Immunohistochemical study of kuru plaques using antibodies against synthetic prion protein peptides

1992 ◽  
Vol 83 (6) ◽  
pp. 613-617 ◽  
Author(s):  
Kouichi Hashimoto ◽  
Toru Mannen ◽  
Nobuyuki Nukina
Keyword(s):  
Prion Protein ◽  
Immunohistochemical Study ◽  
Kuru Plaques

Creutzfeldt-Jakob disease patients with congophilic kuru plaques have the missense variant prion protein common to Gerstmann-Sträussler syndrome

1990 ◽  
Vol 27 (2) ◽  
pp. 121-126 ◽  
Author(s):  
Katsumi Doh-Ura ◽  
Jun Tateishi ◽  
Tetsuyuki Kitamoto ◽  
Hiroyuki Sasaki ◽  
Yoshiyuki Sakaki
Keyword(s):  
Prion Protein ◽  
Missense Variant ◽  
Jakob Disease ◽  
Kuru Plaques

Distinct immunohistochemical localization in Kuru plaques using novel anti-prion protein antibodies

2008 ◽  
Vol 52 (1) ◽  
pp. 25-29 ◽  
Author(s):  
Tomoko Hosokawa ◽  
Fumiko Ono ◽  
Kotaro Tsuchiya ◽  
Ichiro Sato ◽  
Natsumi Takeyama ◽  
...  
Keyword(s):  
Prion Protein ◽  
Immunohistochemical Localization ◽  
Kuru Plaques

N-terminal sequence of prion protein is also intergrated into kuru plaques in patients with Gerstmann-Stra¨ussler syndrome

1991 ◽  
Vol 545 (1-2) ◽  
pp. 319-321 ◽  
Author(s):  
Tetsuyuki Kitamoto ◽  
Tamaki Muramoto ◽  
Caroline Hilbich ◽  
Konrad Beyreuther ◽  
Jun Tateishi
Keyword(s):  
Prion Protein ◽  
Terminal Sequence ◽  
Kuru Plaques

Species-specificity of a Panel of Prion Protein Antibodies for the Immunohistochemical Study of Animal and Human Prion Diseases

2007 ◽  
Vol 136 (1) ◽  
pp. 9-17 ◽  
Author(s):  
H. Furuoka ◽  
A. Yabuzoe ◽  
M. Horiuchi ◽  
Y. Tagawa ◽  
T. Yokoyama ◽  
...  
Keyword(s):  
Prion Protein ◽  
Immunohistochemical Study ◽  
Prion Diseases ◽  
Species Specificity

Expression of the prion protein in the rat forebrain – an immunohistochemical study

1999 ◽  
Vol 272 (1) ◽  
pp. 9-12 ◽  
Author(s):  
Susan Verghese–Nikolakaki ◽  
Helen Michaloudi ◽  
Magdalini Polymenidou ◽  
Martin H Groschup ◽  
Georgios C Papadopoulos ◽  
...  
Keyword(s):  
Prion Protein ◽  
Immunohistochemical Study ◽  
Rat Forebrain

Metallic prions

2004 ◽  
Vol 71 ◽  
pp. 193-202 ◽  
Author(s):  
David R Brown
Keyword(s):  
Prion Protein ◽  
Binding Capacity ◽  
Normal Function ◽  
Transmissible Spongiform Encephalopathies ◽  
Published Data ◽  
Normal Brain ◽  
Copper Binding ◽  
Loss Of Function ◽  
Spongiform Encephalopathies ◽  
The Brain

Prion diseases, also referred to as transmissible spongiform encephalopathies, are characterized by the deposition of an abnormal isoform of the prion protein in the brain. However, this aggregated, fibrillar, amyloid protein, termed PrPSc, is an altered conformer of a normal brain glycoprotein, PrPc. Understanding the nature of the normal cellular isoform of the prion protein is considered essential to understanding the conversion process that generates PrPSc. To this end much work has focused on elucidation of the normal function and activity of PrPc. Substantial evidence supports the notion that PrPc is a copper-binding protein. In conversion to the abnormal isoform, this Cu-binding activity is lost. Instead, there are some suggestions that the protein might bind other metals such as Mn or Zn. PrPc functions currently under investigation include the possibility that the protein is involved in signal transduction, cell adhesion, Cu transport and resistance to oxidative stress. Of these possibilities, only a role in Cu transport and its action as an antioxidant take into consideration PrPc's Cu-binding capacity. There are also more published data supporting these two functions. There is strong evidence that during the course of prion disease, there is a loss of function of the prion protein. This manifests as a change in metal balance in the brain and other organs and substantial oxidative damage throughout the brain. Thus prions and metals have become tightly linked in the quest to understand the nature of transmissible spongiform encephalopathies.

Sign in / Sign up

Export Citation Format

Share Document