Effect of vanadium compounds on acid phosphatase activity

Autores
Vescina, Cecilia M.; Sálice, Viviana C.; Cortizo, Ana María; Etcheverry, Susana B.
Año de publicación
1996
Idioma
inglés
Tipo de recurso
artículo
Estado
versión enviada
Descripción
The direct effect of different vanadium compounds on acid phosphatase (ACP) activity was investigated. Vanadate and vanadyl but not pervanadate inhibited the wheat germ ACP activity. These vanadium derivatives did not alter the fibroblast Swiss 3T3 soluble fraction ACP activity. Using inhibitors of tyrosine phosphatases (PTPases), the wheat germ ACP was partially characterized as a PTPase. This study suggests that the inhibitory ability of different vanadium derivatives to modulate ACP activity seems to depend on the geometry around the vanadium atom more than on the oxidation state. Our results indicate a correlation between the PTPase activity and the sensitivity to vanadate and vanadyl cation.
Materia
Ciencias Químicas
Vanadium
acid phosphatase
Tyrosine-phosphatase
fibroblast cells
inhibitory effects
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/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:11746/4413
Acceder
id CICBA_dc745b309766724fc7135e54a421caa9
oai_identifier_str oai:digital.cic.gba.gob.ar:11746/4413
network_acronym_str CICBA
repository_id_str 9441
network_name_str CIC Digital (CICBA)
spelling Effect of vanadium compounds on acid phosphatase activityVescina, Cecilia M.Sálice, Viviana C.Cortizo, Ana MaríaEtcheverry, Susana B.Ciencias QuímicasVanadiumacid phosphataseTyrosine-phosphatasefibroblast cellsinhibitory effectsThe direct effect of different vanadium compounds on acid phosphatase (ACP) activity was investigated. Vanadate and vanadyl but not pervanadate inhibited the wheat germ ACP activity. These vanadium derivatives did not alter the fibroblast Swiss 3T3 soluble fraction ACP activity. Using inhibitors of tyrosine phosphatases (PTPases), the wheat germ ACP was partially characterized as a PTPase. This study suggests that the inhibitory ability of different vanadium derivatives to modulate ACP activity seems to depend on the geometry around the vanadium atom more than on the oxidation state. Our results indicate a correlation between the PTPase activity and the sensitivity to vanadate and vanadyl cation.1996info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttps://digital.cic.gba.gob.ar/handle/11746/4413enginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/reponame:CIC Digital (CICBA)instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Airesinstacron:CICBA2025-10-16T09:27:19Zoai:digital.cic.gba.gob.ar:11746/4413Institucionalhttp://digital.cic.gba.gob.arOrganismo científico-tecnológicoNo correspondehttp://digital.cic.gba.gob.ar/oai/snrdmarisa.degiusti@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:94412025-10-16 09:27:20.559CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Airesfalse
dc.title.none.fl_str_mv Effect of vanadium compounds on acid phosphatase activity
title Effect of vanadium compounds on acid phosphatase activity
spellingShingle Effect of vanadium compounds on acid phosphatase activity
Vescina, Cecilia M.
Ciencias Químicas
Vanadium
acid phosphatase
Tyrosine-phosphatase
fibroblast cells
inhibitory effects
title_short Effect of vanadium compounds on acid phosphatase activity
title_full Effect of vanadium compounds on acid phosphatase activity
title_fullStr Effect of vanadium compounds on acid phosphatase activity
title_full_unstemmed Effect of vanadium compounds on acid phosphatase activity
title_sort Effect of vanadium compounds on acid phosphatase activity
dc.creator.none.fl_str_mv Vescina, Cecilia M.
Sálice, Viviana C.
Cortizo, Ana María
Etcheverry, Susana B.
author Vescina, Cecilia M.
author_facet Vescina, Cecilia M.
Sálice, Viviana C.
Cortizo, Ana María
Etcheverry, Susana B.
author_role author
author2 Sálice, Viviana C.
Cortizo, Ana María
Etcheverry, Susana B.
author2_role author
author
author
dc.subject.none.fl_str_mv Ciencias Químicas
Vanadium
acid phosphatase
Tyrosine-phosphatase
fibroblast cells
inhibitory effects
topic Ciencias Químicas
Vanadium
acid phosphatase
Tyrosine-phosphatase
fibroblast cells
inhibitory effects
dc.description.none.fl_txt_mv The direct effect of different vanadium compounds on acid phosphatase (ACP) activity was investigated. Vanadate and vanadyl but not pervanadate inhibited the wheat germ ACP activity. These vanadium derivatives did not alter the fibroblast Swiss 3T3 soluble fraction ACP activity. Using inhibitors of tyrosine phosphatases (PTPases), the wheat germ ACP was partially characterized as a PTPase. This study suggests that the inhibitory ability of different vanadium derivatives to modulate ACP activity seems to depend on the geometry around the vanadium atom more than on the oxidation state. Our results indicate a correlation between the PTPase activity and the sensitivity to vanadate and vanadyl cation.
description The direct effect of different vanadium compounds on acid phosphatase (ACP) activity was investigated. Vanadate and vanadyl but not pervanadate inhibited the wheat germ ACP activity. These vanadium derivatives did not alter the fibroblast Swiss 3T3 soluble fraction ACP activity. Using inhibitors of tyrosine phosphatases (PTPases), the wheat germ ACP was partially characterized as a PTPase. This study suggests that the inhibitory ability of different vanadium derivatives to modulate ACP activity seems to depend on the geometry around the vanadium atom more than on the oxidation state. Our results indicate a correlation between the PTPase activity and the sensitivity to vanadate and vanadyl cation.
publishDate 1996
dc.date.none.fl_str_mv 1996
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv https://digital.cic.gba.gob.ar/handle/11746/4413
url https://digital.cic.gba.gob.ar/handle/11746/4413
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/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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score 12.712165

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