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

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 near...

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Autores principales: Navone, N.M., Polo, C.F., Dinger, R.M., Del C. Batlle, A.M.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 1990
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n9_p1005_Navone
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spelling paperaa:paper_0020711X_v22_n9_p1005_Navone2023-06-12T16:42:15Z 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 Int. J. Biochem. 1990;22(9):1005-1008 Navone, N.M. Polo, C.F. Dinger, R.M. Del C. Batlle, A.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 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. 1990 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion application/pdf eng info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n9_p1005_Navone
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
language Inglés
orig_language_str_mv eng
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
spellingShingle 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
Navone, N.M.
Polo, C.F.
Dinger, R.M.
Del C. Batlle, A.M.
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
topic_facet 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
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.
format Artículo
Artículo
publishedVersion
author Navone, N.M.
Polo, C.F.
Dinger, R.M.
Del C. Batlle, A.M.
author_facet Navone, N.M.
Polo, C.F.
Dinger, R.M.
Del C. Batlle, A.M.
author_sort Navone, N.M.
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
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
publishDate 1990
url http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n9_p1005_Navone
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