Prion protein (PrP) is not involved in the pathogenesis of spongiform encephalopathy in zitter rats

Hiroshi Gomi; Toshio Ikeda; Tetsuo Kunieda; Shigeyoshi Itohara; Stanley B. Prusiner; Kazuya Yamanouchi

doi:10.1016/0304-3940(94)90478-2

Prion protein (PrP) is not involved in the pathogenesis of spongiform encephalopathy in zitter rats

Hiroshi Gomi, Toshio Ikeda, Tetsuo Kunieda, Shigeyoshi Itohara, Stanley B. Prusiner, Kazuya Yamanouchi

Research output: Contribution to journal › Article

12 Citations (Scopus)

Abstract

In order to elucidate the relationship between the prion protein (PrP) structure and the development of spongiform encephalopathy in zitter rats, we analyzed the nucleotide sequences and restriction fragment length variation (RFLV) of the Prn gene encoding PrP in zitter 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 zitter rats by a Southern blot hybridization. Consistently, zitter rat brains express the normal cellular PrP (PrP^C), but do not accumulate the protease-resistant modified isoform (PrP^SC). These results indicate that PrP is not involved in the pathogenesis of spongiform encephalopathy in zitter rats.

Original language	English
Pages (from-to)	171-174
Number of pages	4
Journal	Neuroscience Letters
Volume	166
Issue number	2
DOIs	https://doi.org/10.1016/0304-3940(94)90478-2
Publication status	Published - Jan 31 1994
Externally published	Yes

Keywords

Polymerase chain reaction
Prion protein
Prn
Spongiform encephalopathy
Zitter rat

ASJC Scopus subject areas

Neuroscience(all)

Access to Document

10.1016/0304-3940(94)90478-2

Fingerprint Dive into the research topics of 'Prion protein (PrP) is not involved in the pathogenesis of spongiform encephalopathy in zitter rats'. Together they form a unique fingerprint.

Cite this

@article{eddd1768ad994fc594814f3dad8999c3,

title = "Prion protein (PrP) is not involved in the pathogenesis of spongiform encephalopathy in zitter rats",

abstract = "In order to elucidate the relationship between the prion protein (PrP) structure and the development of spongiform encephalopathy in zitter rats, we analyzed the nucleotide sequences and restriction fragment length variation (RFLV) of the Prn gene encoding PrP in zitter 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 zitter rats by a Southern blot hybridization. Consistently, zitter rat brains express the normal cellular PrP (PrPC), but do not accumulate the protease-resistant modified isoform (PrPSC). These results indicate that PrP is not involved in the pathogenesis of spongiform encephalopathy in zitter rats.",

keywords = "Polymerase chain reaction, Prion protein, Prn, Spongiform encephalopathy, Zitter rat",

author = "Hiroshi Gomi and Toshio Ikeda and Tetsuo Kunieda and Shigeyoshi Itohara and Prusiner, {Stanley B.} and Kazuya Yamanouchi",

year = "1994",

month = jan,

day = "31",

doi = "10.1016/0304-3940(94)90478-2",

language = "English",

volume = "166",

pages = "171--174",

journal = "Neuroscience Letters",

issn = "0304-3940",

publisher = "Elsevier Ireland Ltd",

number = "2",

}

TY - JOUR

T1 - Prion protein (PrP) is not involved in the pathogenesis of spongiform encephalopathy in zitter rats

AU - Gomi, Hiroshi

AU - Ikeda, Toshio

AU - Kunieda, Tetsuo

AU - Itohara, Shigeyoshi

AU - Prusiner, Stanley B.

AU - Yamanouchi, Kazuya

PY - 1994/1/31

Y1 - 1994/1/31

N2 - In order to elucidate the relationship between the prion protein (PrP) structure and the development of spongiform encephalopathy in zitter rats, we analyzed the nucleotide sequences and restriction fragment length variation (RFLV) of the Prn gene encoding PrP in zitter 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 zitter rats by a Southern blot hybridization. Consistently, zitter rat brains express the normal cellular PrP (PrPC), but do not accumulate the protease-resistant modified isoform (PrPSC). These results indicate that PrP is not involved in the pathogenesis of spongiform encephalopathy in zitter rats.

AB - In order to elucidate the relationship between the prion protein (PrP) structure and the development of spongiform encephalopathy in zitter rats, we analyzed the nucleotide sequences and restriction fragment length variation (RFLV) of the Prn gene encoding PrP in zitter 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 zitter rats by a Southern blot hybridization. Consistently, zitter rat brains express the normal cellular PrP (PrPC), but do not accumulate the protease-resistant modified isoform (PrPSC). These results indicate that PrP is not involved in the pathogenesis of spongiform encephalopathy in zitter rats.

KW - Polymerase chain reaction

KW - Prion protein

KW - Prn

KW - Spongiform encephalopathy

KW - Zitter rat

UR - http://www.scopus.com/inward/record.url?scp=0027979911&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027979911&partnerID=8YFLogxK

U2 - 10.1016/0304-3940(94)90478-2

DO - 10.1016/0304-3940(94)90478-2

M3 - Article

C2 - 7909925

AN - SCOPUS:0027979911

VL - 166

SP - 171

EP - 174

JO - Neuroscience Letters

JF - Neuroscience Letters

SN - 0304-3940

IS - 2

ER -