Expression and activity of beta-site amyloid precursor protein cleaving enzyme in Alzheimer's disease
| Autor: | David T.R. Coulson, W.W. Liu, Anthony Peter Passmore, Stephen Todd, G.B. Irvine, Janet A. Johnston, Suzanne P. Murphy |
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| Rok vydání: | 2005 |
| Předmět: |
chemistry.chemical_classification
Blood Platelets Proteases biology Chemistry P3 peptide Brain Cleavage (embryo) Biochemistry Biochemistry of Alzheimer's disease Amyloid beta-Protein Precursor Enzyme Cholesterol Alzheimer Disease Endopeptidases biology.protein Amyloid precursor protein Aspartic Acid Endopeptidases Humans Platelet Amyloid Precursor Protein Secretases Amyloid precursor protein secretase |
| Zdroj: | Biochemical Society transactions. 33(Pt 5) |
| ISSN: | 0300-5127 |
| Popis: | Several lines of evidence indicate that the Abeta peptide is involved at some level in the pathological process that results in the clinical symptoms of AD (Alzheimer's disease). The N-terminus of Abeta is generated by cleavage of the Met-Asp bond at position 671-672 of APP (amyloid precursor protein), catalysed by a proteolytic activity called beta-secretase. Two 'beta-secretase' proteases have been identified: BACE (beta-site APP-cleaving enzyme) and BACE2. The cause of sporadic AD is currently unknown, but some studies have reported elevated BACE/beta-secretase activity in brain regions affected by the disease. We have demonstrated that robust beta-secretase activity is also detectable in platelets that contain APP and release Abeta. This review considers the current evidence for alterations in beta-secretase activity, and/or alterations in BACE expression, in post-mortem brain tissue and platelets from individuals with AD. |
| Databáze: | OpenAIRE |
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