A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studies
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.1/1449 |
Resumo: | The studies about the interaction of actin with vanadium are seldom. In the present paper the effects of vanadyl, vanadate, and decavanadate in the actin structure and function were compared. Decavanadate clearly interacts with actin, as shown by 51V-NMR spectroscopy. Decavanadate interaction with actin induces protein cysteine oxidation and vanadyl formation, being both prevented by the natural ligand of the protein, ATP. Monomeric actin (G-actin) titration with vanadyl, as analysed by EPR spectroscopy, indicates a 1 : 1 binding stoichiometry and a kd of 7.5 μM. Both decavanadate and vanadyl inhibited G-actin polymerization into actin filaments (F-actin), with a IC50 of 68 and 300 μM, respectively, as analysed by light-scattering assays. However, only vanadyl induces G-actin intrinsic fluorescence quenching, which suggests the presence of vanadyl high-affinity actin-binding sites. Decavanadate increases (2.6-fold) actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Finally, both vanadium species increased ε-ATP exchange rate (k = 6.5 × 10−3 and 4.47 × 10−3 s−1 for decavanadate and vanadyl, resp.). Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl. |
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A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studiesVanadylActinThe studies about the interaction of actin with vanadium are seldom. In the present paper the effects of vanadyl, vanadate, and decavanadate in the actin structure and function were compared. Decavanadate clearly interacts with actin, as shown by 51V-NMR spectroscopy. Decavanadate interaction with actin induces protein cysteine oxidation and vanadyl formation, being both prevented by the natural ligand of the protein, ATP. Monomeric actin (G-actin) titration with vanadyl, as analysed by EPR spectroscopy, indicates a 1 : 1 binding stoichiometry and a kd of 7.5 μM. Both decavanadate and vanadyl inhibited G-actin polymerization into actin filaments (F-actin), with a IC50 of 68 and 300 μM, respectively, as analysed by light-scattering assays. However, only vanadyl induces G-actin intrinsic fluorescence quenching, which suggests the presence of vanadyl high-affinity actin-binding sites. Decavanadate increases (2.6-fold) actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Finally, both vanadium species increased ε-ATP exchange rate (k = 6.5 × 10−3 and 4.47 × 10−3 s−1 for decavanadate and vanadyl, resp.). Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl.Hindawi Publishing CorporationSapientiaAureliano, M.2012-07-16T11:28:16Z20122012-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/1449eng1875-922Xinfo: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:RCAAP2023-07-24T10:12:34Zoai:sapientia.ualg.pt:10400.1/1449Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:55:39.780741Repositório 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 |
A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studies |
title |
A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studies |
spellingShingle |
A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studies Aureliano, M. Vanadyl Actin |
title_short |
A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studies |
title_full |
A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studies |
title_fullStr |
A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studies |
title_full_unstemmed |
A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studies |
title_sort |
A comparison between Vanadyl, Vanadate, and decavanadate effects in actin structure and function: combination of several spectroscopic studies |
author |
Aureliano, M. |
author_facet |
Aureliano, M. |
author_role |
author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Aureliano, M. |
dc.subject.por.fl_str_mv |
Vanadyl Actin |
topic |
Vanadyl Actin |
description |
The studies about the interaction of actin with vanadium are seldom. In the present paper the effects of vanadyl, vanadate, and decavanadate in the actin structure and function were compared. Decavanadate clearly interacts with actin, as shown by 51V-NMR spectroscopy. Decavanadate interaction with actin induces protein cysteine oxidation and vanadyl formation, being both prevented by the natural ligand of the protein, ATP. Monomeric actin (G-actin) titration with vanadyl, as analysed by EPR spectroscopy, indicates a 1 : 1 binding stoichiometry and a kd of 7.5 μM. Both decavanadate and vanadyl inhibited G-actin polymerization into actin filaments (F-actin), with a IC50 of 68 and 300 μM, respectively, as analysed by light-scattering assays. However, only vanadyl induces G-actin intrinsic fluorescence quenching, which suggests the presence of vanadyl high-affinity actin-binding sites. Decavanadate increases (2.6-fold) actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Finally, both vanadium species increased ε-ATP exchange rate (k = 6.5 × 10−3 and 4.47 × 10−3 s−1 for decavanadate and vanadyl, resp.). Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-07-16T11:28:16Z 2012 2012-01-01T00:00:00Z |
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/10400.1/1449 |
url |
http://hdl.handle.net/10400.1/1449 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
1875-922X |
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 |
Hindawi Publishing Corporation |
publisher.none.fl_str_mv |
Hindawi Publishing Corporation |
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 |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799133159346929664 |