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

descriptionPublicationkeyboard_double_arrow_right Article 01 Jun 2002 English Publisher:Elsevier BVJournal:Neuroscience Letters, volume 325, pages 199-202 (issn: 0304-3940,

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Authors: Sáez-Valero, Javier; Ceballos, María L. de; Small, David H.; Felipe, Carmen de;

doi: 10.1016/s0304-3940(02)00282-3

pmid: 12044655

handle: 10261/62794 , 10261/36465

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

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Abstract

Previous studies have shown that an abnormal salt-soluble form of G(1) 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 beta-amyloid peptide (A beta) administration. Rats received intracerebroventricular injections of A beta(25-35) (20 microg/day for seven days). Levels of AChE were measured in cerebral cortex and cerebrospinal fluid (CSF) after two months. A beta(25-35) 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 G(1) 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 A beta accumulation.

Related Organizations

Miguel Hernandez University
Spain
Cajal Institute
Spain
Spanish National Research Council
Spain
Instituto de Neurociencias de Alicante
Spain
University of Melbourne
Australia

Keywords

Cerebral Cortex, Male, Amyloid beta-Peptides, Acetylcholinesterase, Animals, Rats, Wistar, Peptide Fragments, Injections, Intraventricular, Rats

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