Vanadium Compounds : Their Action on Alkaline Phosphatase Activity

Autores
Cortizo, Ana María; Salice, Viviana C.; Etcheverry, Susana B.
Año de publicación
1994
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The direct effect of different vanadium compounds upon alkaline phosphatase (ALP) activity was investigated~ Vanadate and vanadyl inhibited both the soluble and particulate ALP activity from UMR.106 cells and front bovine intestinal ALP. We have also shown the inhibition of ALP activity in the soluble fraction of osteoblasts by peroxo and hydroperoxo vanadium compounds. ALP activity in the particulate fraction was not inhibited by these species; nor was the bovine intestinal ALP. Using inhibitors of Tyr-phosphatase (PTPases), the soluble ALP was partially characterized as a PTPase. The major activity in the particulate fraction represents the bone-specific ALPactivity. This study demonstrates that different forms of vanadium are direct inhibitors of ALP activity. This effect is dependent on the enzymatic activity investigated and on the origin of the ALP.
Facultad de Ciencias Médicas
Materia
Ciencias Médicas
vanadium, alkaline phosphatase, tyrosine-phosphatase, osteoblast cells, bone cells, inhibitory effects
Vanadio
Fosfatasa Alcalina
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:10915/67403
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/67403
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Vanadium Compounds : Their Action on Alkaline Phosphatase ActivityCortizo, Ana MaríaSalice, Viviana C.Etcheverry, Susana B.Ciencias Médicasvanadium, alkaline phosphatase, tyrosine-phosphatase, osteoblast cells, bone cells, inhibitory effectsVanadioFosfatasa AlcalinaThe direct effect of different vanadium compounds upon alkaline phosphatase (ALP) activity was investigated~ Vanadate and vanadyl inhibited both the soluble and particulate ALP activity from UMR.106 cells and front bovine intestinal ALP. We have also shown the inhibition of ALP activity in the soluble fraction of osteoblasts by peroxo and hydroperoxo vanadium compounds. ALP activity in the particulate fraction was not inhibited by these species; nor was the bovine intestinal ALP. Using inhibitors of Tyr-phosphatase (PTPases), the soluble ALP was partially characterized as a PTPase. The major activity in the particulate fraction represents the bone-specific ALPactivity. This study demonstrates that different forms of vanadium are direct inhibitors of ALP activity. This effect is dependent on the enzymatic activity investigated and on the origin of the ALP.Facultad de Ciencias Médicas1994info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf331-339http://sedici.unlp.edu.ar/handle/10915/67403enginfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2FBF02917433info:eu-repo/semantics/altIdentifier/issn/0163-4984info:eu-repo/semantics/altIdentifier/hdl/11746/4446info: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:UNLP2025-09-03T10:42:18Zoai:sedici.unlp.edu.ar:10915/67403Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:42:18.909SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Vanadium Compounds : Their Action on Alkaline Phosphatase Activity
title Vanadium Compounds : Their Action on Alkaline Phosphatase Activity
spellingShingle Vanadium Compounds : Their Action on Alkaline Phosphatase Activity
Cortizo, Ana María
Ciencias Médicas
vanadium, alkaline phosphatase, tyrosine-phosphatase, osteoblast cells, bone cells, inhibitory effects
Vanadio
Fosfatasa Alcalina
title_short Vanadium Compounds : Their Action on Alkaline Phosphatase Activity
title_full Vanadium Compounds : Their Action on Alkaline Phosphatase Activity
title_fullStr Vanadium Compounds : Their Action on Alkaline Phosphatase Activity
title_full_unstemmed Vanadium Compounds : Their Action on Alkaline Phosphatase Activity
title_sort Vanadium Compounds : Their Action on Alkaline Phosphatase Activity
dc.creator.none.fl_str_mv Cortizo, Ana María
Salice, Viviana C.
Etcheverry, Susana B.
author Cortizo, Ana María
author_facet Cortizo, Ana María
Salice, Viviana C.
Etcheverry, Susana B.
author_role author
author2 Salice, Viviana C.
Etcheverry, Susana B.
author2_role author
author
dc.subject.none.fl_str_mv Ciencias Médicas
vanadium, alkaline phosphatase, tyrosine-phosphatase, osteoblast cells, bone cells, inhibitory effects
Vanadio
Fosfatasa Alcalina
topic Ciencias Médicas
vanadium, alkaline phosphatase, tyrosine-phosphatase, osteoblast cells, bone cells, inhibitory effects
Vanadio
Fosfatasa Alcalina
dc.description.none.fl_txt_mv The direct effect of different vanadium compounds upon alkaline phosphatase (ALP) activity was investigated~ Vanadate and vanadyl inhibited both the soluble and particulate ALP activity from UMR.106 cells and front bovine intestinal ALP. We have also shown the inhibition of ALP activity in the soluble fraction of osteoblasts by peroxo and hydroperoxo vanadium compounds. ALP activity in the particulate fraction was not inhibited by these species; nor was the bovine intestinal ALP. Using inhibitors of Tyr-phosphatase (PTPases), the soluble ALP was partially characterized as a PTPase. The major activity in the particulate fraction represents the bone-specific ALPactivity. This study demonstrates that different forms of vanadium are direct inhibitors of ALP activity. This effect is dependent on the enzymatic activity investigated and on the origin of the ALP.
Facultad de Ciencias Médicas
description The direct effect of different vanadium compounds upon alkaline phosphatase (ALP) activity was investigated~ Vanadate and vanadyl inhibited both the soluble and particulate ALP activity from UMR.106 cells and front bovine intestinal ALP. We have also shown the inhibition of ALP activity in the soluble fraction of osteoblasts by peroxo and hydroperoxo vanadium compounds. ALP activity in the particulate fraction was not inhibited by these species; nor was the bovine intestinal ALP. Using inhibitors of Tyr-phosphatase (PTPases), the soluble ALP was partially characterized as a PTPase. The major activity in the particulate fraction represents the bone-specific ALPactivity. This study demonstrates that different forms of vanadium are direct inhibitors of ALP activity. This effect is dependent on the enzymatic activity investigated and on the origin of the ALP.
publishDate 1994
dc.date.none.fl_str_mv 1994
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/67403
url http://sedici.unlp.edu.ar/handle/10915/67403
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2FBF02917433
info:eu-repo/semantics/altIdentifier/issn/0163-4984
info:eu-repo/semantics/altIdentifier/hdl/11746/4446
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
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)
dc.format.none.fl_str_mv application/pdf
331-339
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.13397

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