Amyloid β-Peptide Promotes Permeability Transition Pore in Brain Mitochondria. Issue 6 (December 2001)

• Record Type: Journal Article
• Authors: Moreira, Paula I.; Santos, Maria S.; Moreno, António; Oliveira, Catarina
• Is Part Of: Bioscience reports. Volume 21:Issue 6(2001)
• Page Start: 789
• Page End: 800
• Publication Date: 2001-12
• Subjects: Amyloid β-peptide -- permeability transition pore -- brain mitochondria -- mitochondrial transmembrane potential -- calcium fluxes -- neurodegeneration; Molecular biology -- Periodicals; Cytology -- Periodicals; 572.8
• DOI: 10.1023/A:1015536808304
• Languages: English
• ISSNs: 0144-8463

Abstract

Abstract : In this work the effect of the neurotoxic amino acid sequence, Aβ25–35, on brain mitochondrial permeability transition pore (PTP) was studied. For the purpose, the mitochondrial transmembrane potential (ΔΨm), mitochondrial respiration and the calcium fluxes were examined. It was observed that Aβ25–35, in the presence of Ca 2+, decreased the ΔΨm, the capacity of brain mitochondria to accumulate calcium and led to a complete uncoupling of the respiration. However, the reverse sequence of the peptide Aβ25–35 (Aβ35–25 ) did not promote the PTP. The alterations promoted by Aβ35–25 and/or Ca 2+ could be reversed when Ca 2+ was removed by EGTA or when ADP plus oligomycin were present. The pre-treatment with CsA or ADP plus oligomycin prevented the ΔΨm drop and preserved the capacity of mitochondria to accumulate Ca 2+ . These results suggest that Aβ25–35 can promote the PTP induced by Ca 2+ .