PRION PROTEIN (PRP) IS NOT INVOLVED IN THE PATHOGENESIS OF SPONGIFORM ENCEPHALOPATHY IN ZITTER RATS

被引:11
作者
GOMI, H
IKEDA, T
KUNIEDA, T
ITOHARA, S
PRUSINER, SB
YAMANOUCHI, K
机构
[1] IMAMICHI INST ANIM REPROD,DEJIMA,IBARAKI,JAPAN
[2] UNIV CALIF SAN FRANCISCO,DEPT NEUROL,SAN FRANCISCO,CA 94143
[3] NIPPON INST BIOL SCI,OME,TOKYO,JAPAN
关键词
PRION PROTEIN; PRN; POLYMERASE CHAIN REACTION; SPONGIFORM ENCEPHALOPATHY; ZITTER RAT;
D O I
10.1016/0304-3940(94)90478-2
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
In order to elucidate the relationship between the prion protein (PrP) structure and the development of spongiform encephalopathy in titter rats, we analyzed the nucleotide sequences and restriction fragment length variation (RFLV) of the Pun gene encoding PrP in titter rats and inbred SD/J rats as a control. Prn genes from two strains had identical nucleotide sequences in their coding sequences. Obvious RFLV on the locus was not detected in titter rats by a Southern blot hybridization. Consistently, titter rat brains express the normal cellular PrP (PrPC), but do not accumulate the prelease-resistant modified isoform (PrPSC). These results indicate that PrP is not involved in the pathogenesis of spongiform encephalopathy in titter rats.
引用
收藏
页码:171 / 174
页数:4
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