Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells

Autores
León, Ignacio Esteban; Díez, Paula; Baran, Enrique José; Etcheverry, Susana Beatriz; Fuentes, Manuel
Año de publicación
2017
Idioma
inglés
Tipo de recurso
conjunto de datos
Estado
versión publicada
Descripción
Vanadium compounds were studied in recent years by considering them as a representative of a new class of non-platinum metal anticancer drugs. However, a few challenges still remain in the discovery of new molecular targets of these new metallodrugs. Studies on cell signaling pathways related to vanadium compounds have scarcely been reported and so far this information is highly critical for identifying novel targets that play a key role in the antitumor actions of vanadium complexes. This research deals with the alterations in the intracellular signaling pathways promoted by an oxovanadium(IV) complex with the clioquinol (5-chloro-7-iodo-8-quinolinol), VO(CQ)2, on a human osteosarcoma cell line (MG-63). Herein are reported, for the first time, the antitumor properties of VO(CQ)2 and the relative abundance of 224 proteins (which are involved in most of the common intracellular pathways) to identify novel targets of the studied complex. Besides, full-length human recombinant AKT1 kinase was produced by using an IVTT system to evaluate the variation of relative tyrosin-phosphorylation levels caused by this compound. The results of the differential protein expression levels reveal several up-regulated proteins such as CASP3, CASP6, CASP7, CASP10, CASP11, Bcl-x, DAPK and down-regulated ones, such as PKB/AKT, DIABLO, among others. Moreover, cell signaling pathways involved in several altered pathways related to the PKC and AP2 family have been identified in both treatments (2.5 and 10 μM) suggesting the crucial antitumoral role of VO(CQ)2. Finally, it has been demonstrated that this compound (10 μM, 6 h) triggers a decrease of 2-fold in in situ AKT1 expression.
Fil: Baran, Enrique José. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica; Argentina.
Fil: Etcheverry, Susana Beatriz. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica; Argentina.
Fil: León, Ignacio Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; Argentina
Facultad de Ciencias Exactas
Centro de Química Inorgánica
Materia
Ciencias Exactas
Química
Ciencias Médicas
vanadium
AKT
cancer
Osteosarcoma
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/108112
Acceder
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repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cellsLeón, Ignacio EstebanDíez, PaulaBaran, Enrique JoséEtcheverry, Susana BeatrizFuentes, ManuelCiencias ExactasQuímicaCiencias Médicashttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/3vanadiumAKTcancerOsteosarcomaVanadium compounds were studied in recent years by considering them as a representative of a new class of non-platinum metal anticancer drugs. However, a few challenges still remain in the discovery of new molecular targets of these new metallodrugs. Studies on cell signaling pathways related to vanadium compounds have scarcely been reported and so far this information is highly critical for identifying novel targets that play a key role in the antitumor actions of vanadium complexes. This research deals with the alterations in the intracellular signaling pathways promoted by an oxovanadium(IV) complex with the clioquinol (5-chloro-7-iodo-8-quinolinol), VO(CQ)<sub>2</sub>, on a human osteosarcoma cell line (MG-63). Herein are reported, for the first time, the antitumor properties of VO(CQ)<sub>2</sub> and the relative abundance of 224 proteins (which are involved in most of the common intracellular pathways) to identify novel targets of the studied complex. Besides, full-length human recombinant AKT1 kinase was produced by using an IVTT system to evaluate the variation of relative tyrosin-phosphorylation levels caused by this compound. The results of the differential protein expression levels reveal several up-regulated proteins such as CASP3, CASP6, CASP7, CASP10, CASP11, Bcl-x, DAPK and down-regulated ones, such as PKB/AKT, DIABLO, among others. Moreover, cell signaling pathways involved in several altered pathways related to the PKC and AP2 family have been identified in both treatments (2.5 and 10 μM) suggesting the crucial antitumoral role of VO(CQ)<sub>2</sub>. Finally, it has been demonstrated that this compound (10 μM, 6 h) triggers a decrease of 2-fold in <i>in situ</i> AKT1 expression.Fil: Baran, Enrique José. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica; Argentina.Fil: Etcheverry, Susana Beatriz. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica; Argentina.Fil: León, Ignacio Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; ArgentinaFacultad de Ciencias ExactasCentro de Química Inorgánica2017info:eu-repo/semantics/publishedVersionConjunto de datoshttp://purl.org/coar/resource_type/c_ddb1info:ar-repo/semantics/conjuntoDeDatosinfo:eu-repo/semantics/dataSetapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/108112https://doi.org/10.35537/10915/108112enginfo:eu-repo/semantics/reference/hdl/10915/108044info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:24:27Zoai:sedici.unlp.edu.ar:10915/108112Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:24:27.789SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells
title Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells
spellingShingle Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells
León, Ignacio Esteban
Ciencias Exactas
Química
Ciencias Médicas
vanadium
AKT
cancer
Osteosarcoma
title_short Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells
title_full Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells
title_fullStr Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells
title_full_unstemmed Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells
title_sort Data from: Decoding the anticancer activity of VO-clioquinol compound: the mechanism of action and cell death pathways in human osteosarcoma cells
dc.creator.none.fl_str_mv León, Ignacio Esteban
Díez, Paula
Baran, Enrique José
Etcheverry, Susana Beatriz
Fuentes, Manuel
author León, Ignacio Esteban
author_facet León, Ignacio Esteban
Díez, Paula
Baran, Enrique José
Etcheverry, Susana Beatriz
Fuentes, Manuel
author_role author
author2 Díez, Paula
Baran, Enrique José
Etcheverry, Susana Beatriz
Fuentes, Manuel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Química
Ciencias Médicas
vanadium
AKT
cancer
Osteosarcoma
topic Ciencias Exactas
Química
Ciencias Médicas
vanadium
AKT
cancer
Osteosarcoma
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Vanadium compounds were studied in recent years by considering them as a representative of a new class of non-platinum metal anticancer drugs. However, a few challenges still remain in the discovery of new molecular targets of these new metallodrugs. Studies on cell signaling pathways related to vanadium compounds have scarcely been reported and so far this information is highly critical for identifying novel targets that play a key role in the antitumor actions of vanadium complexes. This research deals with the alterations in the intracellular signaling pathways promoted by an oxovanadium(IV) complex with the clioquinol (5-chloro-7-iodo-8-quinolinol), VO(CQ)<sub>2</sub>, on a human osteosarcoma cell line (MG-63). Herein are reported, for the first time, the antitumor properties of VO(CQ)<sub>2</sub> and the relative abundance of 224 proteins (which are involved in most of the common intracellular pathways) to identify novel targets of the studied complex. Besides, full-length human recombinant AKT1 kinase was produced by using an IVTT system to evaluate the variation of relative tyrosin-phosphorylation levels caused by this compound. The results of the differential protein expression levels reveal several up-regulated proteins such as CASP3, CASP6, CASP7, CASP10, CASP11, Bcl-x, DAPK and down-regulated ones, such as PKB/AKT, DIABLO, among others. Moreover, cell signaling pathways involved in several altered pathways related to the PKC and AP2 family have been identified in both treatments (2.5 and 10 μM) suggesting the crucial antitumoral role of VO(CQ)<sub>2</sub>. Finally, it has been demonstrated that this compound (10 μM, 6 h) triggers a decrease of 2-fold in <i>in situ</i> AKT1 expression.
Fil: Baran, Enrique José. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica; Argentina.
Fil: Etcheverry, Susana Beatriz. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica; Argentina.
Fil: León, Ignacio Esteban. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Química Inorgánica "Dr. Pedro J. Aymonino". Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Química Inorgánica "Dr. Pedro J. Aymonino"; Argentina
Facultad de Ciencias Exactas
Centro de Química Inorgánica
description Vanadium compounds were studied in recent years by considering them as a representative of a new class of non-platinum metal anticancer drugs. However, a few challenges still remain in the discovery of new molecular targets of these new metallodrugs. Studies on cell signaling pathways related to vanadium compounds have scarcely been reported and so far this information is highly critical for identifying novel targets that play a key role in the antitumor actions of vanadium complexes. This research deals with the alterations in the intracellular signaling pathways promoted by an oxovanadium(IV) complex with the clioquinol (5-chloro-7-iodo-8-quinolinol), VO(CQ)<sub>2</sub>, on a human osteosarcoma cell line (MG-63). Herein are reported, for the first time, the antitumor properties of VO(CQ)<sub>2</sub> and the relative abundance of 224 proteins (which are involved in most of the common intracellular pathways) to identify novel targets of the studied complex. Besides, full-length human recombinant AKT1 kinase was produced by using an IVTT system to evaluate the variation of relative tyrosin-phosphorylation levels caused by this compound. The results of the differential protein expression levels reveal several up-regulated proteins such as CASP3, CASP6, CASP7, CASP10, CASP11, Bcl-x, DAPK and down-regulated ones, such as PKB/AKT, DIABLO, among others. Moreover, cell signaling pathways involved in several altered pathways related to the PKC and AP2 family have been identified in both treatments (2.5 and 10 μM) suggesting the crucial antitumoral role of VO(CQ)<sub>2</sub>. Finally, it has been demonstrated that this compound (10 μM, 6 h) triggers a decrease of 2-fold in <i>in situ</i> AKT1 expression.
publishDate 2017
dc.date.none.fl_str_mv 2017
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
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https://doi.org/10.35537/10915/108112
dc.language.none.fl_str_mv eng
language eng
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dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
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