Human amyloid-beta1-42 applied in vivo inhibits the fast axonal transport of proteins in the sciatic nerve of rat
Autor: | Haruyasu Yamaguchi, Henrietta Papp, Botond Penke, Peter Kasa, Imre Kovacs, Monika Forgon |
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Rok vydání: | 2000 |
Předmět: |
Male
Amyloid Axonal Transport Rats Sprague-Dawley chemistry.chemical_compound In vivo Alzheimer Disease Vesicular acetylcholine transporter mental disorders Amyloid precursor protein Animals Humans Amyloid beta-Peptides biology General Neuroscience Acetylcholinesterase Sciatic Nerve Axons Peptide Fragments Cell biology Rats nervous system chemistry Depression Chemical biology.protein Axoplasmic transport Synaptophysin Sciatic nerve Neuroscience |
Zdroj: | Neuroscience letters. 278(1-2) |
ISSN: | 0304-3940 |
Popis: | Human amyloid-β1–42 has been suggested to be a pathogenetic factor in Alzheimer's disease. The precise mechanism by which this peptide causes the degeneration of neurons in the affected brain is not yet fully understood. By using immunohistochemistry we explored the inhibitory effects of human amyloid-β1–42 applied in vivo on the fast axonal transport of acetylcholinesterase, the amyloid precursor protein, the vesicular acetylcholine transporter and synaptophysin in the sciatic nerve of rat. Our findings provide evidence for the in vivo neurotoxic effect of human amyloid-β peptide. |
Databáze: | OpenAIRE |
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