Studies on induction of δ-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. Chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats
The present work demonstrates that phenformin exerted an inducing effect on δ-amino-levulinic acid synthase (ALA-S) and ferrochelatase activities and on cytochrome P-450 content in isolated hepatocytes from rats with experimental diabetes. Similar results were obtained with respect to ALA-S activity...
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todo:paper_00062952_v40_n2_p365_Canepa2023-10-03T14:04:16Z Studies on induction of δ-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. Chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats Canepa, E.T. Llambias, E.B.C. Grinstein, M. 5 aminolevulinate synthase allylisopropylacetamide bucladesine chlorpropamide cyclic amp cytochrome p450 ferrochelatase lead acetate phenformin phenobarbital animal cell animal experiment animal model article cell suspension drug concentration enzyme induction hepatic porphyria liver cell male nonhuman priority journal rat streptozocin diabetes 5-Aminolevulinate Synthetase Allylisopropylacetamide Animal Bucladesine Chlorpropamide Cyclic AMP Cytochrome P-450 Enzyme System Diabetes Mellitus, Experimental Enzyme Induction Ferrochelatase In Vitro Lead Liver Lyases Male Phenformin Rats Support, Non-U.S. Gov't The present work demonstrates that phenformin exerted an inducing effect on δ-amino-levulinic acid synthase (ALA-S) and ferrochelatase activities and on cytochrome P-450 content in isolated hepatocytes from rats with experimental diabetes. Similar results were obtained with respect to ALA-S activity and cytochrome P-450 content when chlorpropamide was used. The inducing effect exerted by allylisopropylacetamide (AIA) on ALA-S and ferrochelatase activities in diabetic hepatic cells was markedly greater than that observed in normal hepatocytes. This stimulatory response was not enhanced by adding dibutyryl cyclic AMP (cAMP). When phenformin was added to isolated rat hepatocytes of normal rats, induction of ALA-S and ferrochelatase activities and cytochrome P-450 content was observed only in the presence of added dibutyryl cAMP. Addition of chlorpropamide to this in vitro system did not exert an inducing effect on the same enzymes even in the presence of dibutyryl cAMP. The present results add more experimental evidence about the lability of the heme pathway of diabetic hepatocytes. © 1990. Fil:Canepa, E.T. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Llambias, E.B.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Grinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00062952_v40_n2_p365_Canepa |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
5 aminolevulinate synthase allylisopropylacetamide bucladesine chlorpropamide cyclic amp cytochrome p450 ferrochelatase lead acetate phenformin phenobarbital animal cell animal experiment animal model article cell suspension drug concentration enzyme induction hepatic porphyria liver cell male nonhuman priority journal rat streptozocin diabetes 5-Aminolevulinate Synthetase Allylisopropylacetamide Animal Bucladesine Chlorpropamide Cyclic AMP Cytochrome P-450 Enzyme System Diabetes Mellitus, Experimental Enzyme Induction Ferrochelatase In Vitro Lead Liver Lyases Male Phenformin Rats Support, Non-U.S. Gov't |
spellingShingle |
5 aminolevulinate synthase allylisopropylacetamide bucladesine chlorpropamide cyclic amp cytochrome p450 ferrochelatase lead acetate phenformin phenobarbital animal cell animal experiment animal model article cell suspension drug concentration enzyme induction hepatic porphyria liver cell male nonhuman priority journal rat streptozocin diabetes 5-Aminolevulinate Synthetase Allylisopropylacetamide Animal Bucladesine Chlorpropamide Cyclic AMP Cytochrome P-450 Enzyme System Diabetes Mellitus, Experimental Enzyme Induction Ferrochelatase In Vitro Lead Liver Lyases Male Phenformin Rats Support, Non-U.S. Gov't Canepa, E.T. Llambias, E.B.C. Grinstein, M. Studies on induction of δ-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. Chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats |
topic_facet |
5 aminolevulinate synthase allylisopropylacetamide bucladesine chlorpropamide cyclic amp cytochrome p450 ferrochelatase lead acetate phenformin phenobarbital animal cell animal experiment animal model article cell suspension drug concentration enzyme induction hepatic porphyria liver cell male nonhuman priority journal rat streptozocin diabetes 5-Aminolevulinate Synthetase Allylisopropylacetamide Animal Bucladesine Chlorpropamide Cyclic AMP Cytochrome P-450 Enzyme System Diabetes Mellitus, Experimental Enzyme Induction Ferrochelatase In Vitro Lead Liver Lyases Male Phenformin Rats Support, Non-U.S. Gov't |
description |
The present work demonstrates that phenformin exerted an inducing effect on δ-amino-levulinic acid synthase (ALA-S) and ferrochelatase activities and on cytochrome P-450 content in isolated hepatocytes from rats with experimental diabetes. Similar results were obtained with respect to ALA-S activity and cytochrome P-450 content when chlorpropamide was used. The inducing effect exerted by allylisopropylacetamide (AIA) on ALA-S and ferrochelatase activities in diabetic hepatic cells was markedly greater than that observed in normal hepatocytes. This stimulatory response was not enhanced by adding dibutyryl cyclic AMP (cAMP). When phenformin was added to isolated rat hepatocytes of normal rats, induction of ALA-S and ferrochelatase activities and cytochrome P-450 content was observed only in the presence of added dibutyryl cAMP. Addition of chlorpropamide to this in vitro system did not exert an inducing effect on the same enzymes even in the presence of dibutyryl cAMP. The present results add more experimental evidence about the lability of the heme pathway of diabetic hepatocytes. © 1990. |
format |
JOUR |
author |
Canepa, E.T. Llambias, E.B.C. Grinstein, M. |
author_facet |
Canepa, E.T. Llambias, E.B.C. Grinstein, M. |
author_sort |
Canepa, E.T. |
title |
Studies on induction of δ-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. Chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats |
title_short |
Studies on induction of δ-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. Chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats |
title_full |
Studies on induction of δ-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. Chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats |
title_fullStr |
Studies on induction of δ-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. Chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats |
title_full_unstemmed |
Studies on induction of δ-aminolevulinic acid synthase, ferrochelatase, cytochrome P-450 and cyclic AMP by phenformin. Chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats |
title_sort |
studies on induction of δ-aminolevulinic acid synthase, ferrochelatase, cytochrome p-450 and cyclic amp by phenformin. chlorpropamide, allylisopropylacetamide and lead in hepatocytes from normal and experimental diabetic rats |
url |
http://hdl.handle.net/20.500.12110/paper_00062952_v40_n2_p365_Canepa |
work_keys_str_mv |
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1782025865912123392 |