Redox metals and oxidative abnormalities in human prion diseases.

Redox metals and oxidative abnormalities in human prion diseases. Research Abstract Details 

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Redox metals and oxidative abnormalities in human prion diseases. Abstract Text:

Robert B Petersen,Sandra L Siedlak,Hyoung-gon Lee,Yong-Sun Kim,Akihiko Nunomura,Fabrizio Tagliavini,Bernardino Ghetti,Patrick Cras,Paula I Moreira,Rudy J Castellani,Marin Guentchev,Herbert Budka,James W Ironside,Pierluigi Gambetti,Mark A Smith,George Perry,Robert B Petersen,Sandra L Siedlak,Hyoung-gon Lee,Yong-Sun Kim,Akihiko Nunomura,Fabrizio Tagliavini,Bernardino Ghetti,Patrick Cras,Paula I Moreira,Rudy J Castellani,Marin Guentchev,Herbert Budka,James W Ironside,Pierluigi Gambetti,Mark A Smith,George Perry,

Prion diseases are characterized by the accumulation of diffuse and aggregated plaques of protease-resistant prion protein (PrP) in the brains of affected individuals and animals. Whereas prion diseases in animals appear to be almost exclusively transmitted by infection, human prion diseases most often occur sporadically and, to a lesser extent, by inheritance or infection. In the sporadic cases (sporadic Creutzfeld-Jakob disease, sCJD), PrP-containing plaques are infrequent, whereas in transmitted (variant CJD) and inherited (Gerstmann-Straussler-Scheinker Syndrome) cases, plaques are a usual feature. In the current study, representative cases from each of the classes of human prion disease were analyzed for the presence of markers of oxidative damage that have been found in other neurodegenerative diseases. Interestingly, we found that the pattern of deposition of PrP, amyloid-beta, and redox active metals was distinct for the various prion diseases. Whereas 8-hydroxyguanosine has been shown to be increased in sCJD, and inducible NOS is increased in scrapie-infected mice, well-studied markers of oxidative damage that accumulate in the lesions of other neurodegenerative diseases (such as Alzheimer's disease, progressive supranuclear palsy, and Parkinson's disease), such as heme oxygenase-1 and lipid peroxidation, were not found around PrP deposits or in vulnerable neurons. These findings suggest an important distinction in prion-related oxidative stress, indicating that different neurodegenerative pathways are involved in different prion diseases.

Redox metals and oxidative abnormalities in human prion diseases. Publishing Authors By Initials

RB Petersen,SL Siedlak,HG Lee,YS Kim,A Nunomura,F Tagliavini,B Ghetti,P Cras,PI Moreira,RJ Castellani,M Guentchev,H Budka,JW Ironside,P Gambetti,MA Smith,G Perry,RB Petersen,SL Siedlak,HG Lee,YS Kim,A Nunomura,F Tagliavini,B Ghetti,P Cras,PI Moreira,RJ Castellani,M Guentchev,H Budka,JW Ironside,P Gambetti,MA Smith,G Perry,

For similar proteins: prions research abstracts see: proteins: prions research

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Redox metals and oxidative abnormalities in human prion diseases. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Acta neuropathologica

VOLUME: 110

Page Numbers: 232-8

Journal Abbreviation: Acta Neuropathol.

ISSN: 0001-6322

DAY: 11

MONTH: 08

YEAR: 2005

Redox metals and oxidative abnormalities in human prion diseases. Information

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LANGUAGE: eng

NlmUniqueID: 412041

Redox metals and oxidative abnormalities in human prion diseases. Keywords Mesh Terms:

KEYWORDS: Prions

MESH TERMS: metabolism

Chemical & Substance for Abstract: Redox metals and oxidative abnormalities in human prion diseases. Information

Substance Name: Nitric Oxide Synthase Type II

Registry Number: EC 1.14.13.39

Grant and Affiliation Information for Redox metals and oxidative abnormalities in human prion diseases.

AFFILIATION: Institute of Pathology, Case Western Reserve University, 2085 Adelbert Road, Cleveland, OH 44106, USA.

Country: Germany

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MEDLINETA: Acta Neuropathol

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