Effect of amyloid beta-peptide on permeability transition pore: A comparative study
Autor(a) principal: | |
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Data de Publicação: | 2002 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10316/8324 https://doi.org/10.1002/jnr.10282 |
Resumo: | A potentially central factor in neurodegeneration is the permeability transition pore (PTP). Because of the tissue-specific differences in pore properties, we directly compared isolated brain and liver mitochondria responses to the neurotoxic Abeta peptides. For this purpose, the following parameters were examined: mitochondrial membrane potential (DeltaPsim), respiration, swelling, ultrastructural morphology, and content of cytochrome c. Both peptides, Abeta25-35 (50 muM) and Abeta1-40 (2 muM), had a similar toxicity, exacerbating the effects of Ca2+, although, per se, they did not induce (PTP). In liver mitochondria, Abeta led to a drop in DeltaPsim and potentiated matrix swelling and disruption induced by Ca2+. In contrast, brain mitochondria, exposed to the same conditions, demonstrated a higher capacity to accumulate Ca2+ before the DeltaPsim drop and a slight increase of mitochondrial swelling compared with liver mitochondria. Furthermore, mitochondrial respiratory state 3 was depressed in the presence of Abeta, whereas state 4 was unaltered, resulting in an uncoupling of respiration. In both types of mitochondria, Abeta did not affect the content of cytochrome c. The DeltaPsim drop was reversed when Ca2+ was removed by EGTA or when ADP plus oligomycin was present. Pretreatment with cyclosporin A or ADP plus oligomycin prevented the deleterious effects promoted by Abeta and/or Ca2+. It can be concluded that brain and liver mitochondria show a different susceptibility to the deleterious effect of Abeta peptide, brain mitochondria being more resistant to the potentiation by Abeta of Ca2+-induced PTP. © 2002 Wiley-Liss, Inc. |
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Effect of amyloid beta-peptide on permeability transition pore: A comparative studyA potentially central factor in neurodegeneration is the permeability transition pore (PTP). Because of the tissue-specific differences in pore properties, we directly compared isolated brain and liver mitochondria responses to the neurotoxic Abeta peptides. For this purpose, the following parameters were examined: mitochondrial membrane potential (DeltaPsim), respiration, swelling, ultrastructural morphology, and content of cytochrome c. Both peptides, Abeta25-35 (50 muM) and Abeta1-40 (2 muM), had a similar toxicity, exacerbating the effects of Ca2+, although, per se, they did not induce (PTP). In liver mitochondria, Abeta led to a drop in DeltaPsim and potentiated matrix swelling and disruption induced by Ca2+. In contrast, brain mitochondria, exposed to the same conditions, demonstrated a higher capacity to accumulate Ca2+ before the DeltaPsim drop and a slight increase of mitochondrial swelling compared with liver mitochondria. Furthermore, mitochondrial respiratory state 3 was depressed in the presence of Abeta, whereas state 4 was unaltered, resulting in an uncoupling of respiration. In both types of mitochondria, Abeta did not affect the content of cytochrome c. The DeltaPsim drop was reversed when Ca2+ was removed by EGTA or when ADP plus oligomycin was present. Pretreatment with cyclosporin A or ADP plus oligomycin prevented the deleterious effects promoted by Abeta and/or Ca2+. It can be concluded that brain and liver mitochondria show a different susceptibility to the deleterious effect of Abeta peptide, brain mitochondria being more resistant to the potentiation by Abeta of Ca2+-induced PTP. © 2002 Wiley-Liss, Inc.2002info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/8324http://hdl.handle.net/10316/8324https://doi.org/10.1002/jnr.10282engJournal of Neuroscience Research. 69:2 (2002) 257-267Moreira, Paula I.Santos, Maria S.Moreno, AntónioRego, A. CristinaOliveira, Catarinainfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2021-02-26T11:01:36Zoai:estudogeral.uc.pt:10316/8324Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:55:32.133235Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Effect of amyloid beta-peptide on permeability transition pore: A comparative study |
title |
Effect of amyloid beta-peptide on permeability transition pore: A comparative study |
spellingShingle |
Effect of amyloid beta-peptide on permeability transition pore: A comparative study Moreira, Paula I. |
title_short |
Effect of amyloid beta-peptide on permeability transition pore: A comparative study |
title_full |
Effect of amyloid beta-peptide on permeability transition pore: A comparative study |
title_fullStr |
Effect of amyloid beta-peptide on permeability transition pore: A comparative study |
title_full_unstemmed |
Effect of amyloid beta-peptide on permeability transition pore: A comparative study |
title_sort |
Effect of amyloid beta-peptide on permeability transition pore: A comparative study |
author |
Moreira, Paula I. |
author_facet |
Moreira, Paula I. Santos, Maria S. Moreno, António Rego, A. Cristina Oliveira, Catarina |
author_role |
author |
author2 |
Santos, Maria S. Moreno, António Rego, A. Cristina Oliveira, Catarina |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Moreira, Paula I. Santos, Maria S. Moreno, António Rego, A. Cristina Oliveira, Catarina |
description |
A potentially central factor in neurodegeneration is the permeability transition pore (PTP). Because of the tissue-specific differences in pore properties, we directly compared isolated brain and liver mitochondria responses to the neurotoxic Abeta peptides. For this purpose, the following parameters were examined: mitochondrial membrane potential (DeltaPsim), respiration, swelling, ultrastructural morphology, and content of cytochrome c. Both peptides, Abeta25-35 (50 muM) and Abeta1-40 (2 muM), had a similar toxicity, exacerbating the effects of Ca2+, although, per se, they did not induce (PTP). In liver mitochondria, Abeta led to a drop in DeltaPsim and potentiated matrix swelling and disruption induced by Ca2+. In contrast, brain mitochondria, exposed to the same conditions, demonstrated a higher capacity to accumulate Ca2+ before the DeltaPsim drop and a slight increase of mitochondrial swelling compared with liver mitochondria. Furthermore, mitochondrial respiratory state 3 was depressed in the presence of Abeta, whereas state 4 was unaltered, resulting in an uncoupling of respiration. In both types of mitochondria, Abeta did not affect the content of cytochrome c. The DeltaPsim drop was reversed when Ca2+ was removed by EGTA or when ADP plus oligomycin was present. Pretreatment with cyclosporin A or ADP plus oligomycin prevented the deleterious effects promoted by Abeta and/or Ca2+. It can be concluded that brain and liver mitochondria show a different susceptibility to the deleterious effect of Abeta peptide, brain mitochondria being more resistant to the potentiation by Abeta of Ca2+-induced PTP. © 2002 Wiley-Liss, Inc. |
publishDate |
2002 |
dc.date.none.fl_str_mv |
2002 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10316/8324 http://hdl.handle.net/10316/8324 https://doi.org/10.1002/jnr.10282 |
url |
http://hdl.handle.net/10316/8324 https://doi.org/10.1002/jnr.10282 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Neuroscience Research. 69:2 (2002) 257-267 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799133842246729728 |