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Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Zinc metalloproteinases and amyloid Beta-Peptide metabolism
T2 - the positive side of proteolysis in Alzheimer's disease
AU - Gough, Mallory
AU - Parr-Sturgess, Catherine
AU - Parkin, Edward
N1 - 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.
PY - 2011
Y1 - 2011
N2 - 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.
AB - 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.
U2 - 10.1155/2011/721463
DO - 10.1155/2011/721463
M3 - Journal article
C2 - 21152187
VL - 2011
JO - Biochemistry Research International
JF - Biochemistry Research International
SN - 2090-2255
M1 - 721463
ER -