Amyloid beta-peptide promotes permeability transition pore in brain mitochondria |
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Authors: | Moreira P I Santos M S Moreno A Oliveira C |
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Institution: | (1) Center for Neuroscience and Cellular Biology of Coimbra, Department of Zoology, University of Coimbra, Portugal;(2) Department of Biochemistry, Faculty of Medicine, University of Coimbra, 3004-517 Coimbra, Portugal |
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Abstract: | In this work the effect of the neurotoxic amino acid sequence, A 25–35, on brain mitochondrial permeability transition pore (PTP) was studied. For the purpose, the mitochondrial transmembrane potential (![Delta](/content/ml5rjm8kp31cxpnd/xxlarge916.gif) m), mitochondrial respiration and the calcium fluxes were examined. It was observed that A 25–35, in the presence of Ca2+, decreased the ![Delta](/content/ml5rjm8kp31cxpnd/xxlarge916.gif) m, the capacity of brain mitochondria to accumulate calcium and led to a complete uncoupling of the respiration. However, the reverse sequence of the peptide A 25–35 (A 35–25) did not promote the PTP. The alterations promoted by A 35–25 and/or Ca2+ could be reversed when Ca2+ was removed by EGTA or when ADP plus oligomycin were present. The pre-treatment with CsA or ADP plus oligomycin prevented the ![Delta](/content/ml5rjm8kp31cxpnd/xxlarge916.gif) m drop and preserved the capacity of mitochondria to accumulate Ca2+. These results suggest that A 25–35 can promote the PTP induced by Ca2+. |
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Keywords: | Amyloid -peptide" target="_blank">gif" alt="beta" align="MIDDLE" BORDER="0">-peptide permeability transition pore brain mitochondria mitochondrial transmembrane potential calcium fluxes neurodegeneration |
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