Gough, Mallory and Parr-Sturgess, Catherine and Parkin, Edward (2011) Zinc metalloproteinases and amyloid Beta-Peptide metabolism:the positive side of proteolysis in Alzheimer's disease. Biochemistry Research International, 2011. ISSN 2090-2255
|PDF - Published Version |
Available under License Creative Commons Attribution.
Download (936Kb) | Preview
Alzheimer's disease is a neurodegenerative condition characterized by an accumulation of toxic amyloid beta- (Aβ-)peptides in the brain causing progressive neuronal death. Aβ-peptides are produced by aspartyl proteinase-mediated cleavage of the larger amyloid precursor protein (APP). In contrast to this detrimental "amyloidogenic" form of proteolysis, a range of zinc metalloproteinases can process APP via an alternative "nonamyloidogenic" pathway in which the protein is cleaved within its Aβ region thereby precluding the formation of intact Aβ-peptides. In addition, other members of the zinc metalloproteinase family can degrade preformed Aβ-peptides. As such, the zinc metalloproteinases, collectively, are key to downregulating Aβ generation and enhancing its degradation. It is the role of zinc metalloproteinases in this "positive side of proteolysis in Alzheimer's disease" that is discussed in the current paper.
|Journal or Publication Title:||Biochemistry Research International|
|Additional Information:||Copyright © 2011 Mallory Gough et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited On:||06 Dec 2011 16:05|
|Last Modified:||13 Jan 2016 13:58|
Actions (login required)