scholarly journals Human prion disease

2020 ◽  
Author(s):  
Keyword(s):  
Prion Disease ◽  
Human Prion Disease

Loss of glycosylation associated with the T183A mutation in human prion disease

2004 ◽  
Vol 108 (6) ◽  
pp. 476-484 ◽  
Author(s):  
E. Grasbon-Frodl ◽  
Holger Lorenz ◽  
U. Mann ◽  
R. M. Nitsch ◽  
Otto Windl ◽  
...  
Keyword(s):  
Prion Disease ◽  
Human Prion Disease

Molecular, Genetic and Transgenetic Studies of Human Prion Disease

1998 ◽  
pp. 303-304
Author(s):  
J. Collinge ◽  
J. Beck ◽  
T. A. Campbell ◽  
M. Desbuslais ◽  
I. Gowland ◽  
...  
Keyword(s):  
Prion Disease ◽  
Molecular Genetic ◽  
Human Prion Disease

scholarly journals Genetic human prion disease modelled in PrP transgenic Drosophila

2017 ◽  
Vol 474 (19) ◽  
pp. 3253-3267 ◽  
Author(s):  
Alana M. Thackray ◽  
Alzbeta Cardova ◽  
Hanna Wolf ◽  
Lydia Pradl ◽  
Ina Vorberg ◽  
...  
Keyword(s):  
Prion Protein ◽  
Prion Disease ◽  
Prion Diseases ◽  
Principal Component ◽  
Site Directed Mutagenesis ◽  
Host Protein ◽  
Therapeutic Interventions ◽  
Proteinase K ◽  
Human Prion Disease ◽  
Transgenic Drosophila

Inherited human prion diseases, such as fatal familial insomnia (FFI) and familial Creutzfeldt–Jakob disease (fCJD), are associated with autosomal dominant mutations in the human prion protein gene PRNP and accumulation of PrPSc, an abnormal isomer of the normal host protein PrPC, in the brain of affected individuals. PrPSc is the principal component of the transmissible neurotoxic prion agent. It is important to identify molecular pathways and cellular processes that regulate prion formation and prion-induced neurotoxicity. This will allow identification of possible therapeutic interventions for individuals with, or at risk from, genetic human prion disease. Increasingly, Drosophila has been used to model human neurodegenerative disease. An important unanswered question is whether genetic prion disease with concomitant spontaneous prion formation can be modelled in Drosophila. We have used pUAST/PhiC31-mediated site-directed mutagenesis to generate Drosophila transgenic for murine or hamster PrP (prion protein) that carry single-codon mutations associated with genetic human prion disease. Mouse or hamster PrP harbouring an FFI (D178N) or fCJD (E200K) mutation showed mild Proteinase K resistance when expressed in Drosophila. Adult Drosophila transgenic for FFI or fCJD variants of mouse or hamster PrP displayed a spontaneous decline in locomotor ability that increased in severity as the flies aged. Significantly, this mutant PrP-mediated neurotoxic fly phenotype was transferable to recipient Drosophila that expressed the wild-type form of the transgene. Collectively, our novel data are indicative of the spontaneous formation of a PrP-dependent neurotoxic phenotype in FFI- or CJD-PrP transgenic Drosophila and show that inherited human prion disease can be modelled in this invertebrate host.

scholarly journals Human Prion Disease and Relative Risk Associated with Chronic Wasting Disease

2006 ◽  
Vol 12 (10) ◽  
pp. 1527-1535 ◽  
Author(s):  
Samantha MaWhinney ◽  
W. John Pape ◽  
Jeri E. Forster ◽  
C. Alan Anderson ◽  
Patrick Bosque ◽  
...  
Keyword(s):  
Relative Risk ◽  
Prion Disease ◽  
Chronic Wasting Disease ◽  
Human Prion Disease ◽  
Wasting Disease

scholarly journals BSE and human prion disease

1997 ◽  
Vol 170 (4) ◽  
pp. 298-300 ◽  
Author(s):  
Paul J. Harrison
Keyword(s):  
Prion Disease ◽  
Human Prion Disease
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