Cristiana Carelli Alinovi
Faculty of Medicine, Institute of Biochemistry and Clinical Biochemistry, Catholic University Largo F. Vito 1, 00168 Rome, Italy
Michela Pezzotti
Faculty of Medicine, Institute of Biochemistry and Clinical Biochemistry, Catholic University Largo F. Vito 1, 00168 Rome, Italy
Daniele Mezzogori
Faculty of Medicine, Institute of Biochemistry and Clinical Biochemistry, Catholic University Largo F. Vito 1, 00168 Rome, Italy
M. Elisabetta Clementi
Faculty of Medicine, Institute of Biochemistry and Clinical Biochemistry, Catholic University Largo F. Vito 1, 00168 Rome, Italy
Francesco Misiti
Faculty of Medicine, Institute of Biochemistry and Clinical Biochemistry, Catholic University Largo F. Vito 1, 00168 Rome, Italy
Bruno Giardina
Faculty of Medicine, Institute of Biochemistry and Clinical Biochemistry, Catholic University Largo F. Vito 1, 00168 Rome, Italy
Federica Orsini
Faculty of Medicine, Institute of Biochemistry and Clinical Biochemistry, Catholic University Largo F. Vito 1, 00168 Rome, Italy
ABSTRACT
The pathological features of Alzheimer`s disease include deposition of senile plaques in different brain zones formed by aggregates of fibrillar Aß peptide (AßP), a neurotoxic metabolic product. In this study we used the soluble form of fragment 25-35 of AßP, that includes methionine 35, side chain of AßP, to investigate the role of redox state of Met-35 on the pathogenesis of AD, because this residue in AßP is the most susceptible to oxidation in vivo. The data obtained evidenced that Aß(25-35) peptide determines a loss of PC12 cells viability determining mitochondrial damage with a possible trigger of pro-apoptotic signals. In particular, the following parameters were examined: cytochrome c release, mitochondrial membrane potential (ΔΨm) and mitochondrial respiration. In this study, three different peptides have been used: Aß(25-35) with methionine 35 in the reduced state, oxidized to sulfoxide and/or substituted with norleucine. We conclude that alteration in the mitochondrial functionality might be a contributing factor to the pathogenesis of AD and the amplitude of the effects elicited by Aß peptide is modulated by the redox state of methionine.
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How to cite this article
Cristiana Carelli Alinovi, Michela Pezzotti, Daniele Mezzogori, M. Elisabetta Clementi, Francesco Misiti, Bruno Giardina and Federica Orsini, 2006. Aß(25-35) Peptide Induces Cell Death in PC12 Cells via Mitochondrial Damage and Cytochrome c Release. Journal of Biological Sciences, 6: 140-145.
DOI: 10.3923/jbs.2006.140.145
URL: https://scialert.net/abstract/?doi=jbs.2006.140.145
DOI: 10.3923/jbs.2006.140.145
URL: https://scialert.net/abstract/?doi=jbs.2006.140.145
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