Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cells

Autores
Salice C., Viviana; Cortizo, Ana María; Gómez Dumm, César; Etcheverry, Susana B.
Año de publicación
1999
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The present study was performed to determine the phosphotyrosine-protein levels induced by insulin and by four vanadium derivatives in MC3T3E1 osteoblast-like cells. We have also attempted to associate these patterns with the vanadium-induced growth and morphological changes of such cells. Vanadate (Vi), vanadyl (VO), bis(maltolato)oxovanadium (IV) (BMOV) and bis(maltolato)dioxovanadium (V) (BMV) stimulate cell growth in a narrow range of concentration, but are also inhibitors for the cells at high concentrations. Vanadium-treated cells displayed clear changes in their morphology after overnight incubation. However, BMV was the least cytotoxic and the weakest inducer of morphological changes. All the compounds promote the phosphorylation of tyrosine residues in several proteins. This effect was more pronounced at low than at high doses. At low doses (10 μM), BMV showed a phosphorylation pattern similar to that of insulin, while Vi, VO and BMOV induced strong phosphorylation of cell proteins. The present findings suggest that the vanadium-induced growth regulation and morphological changes in MC3T3E1 osteoblast-like cells are associated with the ability of these agents to increase the phosphotyrosine protein levels and to inhibit phosphotyrosine phosphatases. These properties are dependent on the oxidation state as well as on the organic ligand which coordinates the vanadium atom.
Materia
Bioquímica y Biología Molecular
Vanadate
Vanadyl
Maltol complexes
Proliferation
Cytotoxicity
Tyrosin phosphorylation
Phosphotyrosine phosphatases
Osteoblast-like cells
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
CIC Digital (CICBA)
Institución
Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
OAI Identificador
oai:digital.cic.gba.gob.ar:11746/11950

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network_acronym_str CICBA
repository_id_str 9441
network_name_str CIC Digital (CICBA)
spelling Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cellsSalice C., VivianaCortizo, Ana MaríaGómez Dumm, CésarEtcheverry, Susana B.Bioquímica y Biología MolecularVanadateVanadylMaltol complexesProliferationCytotoxicityTyrosin phosphorylationPhosphotyrosine phosphatasesOsteoblast-like cellsThe present study was performed to determine the phosphotyrosine-protein levels induced by insulin and by four vanadium derivatives in MC3T3E1 osteoblast-like cells. We have also attempted to associate these patterns with the vanadium-induced growth and morphological changes of such cells. Vanadate (Vi), vanadyl (VO), bis(maltolato)oxovanadium (IV) (BMOV) and bis(maltolato)dioxovanadium (V) (BMV) stimulate cell growth in a narrow range of concentration, but are also inhibitors for the cells at high concentrations. Vanadium-treated cells displayed clear changes in their morphology after overnight incubation. However, BMV was the least cytotoxic and the weakest inducer of morphological changes. All the compounds promote the phosphorylation of tyrosine residues in several proteins. This effect was more pronounced at low than at high doses. At low doses (10 μM), BMV showed a phosphorylation pattern similar to that of insulin, while Vi, VO and BMOV induced strong phosphorylation of cell proteins. The present findings suggest that the vanadium-induced growth regulation and morphological changes in MC3T3E1 osteoblast-like cells are associated with the ability of these agents to increase the phosphotyrosine protein levels and to inhibit phosphotyrosine phosphatases. These properties are dependent on the oxidation state as well as on the organic ligand which coordinates the vanadium atom.1999info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://digital.cic.gba.gob.ar/handle/11746/11950enginfo:eu-repo/semantics/altIdentifier/issn/0300-8177info:eu-repo/semantics/altIdentifier/issn/1573-4919info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/reponame:CIC Digital (CICBA)instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Airesinstacron:CICBA2025-10-23T11:14:17Zoai:digital.cic.gba.gob.ar:11746/11950Institucionalhttp://digital.cic.gba.gob.arOrganismo científico-tecnológicoNo correspondehttp://digital.cic.gba.gob.ar/oai/snrdmarisa.degiusti@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:94412025-10-23 11:14:18.142CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Airesfalse
dc.title.none.fl_str_mv Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cells
title Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cells
spellingShingle Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cells
Salice C., Viviana
Bioquímica y Biología Molecular
Vanadate
Vanadyl
Maltol complexes
Proliferation
Cytotoxicity
Tyrosin phosphorylation
Phosphotyrosine phosphatases
Osteoblast-like cells
title_short Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cells
title_full Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cells
title_fullStr Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cells
title_full_unstemmed Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cells
title_sort Tyrosine phosphorylation and morphological transformation induced by four vanadium compounds on MC3T3E1 cells
dc.creator.none.fl_str_mv Salice C., Viviana
Cortizo, Ana María
Gómez Dumm, César
Etcheverry, Susana B.
author Salice C., Viviana
author_facet Salice C., Viviana
Cortizo, Ana María
Gómez Dumm, César
Etcheverry, Susana B.
author_role author
author2 Cortizo, Ana María
Gómez Dumm, César
Etcheverry, Susana B.
author2_role author
author
author
dc.subject.none.fl_str_mv Bioquímica y Biología Molecular
Vanadate
Vanadyl
Maltol complexes
Proliferation
Cytotoxicity
Tyrosin phosphorylation
Phosphotyrosine phosphatases
Osteoblast-like cells
topic Bioquímica y Biología Molecular
Vanadate
Vanadyl
Maltol complexes
Proliferation
Cytotoxicity
Tyrosin phosphorylation
Phosphotyrosine phosphatases
Osteoblast-like cells
dc.description.none.fl_txt_mv The present study was performed to determine the phosphotyrosine-protein levels induced by insulin and by four vanadium derivatives in MC3T3E1 osteoblast-like cells. We have also attempted to associate these patterns with the vanadium-induced growth and morphological changes of such cells. Vanadate (Vi), vanadyl (VO), bis(maltolato)oxovanadium (IV) (BMOV) and bis(maltolato)dioxovanadium (V) (BMV) stimulate cell growth in a narrow range of concentration, but are also inhibitors for the cells at high concentrations. Vanadium-treated cells displayed clear changes in their morphology after overnight incubation. However, BMV was the least cytotoxic and the weakest inducer of morphological changes. All the compounds promote the phosphorylation of tyrosine residues in several proteins. This effect was more pronounced at low than at high doses. At low doses (10 μM), BMV showed a phosphorylation pattern similar to that of insulin, while Vi, VO and BMOV induced strong phosphorylation of cell proteins. The present findings suggest that the vanadium-induced growth regulation and morphological changes in MC3T3E1 osteoblast-like cells are associated with the ability of these agents to increase the phosphotyrosine protein levels and to inhibit phosphotyrosine phosphatases. These properties are dependent on the oxidation state as well as on the organic ligand which coordinates the vanadium atom.
description The present study was performed to determine the phosphotyrosine-protein levels induced by insulin and by four vanadium derivatives in MC3T3E1 osteoblast-like cells. We have also attempted to associate these patterns with the vanadium-induced growth and morphological changes of such cells. Vanadate (Vi), vanadyl (VO), bis(maltolato)oxovanadium (IV) (BMOV) and bis(maltolato)dioxovanadium (V) (BMV) stimulate cell growth in a narrow range of concentration, but are also inhibitors for the cells at high concentrations. Vanadium-treated cells displayed clear changes in their morphology after overnight incubation. However, BMV was the least cytotoxic and the weakest inducer of morphological changes. All the compounds promote the phosphorylation of tyrosine residues in several proteins. This effect was more pronounced at low than at high doses. At low doses (10 μM), BMV showed a phosphorylation pattern similar to that of insulin, while Vi, VO and BMOV induced strong phosphorylation of cell proteins. The present findings suggest that the vanadium-induced growth regulation and morphological changes in MC3T3E1 osteoblast-like cells are associated with the ability of these agents to increase the phosphotyrosine protein levels and to inhibit phosphotyrosine phosphatases. These properties are dependent on the oxidation state as well as on the organic ligand which coordinates the vanadium atom.
publishDate 1999
dc.date.none.fl_str_mv 1999
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://digital.cic.gba.gob.ar/handle/11746/11950
url https://digital.cic.gba.gob.ar/handle/11746/11950
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0300-8177
info:eu-repo/semantics/altIdentifier/issn/1573-4919
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:CIC Digital (CICBA)
instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron:CICBA
reponame_str CIC Digital (CICBA)
collection CIC Digital (CICBA)
instname_str Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
instacron_str CICBA
institution CICBA
repository.name.fl_str_mv CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
repository.mail.fl_str_mv marisa.degiusti@sedici.unlp.edu.ar
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