Generation of amyloid β protein from a presenilin-1 and βAPP complex
Presenilin-1 (PS1) is a causative gene in early onset familial Alzheimer’s disease (FAD). FAD-linked mutant PS1s significantly increased Aβ40 and Aβ42(43) levels (P < 0.001) and decreased the production of an 11.4 kD (β-stub) and an 8.7 kD (α-stub) carboxyl-terminal fragment of amyloid β precurso...
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2002
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v292_n2_p571_ShizukaIkeda http://hdl.handle.net/20.500.12110/paper_0006291X_v292_n2_p571_ShizukaIkeda |
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paper:paper_0006291X_v292_n2_p571_ShizukaIkeda2023-06-08T14:30:13Z Generation of amyloid β protein from a presenilin-1 and βAPP complex Aβ40 Aβ42(43) Presenilin-1 PS1/βAPP complex βAPP γ-secretase 3 [(3 cholamidopropyl)dimethylammonio] 1 propanesulfonic acid amyloid beta protein enzyme inhibitor gamma secretase mutant protein presenilin 1 protein precursor Alzheimer disease amino terminal sequence article carboxy terminal sequence cell line cell lysate pathogenesis pH precipitation priority journal protein analysis protein degradation protein isolation reaction analysis Presenilin-1 (PS1) is a causative gene in early onset familial Alzheimer’s disease (FAD). FAD-linked mutant PS1s significantly increased Aβ40 and Aβ42(43) levels (P < 0.001) and decreased the production of an 11.4 kD (β-stub) and an 8.7 kD (α-stub) carboxyl-terminal fragment of amyloid β precursor protein (βAPP-CTFs) (P < 0.01). In the 2% CHAPS extracted lysates, the complex containing the amino-terminal fragment of PS1 (PS1-NTF), the carboxyl-terminal fragments of PS1 (PS1-CTF), and βAPP-CTFs was identified. Incubation of this isolated complex at pH 6.4 showed the direct generation of Aβ40 and γ-stub from this complex. This reaction was inhibited by a β-secretase inhibitor. The degrading rate of a co-precipitated β-stub was facilitated under the presence of FAD-linked mutant PS1s. This findings suggest that the direct generation of Aβ from the complex may play an important role in the pathogenesis of Alzheimer’s disease. © 2002 Elsevier Science (USA). 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v292_n2_p571_ShizukaIkeda http://hdl.handle.net/20.500.12110/paper_0006291X_v292_n2_p571_ShizukaIkeda |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Aβ40 Aβ42(43) Presenilin-1 PS1/βAPP complex βAPP γ-secretase 3 [(3 cholamidopropyl)dimethylammonio] 1 propanesulfonic acid amyloid beta protein enzyme inhibitor gamma secretase mutant protein presenilin 1 protein precursor Alzheimer disease amino terminal sequence article carboxy terminal sequence cell line cell lysate pathogenesis pH precipitation priority journal protein analysis protein degradation protein isolation reaction analysis |
| spellingShingle |
Aβ40 Aβ42(43) Presenilin-1 PS1/βAPP complex βAPP γ-secretase 3 [(3 cholamidopropyl)dimethylammonio] 1 propanesulfonic acid amyloid beta protein enzyme inhibitor gamma secretase mutant protein presenilin 1 protein precursor Alzheimer disease amino terminal sequence article carboxy terminal sequence cell line cell lysate pathogenesis pH precipitation priority journal protein analysis protein degradation protein isolation reaction analysis Generation of amyloid β protein from a presenilin-1 and βAPP complex |
| topic_facet |
Aβ40 Aβ42(43) Presenilin-1 PS1/βAPP complex βAPP γ-secretase 3 [(3 cholamidopropyl)dimethylammonio] 1 propanesulfonic acid amyloid beta protein enzyme inhibitor gamma secretase mutant protein presenilin 1 protein precursor Alzheimer disease amino terminal sequence article carboxy terminal sequence cell line cell lysate pathogenesis pH precipitation priority journal protein analysis protein degradation protein isolation reaction analysis |
| description |
Presenilin-1 (PS1) is a causative gene in early onset familial Alzheimer’s disease (FAD). FAD-linked mutant PS1s significantly increased Aβ40 and Aβ42(43) levels (P < 0.001) and decreased the production of an 11.4 kD (β-stub) and an 8.7 kD (α-stub) carboxyl-terminal fragment of amyloid β precursor protein (βAPP-CTFs) (P < 0.01). In the 2% CHAPS extracted lysates, the complex containing the amino-terminal fragment of PS1 (PS1-NTF), the carboxyl-terminal fragments of PS1 (PS1-CTF), and βAPP-CTFs was identified. Incubation of this isolated complex at pH 6.4 showed the direct generation of Aβ40 and γ-stub from this complex. This reaction was inhibited by a β-secretase inhibitor. The degrading rate of a co-precipitated β-stub was facilitated under the presence of FAD-linked mutant PS1s. This findings suggest that the direct generation of Aβ from the complex may play an important role in the pathogenesis of Alzheimer’s disease. © 2002 Elsevier Science (USA). |
| title |
Generation of amyloid β protein from a presenilin-1 and βAPP complex |
| title_short |
Generation of amyloid β protein from a presenilin-1 and βAPP complex |
| title_full |
Generation of amyloid β protein from a presenilin-1 and βAPP complex |
| title_fullStr |
Generation of amyloid β protein from a presenilin-1 and βAPP complex |
| title_full_unstemmed |
Generation of amyloid β protein from a presenilin-1 and βAPP complex |
| title_sort |
generation of amyloid β protein from a presenilin-1 and βapp complex |
| publishDate |
2002 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0006291X_v292_n2_p571_ShizukaIkeda http://hdl.handle.net/20.500.12110/paper_0006291X_v292_n2_p571_ShizukaIkeda |
| _version_ |
1768544939503779840 |