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
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_0020711X_v22_n9_p1005_Navone

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oai_identifier_str paperaa:paper_0020711X_v22_n9_p1005_Navone
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling 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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