Osmostress-Induced Apoptosis in Xenopus Oocytes

Hyperosmotic shock induces cytochrome c release and capase-3 activation in Xenopus oocytes, but the regulators and signaling pathways involved are not well characterized. Here we show that hyperosmotic shock induces rapid calpain activation and high levels of Smac/DIABLO release from the mitochondri...

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Autores: Ben Messaoud, Nabil, Yue, Jicheng, Valent, Daniel|||0000-0001-6927-3099, Katzarova, Ilina, López Blanco, José Manuel|||0000-0002-4104-6262
Formato: artículo
Fecha de publicación:2015
País:España
Recursos:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:170666
Acesso em linha:https://ddd.uab.cat/record/170666
https://dx.doi.org/urn:doi:10.1371/journal.pone.0124482
Access Level:acceso abierto
Palavra-chave:Xenopus oocytes
Apoptosis
Mitochondria
Oocytes
Osmotic shock
Phosphorylation
Protein kinases
Cytosol
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spelling Osmostress-Induced Apoptosis in Xenopus OocytesRole of Stress Protein Kinases, Calpains and Smac/DIABLOBen Messaoud, NabilYue, JichengValent, Daniel|||0000-0001-6927-3099Katzarova, IlinaLópez Blanco, José Manuel|||0000-0002-4104-6262Xenopus oocytesApoptosisMitochondriaOocytesOsmotic shockPhosphorylationProtein kinasesCytosolHyperosmotic shock induces cytochrome c release and capase-3 activation in Xenopus oocytes, but the regulators and signaling pathways involved are not well characterized. Here we show that hyperosmotic shock induces rapid calpain activation and high levels of Smac/DIABLO release from the mitochondria before significant amounts of cytochrome c are released to promote caspase-3 activation. Calpain inhibitors or EGTA microinjection delays osmostress-induced apoptosis, and blockage of Smac/DIABLO with antibodies markedly reduces cytochrome c release and caspase-3 activation. Hyperosmotic shock also activates the p38 and JNK signaling pathways very quickly. Simultaneous inhibition of both p38 and JNK pathways reduces osmostress-induced apoptosis, while sustained activation of these kinases accelerates the release of cytochrome c and caspase-3 activation. Therefore, at least four different pathways early induced by osmostress converge on the mitochondria to trigger apoptosis. Deciphering the mechanisms of hyperosmotic shock-induced apoptosis gives insight for potential treatments of human diseases that are caused by perturbations in fluid osmolarity. 22015-01-0120152015-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/170666https://dx.doi.org/urn:doi:10.1371/journal.pone.0124482reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengopen accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, fins i tot amb finalitats comercials, sempre i quan es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by/3.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:1706662026-06-06T12:50:31Z
dc.title.none.fl_str_mv Osmostress-Induced Apoptosis in Xenopus Oocytes
Role of Stress Protein Kinases, Calpains and Smac/DIABLO
title Osmostress-Induced Apoptosis in Xenopus Oocytes
spellingShingle Osmostress-Induced Apoptosis in Xenopus Oocytes
Ben Messaoud, Nabil
Xenopus oocytes
Apoptosis
Mitochondria
Oocytes
Osmotic shock
Phosphorylation
Protein kinases
Cytosol
title_short Osmostress-Induced Apoptosis in Xenopus Oocytes
title_full Osmostress-Induced Apoptosis in Xenopus Oocytes
title_fullStr Osmostress-Induced Apoptosis in Xenopus Oocytes
title_full_unstemmed Osmostress-Induced Apoptosis in Xenopus Oocytes
title_sort Osmostress-Induced Apoptosis in Xenopus Oocytes
dc.creator.none.fl_str_mv Ben Messaoud, Nabil
Yue, Jicheng
Valent, Daniel|||0000-0001-6927-3099
Katzarova, Ilina
López Blanco, José Manuel|||0000-0002-4104-6262
author Ben Messaoud, Nabil
author_facet Ben Messaoud, Nabil
Yue, Jicheng
Valent, Daniel|||0000-0001-6927-3099
Katzarova, Ilina
López Blanco, José Manuel|||0000-0002-4104-6262
author_role author
author2 Yue, Jicheng
Valent, Daniel|||0000-0001-6927-3099
Katzarova, Ilina
López Blanco, José Manuel|||0000-0002-4104-6262
author2_role author
author
author
author
dc.subject.none.fl_str_mv Xenopus oocytes
Apoptosis
Mitochondria
Oocytes
Osmotic shock
Phosphorylation
Protein kinases
Cytosol
topic Xenopus oocytes
Apoptosis
Mitochondria
Oocytes
Osmotic shock
Phosphorylation
Protein kinases
Cytosol
description Hyperosmotic shock induces cytochrome c release and capase-3 activation in Xenopus oocytes, but the regulators and signaling pathways involved are not well characterized. Here we show that hyperosmotic shock induces rapid calpain activation and high levels of Smac/DIABLO release from the mitochondria before significant amounts of cytochrome c are released to promote caspase-3 activation. Calpain inhibitors or EGTA microinjection delays osmostress-induced apoptosis, and blockage of Smac/DIABLO with antibodies markedly reduces cytochrome c release and caspase-3 activation. Hyperosmotic shock also activates the p38 and JNK signaling pathways very quickly. Simultaneous inhibition of both p38 and JNK pathways reduces osmostress-induced apoptosis, while sustained activation of these kinases accelerates the release of cytochrome c and caspase-3 activation. Therefore, at least four different pathways early induced by osmostress converge on the mitochondria to trigger apoptosis. Deciphering the mechanisms of hyperosmotic shock-induced apoptosis gives insight for potential treatments of human diseases that are caused by perturbations in fluid osmolarity.
publishDate 2015
dc.date.none.fl_str_mv 2
2015-01-01
2015
2015-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://ddd.uab.cat/record/170666
https://dx.doi.org/urn:doi:10.1371/journal.pone.0124482
url https://ddd.uab.cat/record/170666
https://dx.doi.org/urn:doi:10.1371/journal.pone.0124482
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/3.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by/3.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300719

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