Abeta(31-35) peptide induce apoptosis in PC 12 cells: contrast with Abeta(25-35) peptide and examination of underlying mechanisms

The toxic behaviour of the two shorter sequences of the native Abeta amyloid peptide required for cytotoxicity i.e., Abeta(31-35) and Abeta(25-35) peptides, was studied. We have shown that Abeta(31-35) peptide induces neurotoxicity in undifferentiated PC 12 cell via an apoptotic cell death pathway,...

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Bibliographic Details
Published in:Neurochemistry international 2005-06, Vol.46 (7), p.575
Main Authors: Misiti, Francesco, Sampaolese, Beatrice, Pezzotti, Michela, Marini, Stefano, Coletta, Massimo, Ceccarelli, Lia, Giardina, Bruno, Clementi, Maria Elisabetta
Format: Article
Language:English
Subjects:
Alzheimer Disease - metabolism
Alzheimer Disease - physiopathology
Amyloid beta-Peptides - metabolism
Amyloid beta-Peptides - toxicity
Animals
Apoptosis - drug effects
Apoptosis - physiology
Brain - metabolism
Brain - physiopathology
Caspase 3
Caspases - drug effects
Caspases - metabolism
Cell Survival - drug effects
Cell Survival - physiology
DNA Fragmentation - drug effects
DNA Fragmentation - physiology
Methionine - metabolism
Nerve Degeneration - chemically induced
Nerve Degeneration - metabolism
Nerve Degeneration - pathology
Neurons - drug effects
Neurons - metabolism
Neurons - pathology
Oxidation-Reduction
Oxidative Stress - drug effects
Oxidative Stress - physiology
PC12 Cells
Peptide Fragments - metabolism
Peptide Fragments - toxicity
Rats
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Summary:The toxic behaviour of the two shorter sequences of the native Abeta amyloid peptide required for cytotoxicity i.e., Abeta(31-35) and Abeta(25-35) peptides, was studied. We have shown that Abeta(31-35) peptide induces neurotoxicity in undifferentiated PC 12 cell via an apoptotic cell death pathway, including caspase activation and DNA fragmentation. Abeta(25-35) peptide, like the shorter amyloid peptide has the ability to induce neurotoxicity, as evaluated by the MTS reduction assay and by adherent cell count, but the Abeta(25-35) peptide-induced neurotoxicity is not associated with any biochemical features of apoptosis. The differences observed between the neurotoxic properties of Abeta(31-35) and Abeta(25-35) peptides might result on their different ability to be internalised within the neuronal cells. Furthermore, this study reveals that the redox state of methionine residue, C-terminal in Abeta(31-35) and Abeta(25-35) peptides affect in a different way the toxic behaviour of these two short amyloid fragments. Taken together our results suggest that Abeta(31-35) peptide induces cell death by apoptosis, unlike the Abeta(25-35) peptide and that role played by methionine-35 in Abeta induced neurotoxicity might be related to the Abeta aggregation state.
ISSN:0197-0186