Dinamarca_2008_Chem.Biol.Interact_175_142

Reference

Title : Release of acetylcholinesterase (AChE) from beta-amyloid plaques assemblies improves the spatial memory impairments in APP-transgenic mice - Dinamarca_2008_Chem.Biol.Interact_175_142
Author(s) : Dinamarca MC , Arrazola M , Toledo E , Cerpa WF , Hancke J , Inestrosa NC
Ref : Chemico-Biological Interactions , 175 :142 , 2008
Abstract :

The major protein constituent of amyloid deposits in Alzheimer's disease (AD) is the amyloid-beta-peptide (Abeta). Amyloid deposits contain "chaperone molecules" which play critical roles in amyloid formation and toxicity. In the present work, we test an analog of hyperforin (IDN 5706) which releases the AChE from both the Abeta fibrils and the AChE-Abeta burdens in transgenic mice. Hyperforin is an acylphloroglucinol compound isolated from Hypericum perforatum (St. John's Wort), which is able to prevent the Abeta-induced spatial memory impairments and Abeta neurotoxicity. Altogether this gathered evidence indicates the important role of AChE in the neurotoxicity of Abeta plaques and finding new compounds which decrease the AChE-Abeta interaction may be a putative therapeutic agent to fight the disease.

PubMedSearch : Dinamarca_2008_Chem.Biol.Interact_175_142
PubMedID: 18599028

Related information

Citations formats

Dinamarca MC, Arrazola M, Toledo E, Cerpa WF, Hancke J, Inestrosa NC (2008)
Release of acetylcholinesterase (AChE) from beta-amyloid plaques assemblies improves the spatial memory impairments in APP-transgenic mice
Chemico-Biological Interactions 175 :142

Dinamarca MC, Arrazola M, Toledo E, Cerpa WF, Hancke J, Inestrosa NC (2008)
Chemico-Biological Interactions 175 :142