1994年1月
Prion protein (PrP) is not involved in the pathogenesis of spongiform encephalopathy in zitter rats
Neuroscience Letters
- ,
- ,
- ,
- ,
- ,
- 巻
- 166
- 号
- 2
- 開始ページ
- 171
- 終了ページ
- 174
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- 出版者・発行元
- ELSEVIER SCI IRELAND LTD
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.
- リンク情報
- ID情報
-
- ISSN : 0304-3940
- Web of Science ID : WOS:A1994MX72800013