Abstract |
Intracerebral or intraperitoneal injections of brain extracts from the Alzheimer's disease patients result in the acceleration of cerebral β- amyloidosis in transgenic mice. Earlier, we have found that intravenous injections of synthetic full-length amyloid-β (Aβ) comprising the isomerized Asp7 trigger cerebral β- amyloidosis. In vitro studies have shown that isomerization of Asp7 promotes zinc-induced oligomerization of the Aβ metal-binding domain (Aβ1-16). Here we report that single intracerebral injection of the peptide Aβ1-16 with isomerized Asp7 (isoAβ1-16) but not the injection of Aβ1-16 significantly increases amyloid burden in 5XFAD transgenic mice. Our results provide evidence for a role of isoAβ1-16 as a minimal seeding agent of Aβ aggregation in vivo.
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Authors | Alexandra A Kulikova, Ivan B Cheglakov, Michail S Kukharsky, Ruslan K Ovchinnikov, Sergey A Kozin, Alexander A Makarov |
Journal | Neurotoxicity research
(Neurotox Res)
Vol. 29
Issue 4
Pg. 551-7
(May 2016)
ISSN: 1476-3524 [Electronic] United States |
PMID | 26842600
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Amyloid beta-Peptides
- Amyloid beta-Protein Precursor
- PSEN1 protein, human
- Peptide Fragments
- Presenilin-1
- amyloid beta-protein (1-16)
- Aspartic Acid
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Topics |
- Alzheimer Disease
(genetics, metabolism, pathology)
- Amyloid beta-Peptides
(administration & dosage, metabolism, pharmacology)
- Amyloid beta-Protein Precursor
(genetics)
- Amyloidosis
(chemically induced, genetics)
- Analysis of Variance
- Animals
- Aspartic Acid
(metabolism)
- Disease Models, Animal
- Gene Expression Regulation
(drug effects, genetics)
- Humans
- Mice
- Mice, Inbred C57BL
- Mice, Transgenic
- Mutation
(genetics)
- Peptide Fragments
(administration & dosage, pharmacology)
- Plaque, Amyloid
(metabolism)
- Presenilin-1
(genetics)
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