Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate
Autor(a) principal: | |
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Data de Publicação: | 2019 |
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/10400.1/12656 |
Resumo: | Polyoxometalates (POMs) are promising inorganic inhibitors for P-type ATPases. The experimental models used to study the effects of POMs on these ATPases are usually in vitro models using vesicles from several membrane sources. Very recently, some polyoxotungstates, such as the Dawson anion [P2W18O62]6-, were shown to be potent P-type ATPase inhibitors; being active in vitro as well as in ex-vivo. In the present study we broaden the spectrum of highly active inhibitors of Na+/K+-ATPase from basal membrane of epithelial skin to the bi-capped Keggin-type anion phosphotetradecavanadate Cs5.6H3.4PV14O42 (PV14) and we confront the data with activity of other commonly encountered polyoxovanadates, decavanadate (V10) and monovanadate (V1). The X-ray crystal structure of PV14 was solved and contains two trans-bicapped α-Keggin anions HxPV14O42(9-x)-. The anion is built up from the classical Keggin structure [(PO4)@(V12O36)] capped by two [VO] units. PV14 (10 μM) exhibited higher ex-vivo inhibitory effect on Na+/K+-ATPase (78%) than was observed at the same concentrations of V10 (66%) or V1 (33%). Moreover, PV14 is also a potent in vitro inhibitor of the Ca2+-ATPase activity (IC50 5 μM) exhibiting stronger inhibition than the previously reported activities for V10 (15 μM) and V1 (80 μM). Putting it all together, when compared both P-typye ATPases it is suggested that PV14 exibited a high potential to act as an in vivo inhibitor of the Na+/K+-ATPase associated with chloride secretion. |
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Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadatePolyoxometalatesPhosphotetradecavanadateDecavanadateP-type ATPasesEpithelial chloride secretionPolyoxometalates (POMs) are promising inorganic inhibitors for P-type ATPases. The experimental models used to study the effects of POMs on these ATPases are usually in vitro models using vesicles from several membrane sources. Very recently, some polyoxotungstates, such as the Dawson anion [P2W18O62]6-, were shown to be potent P-type ATPase inhibitors; being active in vitro as well as in ex-vivo. In the present study we broaden the spectrum of highly active inhibitors of Na+/K+-ATPase from basal membrane of epithelial skin to the bi-capped Keggin-type anion phosphotetradecavanadate Cs5.6H3.4PV14O42 (PV14) and we confront the data with activity of other commonly encountered polyoxovanadates, decavanadate (V10) and monovanadate (V1). The X-ray crystal structure of PV14 was solved and contains two trans-bicapped α-Keggin anions HxPV14O42(9-x)-. The anion is built up from the classical Keggin structure [(PO4)@(V12O36)] capped by two [VO] units. PV14 (10 μM) exhibited higher ex-vivo inhibitory effect on Na+/K+-ATPase (78%) than was observed at the same concentrations of V10 (66%) or V1 (33%). Moreover, PV14 is also a potent in vitro inhibitor of the Ca2+-ATPase activity (IC50 5 μM) exhibiting stronger inhibition than the previously reported activities for V10 (15 μM) and V1 (80 μM). Putting it all together, when compared both P-typye ATPases it is suggested that PV14 exibited a high potential to act as an in vivo inhibitor of the Na+/K+-ATPase associated with chloride secretion.FCT, Foundation for Science and Technology (UID/Multi/04326/2013) ; (SFRH/BSAB/129821/2017) Austrian Science Fund (FWF) (P27534) (M2200) Council of Scientific & Industrial Research (CSIR) (01(2906)/17/EMR-II) Grant Agency of the Ministry of Education of the Slovak Republic and Slovak Academy of Sciences VEGA (1/0507/17)ElsevierSapientiaFraqueza, GilFuentes, JuanKrivosudský, LukášDutta, SaikatMal, Sib SankarRoller, AlexanderGiester, GeraldRompel, AnnetteAureliano, Manuel2019-07-12T12:53:12Z20192019-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/12656eng0162-013410.1016/j.jinorgbio.2019.110700info: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:RCAAP2023-07-24T10:24:38Zoai:sapientia.ualg.pt:10400.1/12656Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:03:58.082015Repositório 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 |
Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate |
title |
Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate |
spellingShingle |
Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate Fraqueza, Gil Polyoxometalates Phosphotetradecavanadate Decavanadate P-type ATPases Epithelial chloride secretion |
title_short |
Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate |
title_full |
Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate |
title_fullStr |
Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate |
title_full_unstemmed |
Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate |
title_sort |
Inhibition of Na+/K+- and Ca2+-ATPase activities by phosphotetradecavanadate |
author |
Fraqueza, Gil |
author_facet |
Fraqueza, Gil Fuentes, Juan Krivosudský, Lukáš Dutta, Saikat Mal, Sib Sankar Roller, Alexander Giester, Gerald Rompel, Annette Aureliano, Manuel |
author_role |
author |
author2 |
Fuentes, Juan Krivosudský, Lukáš Dutta, Saikat Mal, Sib Sankar Roller, Alexander Giester, Gerald Rompel, Annette Aureliano, Manuel |
author2_role |
author author author author author author author author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Fraqueza, Gil Fuentes, Juan Krivosudský, Lukáš Dutta, Saikat Mal, Sib Sankar Roller, Alexander Giester, Gerald Rompel, Annette Aureliano, Manuel |
dc.subject.por.fl_str_mv |
Polyoxometalates Phosphotetradecavanadate Decavanadate P-type ATPases Epithelial chloride secretion |
topic |
Polyoxometalates Phosphotetradecavanadate Decavanadate P-type ATPases Epithelial chloride secretion |
description |
Polyoxometalates (POMs) are promising inorganic inhibitors for P-type ATPases. The experimental models used to study the effects of POMs on these ATPases are usually in vitro models using vesicles from several membrane sources. Very recently, some polyoxotungstates, such as the Dawson anion [P2W18O62]6-, were shown to be potent P-type ATPase inhibitors; being active in vitro as well as in ex-vivo. In the present study we broaden the spectrum of highly active inhibitors of Na+/K+-ATPase from basal membrane of epithelial skin to the bi-capped Keggin-type anion phosphotetradecavanadate Cs5.6H3.4PV14O42 (PV14) and we confront the data with activity of other commonly encountered polyoxovanadates, decavanadate (V10) and monovanadate (V1). The X-ray crystal structure of PV14 was solved and contains two trans-bicapped α-Keggin anions HxPV14O42(9-x)-. The anion is built up from the classical Keggin structure [(PO4)@(V12O36)] capped by two [VO] units. PV14 (10 μM) exhibited higher ex-vivo inhibitory effect on Na+/K+-ATPase (78%) than was observed at the same concentrations of V10 (66%) or V1 (33%). Moreover, PV14 is also a potent in vitro inhibitor of the Ca2+-ATPase activity (IC50 5 μM) exhibiting stronger inhibition than the previously reported activities for V10 (15 μM) and V1 (80 μM). Putting it all together, when compared both P-typye ATPases it is suggested that PV14 exibited a high potential to act as an in vivo inhibitor of the Na+/K+-ATPase associated with chloride secretion. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-07-12T12:53:12Z 2019 2019-01-01T00:00:00Z |
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/10400.1/12656 |
url |
http://hdl.handle.net/10400.1/12656 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0162-0134 10.1016/j.jinorgbio.2019.110700 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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 |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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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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