Changes in molecular isoform distribution of acetylcholinesterase in rat cortex and cerebrospinal fluid after intracerebroventricular administration of amyloid beta-peptide.
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.
Sáez-Valero
Javier
J
Instituto de Neurociencias, Universidad Miguel Hernández-CSIC, 03550 San Juan de Alicante, Spain. j.saez@umh.es
de Ceballos
María L
ML
Small
David H
DH
de Felipe
Carmen
C
D000110:Acetylcholinesterase / Q000134:cerebrospinal fluid* / Q000187:drug effects* / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000008:administration & dosage / Q000494:pharmacology*; D000818:Animals; D002540:Cerebral Cortex / Q000187:drug effects* / Q000201:enzymology*; D007276:Injections, Intraventricular; D008297:Male; D010446:Peptide Fragments / Q000008:administration & dosage / Q000494:pharmacology*; D051381:Rats; D017208:Rats, Wistar
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C113041:amyloid beta-protein (35-25); D000110:Acetylcholinesterase