Journal of Veterinary Diagnostic Investigation, Vol 14, Issue 3, 255-257
Copyright © 2002 by American Association of Veterinary Laboratory Diagnosticians
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
KM Kimura,
T Yokoyama,
M Haritani,
M Narita,
P Belleby,
J Smith,
and
YI Spencer
National Institute of Animal Health, Tsukuba, Ibaraki, Japan.
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.
