Document Detail

Acetylcholinesterase triggers the aggregation of PrP 106-126.
MedLine Citation:
PMID:  16750169     Owner:  NLM     Status:  MEDLINE    
Acetylcholinesterase (AChE), a senile plaque component, promotes amyloid-beta-protein (Abeta) fibril formation in vitro. The presence of prion protein (PrP) in Alzheimer's disease (AD) senile plaques prompted us to assess if AChE could trigger the PrP peptides aggregation as well. Consequently, the efficacy of AChE on the PrP peptide spanning-residues 106-126 aggregation containing a coumarin fluorescence probe (coumarin-PrP 106-126) was studied. Kinetics of coumarin-PrP 106-126 aggregation showed a significant increase of maximum size of aggregates (MSA), which was dependent on AChE concentration. AChE-PrP 106-126 aggregates showed the tinctorial and optical amyloid properties as determined by polarized light and electronic microscopy analysis. A remarkable inhibition of MSA was obtained with propidium iodide, suggesting that AChE triggers PrP 106-126 and Abeta aggregation through a similar mechanism. Huprines (AChE inhibitors) also significantly decreased MSA induced by AChE as well, unveiling the potential interest for some AChE inhibitors as a novel class of potential anti-prion drugs.
M Pera; S Román; M Ratia; P Camps; D Muñoz-Torrero; L Colombo; C Manzoni; M Salmona; A Badia; M V Clos
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-05-24
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  346     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2006 Jul 
Date Detail:
Created Date:  2006-06-19     Completed Date:  2006-08-28     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  89-94     Citation Subset:  IM    
Departament de Farmacologia, de Terapèutica i de Toxicología, Institut Neurociències, Universitat Autónoma de Barcelona, Barcelona, Spain.
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MeSH Terms
Acetylcholinesterase / metabolism*
Aminoquinolines / pharmacology
Cholinesterase Inhibitors / pharmacology
Heterocyclic Compounds with 4 or More Rings / pharmacology
Microscopy, Fluorescence
Peptide Fragments / chemistry*,  metabolism
Prions / chemistry*,  metabolism
Propidium / pharmacology
Protein Structure, Secondary / drug effects
Sesquiterpenes / pharmacology
Reg. No./Substance:
0/Aminoquinolines; 0/Cholinesterase Inhibitors; 0/Coumarins; 0/Heterocyclic Compounds with 4 or More Rings; 0/Peptide Fragments; 0/Prions; 0/Sesquiterpenes; 0/huprine X; 0/huprine Y; 0/prion protein (106-126); 102518-79-6/huperzine A; 36015-30-2/Propidium; EC

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

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