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Acyl peptide hydrolase degrades monomeric and oligomeric amyloid-beta peptide
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Yamin, Rina, Zhao, Cheng, O'Connor, Peter B., McKee, Ann C. and Abraham, Carmela R.. (2009) Acyl peptide hydrolase degrades monomeric and oligomeric amyloid-beta peptide. Molecular Neurodegeneration, Vol.4 (No.1). Article: 33. ISSN 1750-1326
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Official URL: http://dx.doi.org/10.1186/1750-1326-4-33
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 > 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 |
| Date: | 2009 |
| Volume: | Vol.4 |
| Number: | No.1 |
| Number of Pages: | 10 |
| Page Range: | Article: 33 |
| Identification Number: | 10.1186/1750-1326-4-33 |
| Status: | Peer Reviewed |
| Publication Status: | Published |
| Access rights to Published version: | Open Access |
| 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: | http://wrap.warwick.ac.uk/id/eprint/40607 |
Data sourced from Thomson Reuters' Web of Knowledge
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