Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential

Detalhes bibliográficos
Autor(a) principal: Smaili, Soraya Soubhi [UNIFESP]
Data de Publicação: 2001
Outros Autores: Hsu, Y. T., Sanders, K. M., Russel, J. T., Youle, R. J.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: http://dx.doi.org/10.1038/sj.cdd.4400889
http://repositorio.unifesp.br/handle/11600/26609
Resumo: Bax, a pro-apoptotic member of the Bcl-2 family, is a cytosolic protein that inserts into mitochondrial membranes upon induction of cell death. Using the green fluorescent protein fused to Bax (GFP-Bax) to quantitate mitochondrial binding in living cells we have investigated the cause of Bax association with mitochondria and the time course relative to endogenous and induced changes in mitochondrial membrane potential (Delta Psi (m)). We have found that staurosporine (STS) induces a loss in Delta Psi (m) before GFP-Bax translocation can be measured. the onset of the Delta Psi (m) loss is followed by a rapid and complete collapse of Delta Psi (m) which is followed by Bax association with mitochondria. the mitochondria uncoupler FCCP, in the presence of the F-1-F-0 ATPase inhibitor oligomycin, can trigger Bax translocation to mitochondria suggesting that when ATP levels are maintained a collapse of Delta Psi (m) induces Bax translocation. Neither FCCP nor oligomycin alone alters Bax location. Bax association with mitochondria is also triggered by inhibitors of the electron transport chain, antimycin and rotenone, compounds that collapse Delta Psi (m) without inducing rapid ATP hydrolysis that typically occurs with uncouplers such as FCCP. Taken together, our results suggest that alterations in mitochondrial energization associated with apoptosis can initiate Bax docking to mitochondria.
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spelling Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potentialmitochondriaBaxmitochondrial membrane potentialmitochondrial inhibitorsBax, a pro-apoptotic member of the Bcl-2 family, is a cytosolic protein that inserts into mitochondrial membranes upon induction of cell death. Using the green fluorescent protein fused to Bax (GFP-Bax) to quantitate mitochondrial binding in living cells we have investigated the cause of Bax association with mitochondria and the time course relative to endogenous and induced changes in mitochondrial membrane potential (Delta Psi (m)). We have found that staurosporine (STS) induces a loss in Delta Psi (m) before GFP-Bax translocation can be measured. the onset of the Delta Psi (m) loss is followed by a rapid and complete collapse of Delta Psi (m) which is followed by Bax association with mitochondria. the mitochondria uncoupler FCCP, in the presence of the F-1-F-0 ATPase inhibitor oligomycin, can trigger Bax translocation to mitochondria suggesting that when ATP levels are maintained a collapse of Delta Psi (m) induces Bax translocation. Neither FCCP nor oligomycin alone alters Bax location. Bax association with mitochondria is also triggered by inhibitors of the electron transport chain, antimycin and rotenone, compounds that collapse Delta Psi (m) without inducing rapid ATP hydrolysis that typically occurs with uncouplers such as FCCP. Taken together, our results suggest that alterations in mitochondrial energization associated with apoptosis can initiate Bax docking to mitochondria.NINDS, Biochem Sect, Surg Neurol Branch, NIH, Bethesda, MD 20892 USAUniversidade Federal de São Paulo, Dept Farmacol, São Paulo, BrazilNICHHD, Lab Cellular & Mol Neurophysiol, NIH, Bethesda, MD 20892 USAMed Univ S Carolina, Charleston, SC 29425 USAUniversidade Federal de São Paulo, Dept Farmacol, São Paulo, BrazilWeb of ScienceNature Publishing GroupNINDSUniversidade Federal de São Paulo (UNIFESP)NICHHDMed Univ S CarolinaSmaili, Soraya Soubhi [UNIFESP]Hsu, Y. T.Sanders, K. M.Russel, J. T.Youle, R. J.2016-01-24T12:31:27Z2016-01-24T12:31:27Z2001-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion909-920http://dx.doi.org/10.1038/sj.cdd.4400889Cell Death and Differentiation. Basingstoke: Nature Publishing Group, v. 8, n. 9, p. 909-920, 2001.10.1038/sj.cdd.44008891350-9047http://repositorio.unifesp.br/handle/11600/26609WOS:000170472300005engCell Death and Differentiationinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2023-05-18T13:50:59Zoai:repositorio.unifesp.br/:11600/26609Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652023-05-18T13:50:59Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
title Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
spellingShingle Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
Smaili, Soraya Soubhi [UNIFESP]
mitochondria
Bax
mitochondrial membrane potential
mitochondrial inhibitors
title_short Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
title_full Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
title_fullStr Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
title_full_unstemmed Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
title_sort Bax translocation to mitochondria subsequent to a rapid loss of mitochondrial membrane potential
author Smaili, Soraya Soubhi [UNIFESP]
author_facet Smaili, Soraya Soubhi [UNIFESP]
Hsu, Y. T.
Sanders, K. M.
Russel, J. T.
Youle, R. J.
author_role author
author2 Hsu, Y. T.
Sanders, K. M.
Russel, J. T.
Youle, R. J.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv NINDS
Universidade Federal de São Paulo (UNIFESP)
NICHHD
Med Univ S Carolina
dc.contributor.author.fl_str_mv Smaili, Soraya Soubhi [UNIFESP]
Hsu, Y. T.
Sanders, K. M.
Russel, J. T.
Youle, R. J.
dc.subject.por.fl_str_mv mitochondria
Bax
mitochondrial membrane potential
mitochondrial inhibitors
topic mitochondria
Bax
mitochondrial membrane potential
mitochondrial inhibitors
description Bax, a pro-apoptotic member of the Bcl-2 family, is a cytosolic protein that inserts into mitochondrial membranes upon induction of cell death. Using the green fluorescent protein fused to Bax (GFP-Bax) to quantitate mitochondrial binding in living cells we have investigated the cause of Bax association with mitochondria and the time course relative to endogenous and induced changes in mitochondrial membrane potential (Delta Psi (m)). We have found that staurosporine (STS) induces a loss in Delta Psi (m) before GFP-Bax translocation can be measured. the onset of the Delta Psi (m) loss is followed by a rapid and complete collapse of Delta Psi (m) which is followed by Bax association with mitochondria. the mitochondria uncoupler FCCP, in the presence of the F-1-F-0 ATPase inhibitor oligomycin, can trigger Bax translocation to mitochondria suggesting that when ATP levels are maintained a collapse of Delta Psi (m) induces Bax translocation. Neither FCCP nor oligomycin alone alters Bax location. Bax association with mitochondria is also triggered by inhibitors of the electron transport chain, antimycin and rotenone, compounds that collapse Delta Psi (m) without inducing rapid ATP hydrolysis that typically occurs with uncouplers such as FCCP. Taken together, our results suggest that alterations in mitochondrial energization associated with apoptosis can initiate Bax docking to mitochondria.
publishDate 2001
dc.date.none.fl_str_mv 2001-09-01
2016-01-24T12:31:27Z
2016-01-24T12:31:27Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1038/sj.cdd.4400889
Cell Death and Differentiation. Basingstoke: Nature Publishing Group, v. 8, n. 9, p. 909-920, 2001.
10.1038/sj.cdd.4400889
1350-9047
http://repositorio.unifesp.br/handle/11600/26609
WOS:000170472300005
url http://dx.doi.org/10.1038/sj.cdd.4400889
http://repositorio.unifesp.br/handle/11600/26609
identifier_str_mv Cell Death and Differentiation. Basingstoke: Nature Publishing Group, v. 8, n. 9, p. 909-920, 2001.
10.1038/sj.cdd.4400889
1350-9047
WOS:000170472300005
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Cell Death and Differentiation
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 909-920
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
repository.name.fl_str_mv Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)
repository.mail.fl_str_mv biblioteca.csp@unifesp.br
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