Identification of new allelic variants in the ovine prion protein (PrP) gene

2002 ◽  
Vol 119 (4) ◽  
pp. 201-208 ◽  
Author(s):  
T. KUTZER ◽  
I. PFEIFFER ◽  
B. BRENIG
Keyword(s):  
Prion Protein ◽  
Allelic Variants ◽  
Prp Gene

scholarly journals Prion protein gene polymorphisms in healthy and scrapie-affected sheep in Greece

2004 ◽  
Vol 85 (2) ◽  
pp. 547-554 ◽  
Author(s):  
Charalambos Billinis ◽  
Vassilios Psychas ◽  
Leonidas Leontides ◽  
Vassiliki Spyrou ◽  
Stamatis Argyroudis ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Denaturing Gradient Gel Electrophoresis ◽  
Gradient Gel Electrophoresis ◽  
Healthy Control ◽  
The Moment ◽  
Chios Sheep ◽  
Prp Gene ◽  
Control Study ◽  
Clinical Cases

A total of 216 local crossbred sheep from 16 scrapie-affected Greek flocks and 210 purebred sheep of the milk breeds Chios and Karagouniko from healthy flocks were analysed for scrapie-linked polymorphisms in the prion protein (PrP) gene. Of the 216 sheep in this case–control study, 96 sheep were clinical cases, 25 subclinical cases (asymptomatic at the moment of euthanasia but positive by histopathology and/or ELISA detecting proteinase-resistant PrP) and 95 healthy controls (negative by all evaluations). Polymorphisms at codons 136, 154 and 171 were determined by denaturing gradient gel electrophoresis, followed by RFLP and sequencing. Scrapie, both clinical and subclinical, was associated with the genotypes ARQ/ARQ (88 of 110 sheep of that genotype), ARQ/TRQ (9 of 13), ARQ/AHQ (15 of 38) and VRQ/VRQ (9 of 17). Histopathological lesions were more severe in the clinical cases. Genotypes ARQ/ARR (26 sheep), ARQ/ARK (seven sheep), AHQ/ARR (one sheep), ARH/ARH (one sheep) and ARR/ARH (three sheep) were detected exclusively in healthy control sheep. In the purebred survey, four genotypes were present in the Chios sheep (ARQ/ARQ, ARQ/TRQ, ARQ/AHQ and ARQ/ARR) and four in the Karagouniko sheep (ARQ/ARQ, ARQ/AHQ, ARQ/ARR and ARQ/ARH).

scholarly journals Serum Withdrawal-Induced Apoptosis in ZrchI Prion Protein (PrP) Gene-Deficient Neuronal Cell Line Is Suppressed by PrP, Independent of Doppel

2007 ◽  
Vol 51 (4) ◽  
pp. 457-466 ◽  
Author(s):  
Takuya Nishimura ◽  
Akikazu Sakudo ◽  
Yoriko Hashiyama ◽  
Akiko Yachi ◽  
Keiichi Saeki ◽  
...  
Keyword(s):  
Cell Line ◽  
Prion Protein ◽  
Neuronal Cell ◽  
Neuronal Cell Line ◽  
Serum Withdrawal ◽  
Induced Apoptosis ◽  
Prp Gene

Cloning and expression of a prion protein (PrP) gene from Korean bovine (Bos taurus coreanae) and production of rabbit anti-bovine PrP antibody

2008 ◽  
Vol 30 (10) ◽  
pp. 1705-1711 ◽  
Author(s):  
Wooseok Shin ◽  
Byungwoo Lee ◽  
Sungyoul Hong ◽  
Chongsuk Ryou ◽  
Moosik Kwon
Keyword(s):  
Prion Protein ◽  
Bos Taurus ◽  
Cloning And Expression ◽  
Prp Gene

scholarly journals The prion protein gene: a role in mouse embryogenesis?

Development ◽  
1992 ◽  
Vol 115 (1) ◽  
pp. 117-122 ◽  
Author(s):  
J. Manson ◽  
J.D. West ◽  
V. Thomson ◽  
P. McBride ◽  
M.H. Kaufman ◽  
...  
Keyword(s):  
Gene Expression ◽  
Nervous System ◽  
Prion Protein ◽  
In Situ Hybridisation ◽  
Neuronal Cell ◽  
Normal Function ◽  
Cell Populations ◽  
Specific Expression ◽  
The Brain ◽  
Prp Gene

The neural membrane glycoprotein PrP (prion protein) has a key role in the development of scrapie and related neurodegenerative diseases. During pathogenesis, PrP accumulates in and around cells of the brain from which it can be isolated in a disease-specific, protease-resistant form. Although the involvement of PrP in the pathology of these diseases has long been known, the normal function of PrP remains unknown. Previous studies have shown that the PrP gene is expressed tissue specifically in adult animals, the highest levels in the brain, with intermediate levels in heart and lung and low levels in spleen. Prenatally, PrP mRNA has been detected in the brain of rat and hamster just prior to birth. In this study we have examined the expression of the PrP gene during mouse embryonic development by in situ hybridisation and observed dramatic regional and temporal gene expression in the embryo. Transcripts were detected in developing brain and spinal cord by 13.5 days. In addition, PrP gene expression was detected in the peripheral nervous system, in ganglia and nerve trunks of the sympathetic nervous system and neural cell populations of sensory organs. Expression of the PrP gene was not limited to neuronal cells, but was also detected in specific non-neuronal cell populations of the 13.5 and 16.5 day embryos and in extra-embryonic tissues from 6.5 days. This cell-specific expression suggests a pleiotropic role for PrP during development.

Deletion of the α(1,3)galactosyl transferase (GGTA1) gene and the prion protein (PrP) gene in sheep

10.1038/89313 ◽  
2001 ◽  
Vol 19 (6) ◽  
pp. 559-562 ◽  
Author(s):  
C. Denning ◽  
S. Burl ◽  
A. Ainslie ◽  
J. Bracken ◽  
A. Dinnyes ◽  
...  
Keyword(s):  
Prion Protein ◽  
Galactosyl Transferase ◽  
Prp Gene

A simple and rapid method for sequencing the entire coding region of the human prion protein (PrP) gene

1994 ◽  
Vol 54 (1) ◽  
pp. 103-107 ◽  
Author(s):  
François Boussi ◽  
Alexandre Jaegly ◽  
Jean-Philippe Deslys ◽  
Dominique Dormont
Keyword(s):  
Prion Protein ◽  
Rapid Method ◽  
Coding Region ◽  
Human Prion Protein ◽  
Prp Gene

scholarly journals An Alul RFLP detected in human the human prion protein (PrP) gene

1990 ◽  
Vol 18 (2) ◽  
pp. 385-385
Author(s):  
Marsha S. Harris ◽  
Evelyn Devine-Gage ◽  
Nikolaos Robakis
Keyword(s):  
Prion Protein ◽  
Human Prion Protein ◽  
Prp Gene

scholarly journals Sheep scrapie susceptibility-linked polymorphisms do not modulate the initial binding of cellular to disease-associated prion protein prior to conversion

2005 ◽  
Vol 86 (9) ◽  
pp. 2627-2634 ◽  
Author(s):  
Alan Rigter ◽  
Alex Bossers
Keyword(s):  
Prion Protein ◽  
Transmissible Spongiform Encephalopathy ◽  
Cellular Prion Protein ◽  
Transmissible Spongiform Encephalopathies ◽  
Second Step ◽  
Spongiform Encephalopathy ◽  
Differential Rate ◽  
Allelic Variants ◽  
Scrapie Susceptibility ◽  
Initial Binding

Conversion of the host-encoded protease-sensitive cellular prion protein (PrPC) into the scrapie-associated protease-resistant isoform (PrPSc) of prion protein (PrP) is the central event in transmissible spongiform encephalopathies or prion diseases. Differences in transmissibility and susceptibility are largely determined by polymorphisms in PrP, but the exact molecular mechanism behind PrP conversion and the modulation by disease-associated polymorphisms is still unclear. To assess whether the polymorphisms in either PrPC or PrPSc modulate the initial binding of PrPC to PrPSc, several naturally occurring allelic variants of sheep PrPC and PrPSc that are associated with differential scrapie susceptibility and transmissibility [the phylogenetic wild-type (ARQ), the codon 136Val variant (VRQ) and the codon 171Arg variant (ARR)] were used. Under cell-free PrP conversion conditions known to reproduce the observed in vivo differential scrapie susceptibility, it was found that the relative amounts of PrPC allelic variants bound by various allelic PrPSc variants are PrP-specific and have comparable binding efficiencies. Therefore, the differential rate-limiting step in conversion of sheep PrP variants is not determined by the initial PrPC–PrPSc-binding efficiency, but seems to be an intrinsic property of PrPC itself. Consequently, a second step after PrPC–PrPSc-binding should determine the observed differences in PrP conversion efficiencies. Further study of this second step may provide a future tool to determine the mechanism underlying refolding of PrPC into PrPSc and supports the use of conversion-resistant polymorphic PrPC variants as a potential therapeutic approach to interfere with PrP conversion in transmissible spongiform encephalopathy development.

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