Vanadium Compounds
- Autores
- Cortizo, Ana María; Salice C, Viviana; Etcheverry, Susana B.
- Año de publicación
- 1994
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión enviada
- 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.
- Materia
-
Geología
vanadium
alkaline phosphatase
tyrosine-phosphatase
osteoblast cells
bone cells
inhibitory effects - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/4.0/
- Repositorio
.jpg)
- Institución
- Comisión de Investigaciones Científicas de la Provincia de Buenos Aires
- OAI Identificador
- oai:digital.cic.gba.gob.ar:11746/4446
Ver los metadatos del registro completo
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CIC Digital (CICBA) |
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Vanadium CompoundsCortizo, Ana MaríaSalice C, VivianaEtcheverry, Susana B.Geologíavanadiumalkaline phosphatasetyrosine-phosphataseosteoblast cellsbone cellsinhibitory effectsThe 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.1994info: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/11746/4446enginfo: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:CICBA2025-09-29T13:39:59Zoai:digital.cic.gba.gob.ar:11746/4446Institucionalhttp://digital.cic.gba.gob.arOrganismo científico-tecnológicoNo correspondehttp://digital.cic.gba.gob.ar/oai/snrdmarisa.degiusti@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:94412025-09-29 13:40:00.037CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Airesfalse |
| dc.title.none.fl_str_mv |
Vanadium Compounds |
| title |
Vanadium Compounds |
| spellingShingle |
Vanadium Compounds Cortizo, Ana María Geología vanadium alkaline phosphatase tyrosine-phosphatase osteoblast cells bone cells inhibitory effects |
| title_short |
Vanadium Compounds |
| title_full |
Vanadium Compounds |
| title_fullStr |
Vanadium Compounds |
| title_full_unstemmed |
Vanadium Compounds |
| title_sort |
Vanadium Compounds |
| dc.creator.none.fl_str_mv |
Cortizo, Ana María Salice C, Viviana Etcheverry, Susana B. |
| author |
Cortizo, Ana María |
| author_facet |
Cortizo, Ana María Salice C, Viviana Etcheverry, Susana B. |
| author_role |
author |
| author2 |
Salice C, Viviana Etcheverry, Susana B. |
| author2_role |
author author |
| dc.subject.none.fl_str_mv |
Geología vanadium alkaline phosphatase tyrosine-phosphatase osteoblast cells bone cells inhibitory effects |
| topic |
Geología vanadium alkaline phosphatase tyrosine-phosphatase osteoblast cells bone cells inhibitory effects |
| 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. |
| 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/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/11746/4446 |
| url |
https://digital.cic.gba.gob.ar/handle/11746/4446 |
| 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 |
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reponame:CIC Digital (CICBA) instname:Comisión de Investigaciones Científicas de la Provincia de Buenos Aires instacron:CICBA |
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CIC Digital (CICBA) |
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CIC Digital (CICBA) |
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Comisión de Investigaciones Científicas de la Provincia de Buenos Aires |
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CICBA |
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CICBA |
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CIC Digital (CICBA) - Comisión de Investigaciones Científicas de la Provincia de Buenos Aires |
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marisa.degiusti@sedici.unlp.edu.ar |
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13.070432 |