Acyl peptide hydrolase degrades monomeric and oligomeric amyloid-beta peptide

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Abstract

The abnormal accumulation of amyloid-beta peptide is believed to cause malfunctioning of neurons in the Alzheimer's disease brain. Amyloid-beta exists in different assembly forms in the aging mammalian brain including monomers, oligomers, and aggregates, and in senile plaques, fibrils. Recent findings suggest that soluble amyloid-beta oligomers may represent the primary pathological species in Alzheimer's disease and the most toxic form that impairs synaptic and thus neuronal function. We previously reported the isolation of a novel amyloid-beta-degrading enzyme, acyl peptide hydrolase, a serine protease that degrades amyloid-beta, and is different in structure and activity from other amyloid-beta-degrading enzymes.

Item Type: Journal Article
Subjects: Q Science > QD Chemistry
R Medicine > RC Internal medicine > RC0321 Neuroscience. Biological psychiatry. Neuropsychiatry
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Library of Congress Subject Headings (LCSH): Amyloid beta-protein, Hydrolases, Alzheimer's disease -- Etiology, Neurotoxicology, Peptides, Mass spectrometry
Journal or Publication Title: Molecular Neurodegeneration
Publisher: BioMed Central Ltd.
ISSN: 1750-1326
Official Date: 2009
Dates:
Date
Event
2009
Published
Volume: Vol.4
Number: No.1
Number of Pages: 10
Page Range: Article: 33
DOI: 10.1186/1750-1326-4-33
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons open licence)
Funder: Alzheimer's Association, National Institutes of Health (U.S.) (NIH), National Institute on Aging (NIA), Boston University. Alzheimer's Disease Centre (ADC), United States. Department of Veterans Affairs
Grant number: IIRG-02-3783 (AA), P01-AG00001 (NIA), NIA P30 AG13846 (ADC)
URI: https://wrap.warwick.ac.uk/40607/

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