English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/62794
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Changes in molecular isoform distribution of acetylcholinesterase in rat cortex and cerebrospinal fluid after intracerebroventricular administration of amyloid β-peptide

AuthorsSáez-Valero, Javier; Ceballos, María L. de ; Small, David H.; Felipe, Carmen de
Issue Date2002
PublisherElsevier
CitationNeuroscience Letters 325: 199- 202 (2002)
AbstractPrevious studies have shown that an abnormal salt-soluble form of G1 acetylcholinesterase (AChE) is increased in the Alzheimer's disease (AD) brain. The aim of the present study was to examine changes in AChE activity in an in vivo model of β-amyloid peptide (Aβ) administration. Rats received intracerebroventricular injections of Aβ25-35 (20 μg/day for seven days). Levels of AChE were measured in cerebral cortex and cerebrospinal fluid (CSF) after two months. Aβ25-35 administration did not alter total AChE activity in the cerebral cortex or CSF. However, analysis of salt-extractable AChE isoforms revealed an increase in the proportion of G1 in both cortex and CSF, similar to that previously observed in AD patients. The results support the view that changes in AChE isoform pattern in the AD brain are a direct consequence of Aβ accumulation. © 2002 Elsevier Science Ireland Ltd. All rights reserved.
URIhttp://hdl.handle.net/10261/62794
DOI10.1016/S0304-3940(02)00282-3
Identifiersdoi: 10.1016/S0304-3940(02)00282-3
issn: 0304-3940
Appears in Collections:(IC) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.