Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and...
- Autores
- Navone, N.M.; Polo, C.F.; Dinger, R.M.; Del C. Batlle, A.M.
- Año de publicación
- 1990
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 1. 1. Basal levels and allyl-isopropylacetamide (AIA) or veronal induced levels of δ-aminolevulinate synthetase (ALA-S), cytochrome P-450 (cyt P-450) and cytochrome oxidase were determined in tumor (T) and liver of both normal mice (NM) and T bearing mice (TBM). 2. 2. Basal levels of ALA-S were nearly the same in either source. The amount of cyt P-450 was lower in TBM liver than in NM liver, and no detectable in T. While the basal activity of cytochrome oxidase in TBM liver and T were higher than those of NM liver. 3. 3. In AIA intoxicated animals there was a lower induction of ALA-S in liver of TBM than in NM liver. There was no induction in T ALA-S. The loss of cyt P-450 was less in TBM liver when compared with NM liver. 4. 4. The induction level of cyt P-450 after veronal administration was nearly the same in liver of both TBM and NM. 5. 5. We conclude that lower induction of liver ALA-S activity in TBM liver is due to correspondingly lower drug metabolism ability of TBM liver. Otherwise our results suggest that the control mechanism operating in T and probably in its original tissue are different from those described for normal liver. © 1990.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. - Fuente
- Int. J. Biochem. 1990;22(9):1005-1008
- Materia
-
5 aminolevulinate synthase
allylisopropylacetamide
barbital
cytochrome c oxidase
cytochrome p450
animal cell
article
breast cancer
liver
mouse
nonhuman
5-Aminolevulinate Synthetase
Allylisopropylacetamide
Animal
Barbital
Cytochrome P-450 Enzyme System
Cytochrome-c Oxidase
Enzyme Induction
Heme
Liver
Male
Mammary Neoplasms, Experimental
Mice
Mice, Inbred BALB C
Support, Non-U.S. Gov't
Animalia - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by/2.5/ar
- Repositorio
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_0020711X_v22_n9_p1005_Navone
Ver los metadatos del registro completo
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Biblioteca Digital (UBA-FCEN) |
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Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidaseNavone, N.M.Polo, C.F.Dinger, R.M.Del C. Batlle, A.M.5 aminolevulinate synthaseallylisopropylacetamidebarbitalcytochrome c oxidasecytochrome p450animal cellarticlebreast cancerlivermousenonhuman5-Aminolevulinate SynthetaseAllylisopropylacetamideAnimalBarbitalCytochrome P-450 Enzyme SystemCytochrome-c OxidaseEnzyme InductionHemeLiverMaleMammary Neoplasms, ExperimentalMiceMice, Inbred BALB CSupport, Non-U.S. Gov'tAnimalia1. 1. Basal levels and allyl-isopropylacetamide (AIA) or veronal induced levels of δ-aminolevulinate synthetase (ALA-S), cytochrome P-450 (cyt P-450) and cytochrome oxidase were determined in tumor (T) and liver of both normal mice (NM) and T bearing mice (TBM). 2. 2. Basal levels of ALA-S were nearly the same in either source. The amount of cyt P-450 was lower in TBM liver than in NM liver, and no detectable in T. While the basal activity of cytochrome oxidase in TBM liver and T were higher than those of NM liver. 3. 3. In AIA intoxicated animals there was a lower induction of ALA-S in liver of TBM than in NM liver. There was no induction in T ALA-S. The loss of cyt P-450 was less in TBM liver when compared with NM liver. 4. 4. The induction level of cyt P-450 after veronal administration was nearly the same in liver of both TBM and NM. 5. 5. We conclude that lower induction of liver ALA-S activity in TBM liver is due to correspondingly lower drug metabolism ability of TBM liver. Otherwise our results suggest that the control mechanism operating in T and probably in its original tissue are different from those described for normal liver. © 1990.Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1990info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_0020711X_v22_n9_p1005_NavoneInt. J. Biochem. 1990;22(9):1005-1008reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:42:54Zpaperaa:paper_0020711X_v22_n9_p1005_NavoneInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:42:55.72Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse |
dc.title.none.fl_str_mv |
Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase |
title |
Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase |
spellingShingle |
Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase Navone, N.M. 5 aminolevulinate synthase allylisopropylacetamide barbital cytochrome c oxidase cytochrome p450 animal cell article breast cancer liver mouse nonhuman 5-Aminolevulinate Synthetase Allylisopropylacetamide Animal Barbital Cytochrome P-450 Enzyme System Cytochrome-c Oxidase Enzyme Induction Heme Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Support, Non-U.S. Gov't Animalia |
title_short |
Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase |
title_full |
Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase |
title_fullStr |
Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase |
title_full_unstemmed |
Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase |
title_sort |
Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice-I. Effect of allyl-isopropylacetamide and veronal on δ -aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase |
dc.creator.none.fl_str_mv |
Navone, N.M. Polo, C.F. Dinger, R.M. Del C. Batlle, A.M. |
author |
Navone, N.M. |
author_facet |
Navone, N.M. Polo, C.F. Dinger, R.M. Del C. Batlle, A.M. |
author_role |
author |
author2 |
Polo, C.F. Dinger, R.M. Del C. Batlle, A.M. |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
5 aminolevulinate synthase allylisopropylacetamide barbital cytochrome c oxidase cytochrome p450 animal cell article breast cancer liver mouse nonhuman 5-Aminolevulinate Synthetase Allylisopropylacetamide Animal Barbital Cytochrome P-450 Enzyme System Cytochrome-c Oxidase Enzyme Induction Heme Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Support, Non-U.S. Gov't Animalia |
topic |
5 aminolevulinate synthase allylisopropylacetamide barbital cytochrome c oxidase cytochrome p450 animal cell article breast cancer liver mouse nonhuman 5-Aminolevulinate Synthetase Allylisopropylacetamide Animal Barbital Cytochrome P-450 Enzyme System Cytochrome-c Oxidase Enzyme Induction Heme Liver Male Mammary Neoplasms, Experimental Mice Mice, Inbred BALB C Support, Non-U.S. Gov't Animalia |
dc.description.none.fl_txt_mv |
1. 1. Basal levels and allyl-isopropylacetamide (AIA) or veronal induced levels of δ-aminolevulinate synthetase (ALA-S), cytochrome P-450 (cyt P-450) and cytochrome oxidase were determined in tumor (T) and liver of both normal mice (NM) and T bearing mice (TBM). 2. 2. Basal levels of ALA-S were nearly the same in either source. The amount of cyt P-450 was lower in TBM liver than in NM liver, and no detectable in T. While the basal activity of cytochrome oxidase in TBM liver and T were higher than those of NM liver. 3. 3. In AIA intoxicated animals there was a lower induction of ALA-S in liver of TBM than in NM liver. There was no induction in T ALA-S. The loss of cyt P-450 was less in TBM liver when compared with NM liver. 4. 4. The induction level of cyt P-450 after veronal administration was nearly the same in liver of both TBM and NM. 5. 5. We conclude that lower induction of liver ALA-S activity in TBM liver is due to correspondingly lower drug metabolism ability of TBM liver. Otherwise our results suggest that the control mechanism operating in T and probably in its original tissue are different from those described for normal liver. © 1990. Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. |
description |
1. 1. Basal levels and allyl-isopropylacetamide (AIA) or veronal induced levels of δ-aminolevulinate synthetase (ALA-S), cytochrome P-450 (cyt P-450) and cytochrome oxidase were determined in tumor (T) and liver of both normal mice (NM) and T bearing mice (TBM). 2. 2. Basal levels of ALA-S were nearly the same in either source. The amount of cyt P-450 was lower in TBM liver than in NM liver, and no detectable in T. While the basal activity of cytochrome oxidase in TBM liver and T were higher than those of NM liver. 3. 3. In AIA intoxicated animals there was a lower induction of ALA-S in liver of TBM than in NM liver. There was no induction in T ALA-S. The loss of cyt P-450 was less in TBM liver when compared with NM liver. 4. 4. The induction level of cyt P-450 after veronal administration was nearly the same in liver of both TBM and NM. 5. 5. We conclude that lower induction of liver ALA-S activity in TBM liver is due to correspondingly lower drug metabolism ability of TBM liver. Otherwise our results suggest that the control mechanism operating in T and probably in its original tissue are different from those described for normal liver. © 1990. |
publishDate |
1990 |
dc.date.none.fl_str_mv |
1990 |
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 |
http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n9_p1005_Navone |
url |
http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n9_p1005_Navone |
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/2.5/ar |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by/2.5/ar |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
Int. J. Biochem. 1990;22(9):1005-1008 reponame:Biblioteca Digital (UBA-FCEN) instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales instacron:UBA-FCEN |
reponame_str |
Biblioteca Digital (UBA-FCEN) |
collection |
Biblioteca Digital (UBA-FCEN) |
instname_str |
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
instacron_str |
UBA-FCEN |
institution |
UBA-FCEN |
repository.name.fl_str_mv |
Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales |
repository.mail.fl_str_mv |
ana@bl.fcen.uba.ar |
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1844618734569783296 |
score |
13.070432 |