The toxic behaviour of the two shorter sequences of the native Aβ amyloid peptide required for cytotoxicity i.e., Aβ(31-35) and Aβ(2535) peptides, was studied. We have shown that Aβ(31-35) peptide induces neurotoxicity in undifferentiated PC 12 cell via an apoptotic cell death pathway, including caspase activation and DNA fragmentation. Aβ(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 Aβ(25-35) peptide-induced neurotoxicity is not associated with any biochemical features of apoptosis. The differences observed between the neurotoxic properties of Aβ(31-35) and Aβ(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 Aβ(31-35) and Aβ(25-35) peptides affect in a different way the toxic behaviour of these two short amyloid fragments. Taken together our results suggest that Aβ(31-35) peptide induces cell death by apoptosis, unlike the Aβ(25-35) peptide and that role played by methionine-35 in Aβ induced neurotoxicity might be related to the Aβ aggregation state. © 2005 Elsevier Ltd. All rights reserved.

Misiti, F., Sampaolese, B., Pezzotti, M., Marini, S., Coletta, M., Ceccarelli, L., et al. (2005). A beta(31-35) peptide induce apoptosis in PC 12 cells: Contrast with A beta(25-35) peptide and examination of underlying mechanisms. NEUROCHEMISTRY INTERNATIONAL, 46(7), 575-583 [10.1016/j.neuint.2005.01.001].

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

MARINI, STEFANO;COLETTA, MASSIMILIANO;
2005

Abstract

The toxic behaviour of the two shorter sequences of the native Aβ amyloid peptide required for cytotoxicity i.e., Aβ(31-35) and Aβ(2535) peptides, was studied. We have shown that Aβ(31-35) peptide induces neurotoxicity in undifferentiated PC 12 cell via an apoptotic cell death pathway, including caspase activation and DNA fragmentation. Aβ(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 Aβ(25-35) peptide-induced neurotoxicity is not associated with any biochemical features of apoptosis. The differences observed between the neurotoxic properties of Aβ(31-35) and Aβ(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 Aβ(31-35) and Aβ(25-35) peptides affect in a different way the toxic behaviour of these two short amyloid fragments. Taken together our results suggest that Aβ(31-35) peptide induces cell death by apoptosis, unlike the Aβ(25-35) peptide and that role played by methionine-35 in Aβ induced neurotoxicity might be related to the Aβ aggregation state. © 2005 Elsevier Ltd. All rights reserved.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/10
eng
Con Impact Factor ISI
amyloid beta-peptide; A beta P(31-35) fragments; A beta P(25-35) fragment; methionine oxidation; mitochondria; apoptosis; neurotoxicity
Misiti, F., Sampaolese, B., Pezzotti, M., Marini, S., Coletta, M., Ceccarelli, L., et al. (2005). A beta(31-35) peptide induce apoptosis in PC 12 cells: Contrast with A beta(25-35) peptide and examination of underlying mechanisms. NEUROCHEMISTRY INTERNATIONAL, 46(7), 575-583 [10.1016/j.neuint.2005.01.001].
Misiti, F; Sampaolese, B; Pezzotti, M; Marini, S; Coletta, M; Ceccarelli, L; Giardina, B; Clementi, M
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/39978
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