Document Detail


Nanoimaging for prion related diseases.
MedLine Citation:
PMID:  20724837     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Misfolding and aggregation of prion proteins is linked to a number of neurodegenerative disorders such as Creutzfeldt-Jacob disease (CJD) and its variants: Kuru, Gerstmann-Straussler-Scheinker syndrome and fatal familial insomnia. In prion diseases, infectious particles are proteins that propagate by transmitting a misfolded state of a protein, leading to the formation of aggregates and ultimately to neurodegeneration. Prion phenomenon is not restricted to humans. There are a number of prion-related diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle. All known prion diseases, collectively called transmissible spongiform encephalopathies (TSEs), are untreatable and fatal. Prion proteins were also found in some fungi where they are responsible for heritable traits. Prion proteins in fungi are easily accessible and provide a powerful model for understanding the general principles of prion phenomenon and molecular mechanisms of mammalian prion diseases. Presently, several fundamental questions related to prions remain unanswered. For example, it is not clear how prions cause the disease. Other unknowns include the nature and structure of infectious agent and how prions replicate. Generally, the phenomenon of misfolding of the prion protein into infectious conformations that have the ability to propagate their properties via aggregation is of significant interest. Despite the crucial importance of misfolding and aggregation, very little is currently known about the molecular mechanisms of these processes. While there is an apparent critical need to study molecular mechanisms underlying misfolding and aggregation, the detailed characterization of these single molecule processes is hindered by the limitation of conventional methods. Although some issues remain unresolved, much progress has been recently made primarily due to the application of nanoimaging tools. The use of nanoimaging methods shows great promise for understanding the molecular mechanisms of prion phenomenon, possibly leading toward early diagnosis and effective treatment of these devastating diseases. This review article summarizes recent reports which advanced our understanding of the prion phenomenon through the use of nanoimaging methods.
Authors:
Alexey V Krasnoslobodtsev; Alexander M Portillo; Tanja Deckert-Gaudig; Volker Deckert; Yuri L Lyubchenko
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Review     Date:  2010-10-23
Journal Detail:
Title:  Prion     Volume:  4     ISSN:  1933-690X     ISO Abbreviation:  Prion     Publication Date:    2010 Oct-Dec
Date Detail:
Created Date:  2010-11-10     Completed Date:  2011-06-06     Revised Date:  2012-02-13    
Medline Journal Info:
Nlm Unique ID:  101472305     Medline TA:  Prion     Country:  United States    
Other Details:
Languages:  eng     Pagination:  265-74     Citation Subset:  IM    
Affiliation:
Department of Pharmaceutical Sciences, University of Nebraska Medical Center, Omaha, NE, USA. akrasnos@unmc.edu
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MeSH Terms
Descriptor/Qualifier:
Amyloid / chemistry
Animals
Diagnostic Imaging / methods*
Humans
Nanotechnology / methods*
Prion Diseases / diagnosis*
Prions / chemistry
Species Specificity
Chemical
Reg. No./Substance:
0/Amyloid; 0/Prions

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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