Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling

Detalhes bibliográficos
Autor(a) principal: Guimarães, Paola Bianchi [UNIFESP]
Data de Publicação: 2011
Outros Autores: Alvarenga, Erika Costa [UNIFESP], Siqueira, Paula D. [UNIFESP], Paredes-Gamero, Edgar Julian [UNIFESP], Sabatini, Regiane Angelica [UNIFESP], Morais, Rafael Leite Tavares de [UNIFESP], Reis, Rosana I., Santos, Edson L., Teixeira, Luis Gustavo de Deus [UNIFESP], Casarini, Dulce Elena [UNIFESP], Martin, Renan Paulo [UNIFESP], Shimuta, Suma Imura [UNIFESP], Carmona, Adriana Karaoglanovic [UNIFESP], Nakaie, Clovis Ryuichi [UNIFESP], Jasiulionis, Miriam Galvonas [UNIFESP], Ferreira, Alice Teixeira [UNIFESP], Pesquero, Jorge L., Oliveira, Suzana M. [UNIFESP], Bader, Michael [UNIFESP], Costa-Neto, Claudio M., Pesquero, João Bosco [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
dARK ID: ark:/48912/001300000j8q0
Texto Completo: http://dx.doi.org/10.1161/HYPERTENSIONAHA.110.167171
http://repositorio.unifesp.br/handle/11600/33657
Resumo: Angiotensin (Ang) I-converting enzyme (ACE) is involved in the control of blood pressure by catalyzing the conversion of Ang I into the vasoconstrictor Ang II and degrading the vasodilator peptide bradykinin. Human ACE also functions as a signal transduction molecule, and the binding of ACE substrates or its inhibitors initiates a series of events. in this study, we examined whether Ang II could bind to ACE generating calcium signaling. Chinese hamster ovary cells transfected with an ACE expression vector reveal that Ang II is able to bind with high affinity to ACE in the absence of the Ang II type 1 and type 2 receptors and to activate intracellular signaling pathways, such as inositol 1,4,5-trisphosphate and calcium. These effects could be blocked by the ACE inhibitor, lisinopril. Calcium mobilization was specific for Ang II, because other ACE substrates or products, namely Ang 1-7, bradykinin, bradykinin 1-5, and N-acetyl-seryl-aspartyl-lysyl-proline, did not trigger this signaling pathway. Moreover, in Tm5, a mouse melanoma cell line endogenously expressing ACE but not Ang II type 1 or type 2 receptors, Ang II increased intracellular calcium and reactive oxygen species. in conclusion, we describe for the first time that Ang II can interact with ACE and evoke calcium and other signaling molecules in cells expressing only ACE. These findings uncover a new mechanism of Ang II action and have implications for the understanding of the renin-Ang system. (Hypertension. 2011;57:965-972.) . Online Data Supplement
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spelling Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signalingangiotensin I-converting enzymeACEcalciumangiotensincellsreceptorsAngiotensin (Ang) I-converting enzyme (ACE) is involved in the control of blood pressure by catalyzing the conversion of Ang I into the vasoconstrictor Ang II and degrading the vasodilator peptide bradykinin. Human ACE also functions as a signal transduction molecule, and the binding of ACE substrates or its inhibitors initiates a series of events. in this study, we examined whether Ang II could bind to ACE generating calcium signaling. Chinese hamster ovary cells transfected with an ACE expression vector reveal that Ang II is able to bind with high affinity to ACE in the absence of the Ang II type 1 and type 2 receptors and to activate intracellular signaling pathways, such as inositol 1,4,5-trisphosphate and calcium. These effects could be blocked by the ACE inhibitor, lisinopril. Calcium mobilization was specific for Ang II, because other ACE substrates or products, namely Ang 1-7, bradykinin, bradykinin 1-5, and N-acetyl-seryl-aspartyl-lysyl-proline, did not trigger this signaling pathway. Moreover, in Tm5, a mouse melanoma cell line endogenously expressing ACE but not Ang II type 1 or type 2 receptors, Ang II increased intracellular calcium and reactive oxygen species. in conclusion, we describe for the first time that Ang II can interact with ACE and evoke calcium and other signaling molecules in cells expressing only ACE. These findings uncover a new mechanism of Ang II action and have implications for the understanding of the renin-Ang system. (Hypertension. 2011;57:965-972.) . Online Data SupplementUniversidade Federal de São Paulo, Dept Biofis, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Med, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Farmacol, BR-04023062 São Paulo, BrazilUniv São Paulo, Fac Med Ribeirao Preto, Dept Bioquim & Imunol, São Paulo, BrazilFundacao Univ Fed Grande Dourados, Fac Ciencias Biol & Ambientais, Mato Grosso, BrazilMax Delbruck Ctr Mol Med, Berlin, GermanyUniversidade Federal de São Paulo, Dept Biofis, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Med, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Farmacol, BR-04023062 São Paulo, BrazilWeb of ScienceFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Deutsche Akademische Austauchdienst ProbralFAPESP: 02/00807-7CNPq: 520012/02-0Lippincott Williams & WilkinsUniversidade Federal de São Paulo (UNIFESP)Universidade de São Paulo (USP)Fundacao Univ Fed Grande DouradosMax Delbruck Ctr Mol MedGuimarães, Paola Bianchi [UNIFESP]Alvarenga, Erika Costa [UNIFESP]Siqueira, Paula D. [UNIFESP]Paredes-Gamero, Edgar Julian [UNIFESP]Sabatini, Regiane Angelica [UNIFESP]Morais, Rafael Leite Tavares de [UNIFESP]Reis, Rosana I.Santos, Edson L.Teixeira, Luis Gustavo de Deus [UNIFESP]Casarini, Dulce Elena [UNIFESP]Martin, Renan Paulo [UNIFESP]Shimuta, Suma Imura [UNIFESP]Carmona, Adriana Karaoglanovic [UNIFESP]Nakaie, Clovis Ryuichi [UNIFESP]Jasiulionis, Miriam Galvonas [UNIFESP]Ferreira, Alice Teixeira [UNIFESP]Pesquero, Jorge L.Oliveira, Suzana M. [UNIFESP]Bader, Michael [UNIFESP]Costa-Neto, Claudio M.Pesquero, João Bosco [UNIFESP]2016-01-24T14:16:40Z2016-01-24T14:16:40Z2011-05-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion965-U200http://dx.doi.org/10.1161/HYPERTENSIONAHA.110.167171Hypertension. Philadelphia: Lippincott Williams & Wilkins, v. 57, n. 5, p. 965-U200, 2011.10.1161/HYPERTENSIONAHA.110.1671710194-911Xhttp://repositorio.unifesp.br/handle/11600/33657WOS:000289730200024ark:/48912/001300000j8q0engHypertensioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2023-05-18T14:58:10Zoai:repositorio.unifesp.br/:11600/33657Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-12-11T20:20:52.529949Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling
title Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling
spellingShingle Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling
Guimarães, Paola Bianchi [UNIFESP]
angiotensin I-converting enzyme
ACE
calcium
angiotensin
cells
receptors
title_short Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling
title_full Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling
title_fullStr Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling
title_full_unstemmed Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling
title_sort Angiotensin II Binding to Angiotensin I-Converting Enzyme Triggers Calcium Signaling
author Guimarães, Paola Bianchi [UNIFESP]
author_facet Guimarães, Paola Bianchi [UNIFESP]
Alvarenga, Erika Costa [UNIFESP]
Siqueira, Paula D. [UNIFESP]
Paredes-Gamero, Edgar Julian [UNIFESP]
Sabatini, Regiane Angelica [UNIFESP]
Morais, Rafael Leite Tavares de [UNIFESP]
Reis, Rosana I.
Santos, Edson L.
Teixeira, Luis Gustavo de Deus [UNIFESP]
Casarini, Dulce Elena [UNIFESP]
Martin, Renan Paulo [UNIFESP]
Shimuta, Suma Imura [UNIFESP]
Carmona, Adriana Karaoglanovic [UNIFESP]
Nakaie, Clovis Ryuichi [UNIFESP]
Jasiulionis, Miriam Galvonas [UNIFESP]
Ferreira, Alice Teixeira [UNIFESP]
Pesquero, Jorge L.
Oliveira, Suzana M. [UNIFESP]
Bader, Michael [UNIFESP]
Costa-Neto, Claudio M.
Pesquero, João Bosco [UNIFESP]
author_role author
author2 Alvarenga, Erika Costa [UNIFESP]
Siqueira, Paula D. [UNIFESP]
Paredes-Gamero, Edgar Julian [UNIFESP]
Sabatini, Regiane Angelica [UNIFESP]
Morais, Rafael Leite Tavares de [UNIFESP]
Reis, Rosana I.
Santos, Edson L.
Teixeira, Luis Gustavo de Deus [UNIFESP]
Casarini, Dulce Elena [UNIFESP]
Martin, Renan Paulo [UNIFESP]
Shimuta, Suma Imura [UNIFESP]
Carmona, Adriana Karaoglanovic [UNIFESP]
Nakaie, Clovis Ryuichi [UNIFESP]
Jasiulionis, Miriam Galvonas [UNIFESP]
Ferreira, Alice Teixeira [UNIFESP]
Pesquero, Jorge L.
Oliveira, Suzana M. [UNIFESP]
Bader, Michael [UNIFESP]
Costa-Neto, Claudio M.
Pesquero, João Bosco [UNIFESP]
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Fundacao Univ Fed Grande Dourados
Max Delbruck Ctr Mol Med
dc.contributor.author.fl_str_mv Guimarães, Paola Bianchi [UNIFESP]
Alvarenga, Erika Costa [UNIFESP]
Siqueira, Paula D. [UNIFESP]
Paredes-Gamero, Edgar Julian [UNIFESP]
Sabatini, Regiane Angelica [UNIFESP]
Morais, Rafael Leite Tavares de [UNIFESP]
Reis, Rosana I.
Santos, Edson L.
Teixeira, Luis Gustavo de Deus [UNIFESP]
Casarini, Dulce Elena [UNIFESP]
Martin, Renan Paulo [UNIFESP]
Shimuta, Suma Imura [UNIFESP]
Carmona, Adriana Karaoglanovic [UNIFESP]
Nakaie, Clovis Ryuichi [UNIFESP]
Jasiulionis, Miriam Galvonas [UNIFESP]
Ferreira, Alice Teixeira [UNIFESP]
Pesquero, Jorge L.
Oliveira, Suzana M. [UNIFESP]
Bader, Michael [UNIFESP]
Costa-Neto, Claudio M.
Pesquero, João Bosco [UNIFESP]
dc.subject.por.fl_str_mv angiotensin I-converting enzyme
ACE
calcium
angiotensin
cells
receptors
topic angiotensin I-converting enzyme
ACE
calcium
angiotensin
cells
receptors
description Angiotensin (Ang) I-converting enzyme (ACE) is involved in the control of blood pressure by catalyzing the conversion of Ang I into the vasoconstrictor Ang II and degrading the vasodilator peptide bradykinin. Human ACE also functions as a signal transduction molecule, and the binding of ACE substrates or its inhibitors initiates a series of events. in this study, we examined whether Ang II could bind to ACE generating calcium signaling. Chinese hamster ovary cells transfected with an ACE expression vector reveal that Ang II is able to bind with high affinity to ACE in the absence of the Ang II type 1 and type 2 receptors and to activate intracellular signaling pathways, such as inositol 1,4,5-trisphosphate and calcium. These effects could be blocked by the ACE inhibitor, lisinopril. Calcium mobilization was specific for Ang II, because other ACE substrates or products, namely Ang 1-7, bradykinin, bradykinin 1-5, and N-acetyl-seryl-aspartyl-lysyl-proline, did not trigger this signaling pathway. Moreover, in Tm5, a mouse melanoma cell line endogenously expressing ACE but not Ang II type 1 or type 2 receptors, Ang II increased intracellular calcium and reactive oxygen species. in conclusion, we describe for the first time that Ang II can interact with ACE and evoke calcium and other signaling molecules in cells expressing only ACE. These findings uncover a new mechanism of Ang II action and have implications for the understanding of the renin-Ang system. (Hypertension. 2011;57:965-972.) . Online Data Supplement
publishDate 2011
dc.date.none.fl_str_mv 2011-05-01
2016-01-24T14:16:40Z
2016-01-24T14:16:40Z
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/10.1161/HYPERTENSIONAHA.110.167171
Hypertension. Philadelphia: Lippincott Williams & Wilkins, v. 57, n. 5, p. 965-U200, 2011.
10.1161/HYPERTENSIONAHA.110.167171
0194-911X
http://repositorio.unifesp.br/handle/11600/33657
WOS:000289730200024
dc.identifier.dark.fl_str_mv ark:/48912/001300000j8q0
url http://dx.doi.org/10.1161/HYPERTENSIONAHA.110.167171
http://repositorio.unifesp.br/handle/11600/33657
identifier_str_mv Hypertension. Philadelphia: Lippincott Williams & Wilkins, v. 57, n. 5, p. 965-U200, 2011.
10.1161/HYPERTENSIONAHA.110.167171
0194-911X
WOS:000289730200024
ark:/48912/001300000j8q0
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Hypertension
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 965-U200
dc.publisher.none.fl_str_mv Lippincott Williams & Wilkins
publisher.none.fl_str_mv Lippincott Williams & Wilkins
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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