a7-Nicotinic acetylcholine receptors mediate an A71-42-induced increase in the level of acetylcholinesterase in primary cortical neurones Fodero, L. R., Mok, S. S., Losic, D., Martin, L. L., Aguilar, M. I., Barrow, C. J., Livett, B. G. and Small, D. H. 2004, a7-Nicotinic acetylcholine receptors mediate an A71-42-induced increase in the level of acetylcholinesterase in primary cortical neurones, Journal of neurochemistry, vol. 88, no. 5, pp. 1186-1193, doi: 10.1046/j.1471-4159.2003.02296.x. Attached Files Name Description MIMEType Size Downloads Title a7-Nicotinic acetylcholine receptors mediate an A71-42-induced increase in the level of acetylcholinesterase in primary cortical neurones Alternative title [alpha 7] -Nicotinic acetylcholine receptors mediate an A71-42-induced increase in the level of acetylcholinesterase in primary cortical neurones Formatted title a7-Nicotinic acetylcholine receptors mediate an Aß1-42-induced increase in the level of acetylcholinesterase in primary cortical neurones Author(s) Fodero, L. R. Mok, S. S. Losic, D. Martin, L. L. Aguilar, M. I. Barrow, C. J. orcid.org/0000-0002-2153-7267 Livett, B. G. Small, D. H. Journal name Journal of neurochemistry Volume number 88 Issue number 5 Start page 1186 End page 1193 Publisher Wiley - Blackwell Place of publication Oxford, England Publication date 2004-03 ISSN 0022-3042 1471-4159 Summary The β-amyloid protein (Aβ) is the major protein component of amyloid plaques found in the Alzheimer brain. Although there is a loss of acetylcholinesterase (AChE) from both cholinergic and non-cholinergic neurones in the brain of Alzheimer patients, the level of AChE is increased around amyloid plaques. Previous studies using P19 cells in culture and transgenic mice which overexpress human Aβ have suggested that this increase may be due to a direct action of Aβ on AChE expression in cells adjacent to amyloid plaques. The aim of the present study was to examine the mechanism by which Aβ increases levels of AChE in primary cortical neurones. Aβ1−42 was more potent than Aβ1−40 in its ability to increase AChE in primary cortical neurones. The increase in AChE was unrelated to the toxic effects of the Aβ peptides. The effect of Aβ1−42 on AChE was blocked by inhibitors of α7 nicotinic acetylcholine receptors (α7 nAChRs) as well as by inhibitors of L- or N-type voltage-dependent calcium channels (VDCCs), whereas agonists of α7 nAChRs (choline, nicotine) increased the level of AChE. The results demonstrate that the effect of Aβ1−42 on AChE is due to an agonist effect of Aβ1−42 on the α7 nAChR. Language eng DOI 10.1046/j.1471-4159.2003.02296.x Field of Research 110106 Medical Biochemistry: Proteins and Peptides (incl Medical Proteomics) Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences HERDC Research category C1.1 Refereed article in a scholarly journal Copyright notice ©2004, Wiley-Blackwell Persistent URL http://hdl.handle.net/10536/DRO/DU:30023806 Document type: Journal Article Collection: School of Life and Environmental Sciences Related Links Link Description Connect to published version (restricted access) Go to link with your DU access privileges     Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved. Versions Version Filter Type Mon, 22 Feb 2010, 10:07:51 EST Thu, 11 Mar 2010, 11:00:23 EST Thu, 11 Mar 2010, 11:08:39 EST Fri, 12 Mar 2010, 08:42:18 EST Fri, 12 Mar 2010, 08:53:00 EST Sun, 21 Mar 2010, 20:07:01 EST Mon, 07 Oct 2013, 14:18:50 EST Mon, 07 Oct 2013, 14:19:59 EST Mon, 16 Jun 2014, 14:26:22 EST Filtered Full Citation counts:   Cited 58 times in TR Web of Science Cited 62 times in Scopus Search Google Scholar Access Statistics: 743 Abstract Views, 0 File Downloads  -  Detailed Statistics Created: Mon, 22 Feb 2010, 10:07:51 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.