016643:Encephalopathy, Bovine Spongiform / Q000175:diagnosis* / Q000473:pathology; D007150:Immunohistochemistry / Q000379:methods*; D011328:Prions / Q000032:analysis*; D020033:Protein Isoforms / Q000032:analysis; D012608:Scrapie / Q000175:diagnosis* / Q000473:pathology; D012680:Sensitivity and Specificity; D012756:Sheep
D011328:Prions; D020033:Protein Isoforms