Drug metabolizing enzyme system and heme pathway in hepatocarcinogenesis
Chemically induced and spontaneous liver tumors share some metabolic alterations. The decline in hemoprotein levels during hepatocarcinogenesis may result from a diminution of the intracellular heme pool. To elucidate if the onset of the pre-initiation stage alters the natural regulation mechanism o...
Guardado en:
| Autores principales: | , , |
|---|---|
| Publicado: |
1999
|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03057232_v17_n1-2_p25_Vazquez http://hdl.handle.net/20.500.12110/paper_03057232_v17_n1-2_p25_Vazquez |
| Aporte de: |
| id |
paper:paper_03057232_v17_n1-2_p25_Vazquez |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_03057232_v17_n1-2_p25_Vazquez2023-06-08T15:30:49Z Drug metabolizing enzyme system and heme pathway in hepatocarcinogenesis Vázquez, Elba Susana Gerez, Esther Noemí Batlle, Alcira María del Carmen δ-Aminolevulinic acid synthase 2-allylisopropyl-acetamide Cytochrome P-450 Gluthatione S-transferase Hepatocarcinogenesis Microsomal heme oxygenase 4 dimethylaminoazobenzene 5 aminolevulinate synthase allylisopropylacetamide beta glucuronidase carcinogen cytochrome P450 enzyme inhibitor glutathione transferase heme heme oxygenase hemoprotein prodrug sulfatase tryptophan 2,3 dioxygenase animal article biological model biotransformation cell transformation chemically induced disorder comparative study drug antagonism drug effect drug resistance enzyme induction enzymology liver microsome liver tumor male metabolism mouse oxidation reduction reaction physiology precancer 5-Aminolevulinate Synthetase Allylisopropylacetamide Animals Biotransformation Carcinogens Cell Transformation, Neoplastic Cytochrome P-450 Enzyme System Drug Resistance Enzyme Induction Enzyme Inhibitors Glucuronidase Glutathione Transferase Heme Heme Oxygenase (Decyclizing) Hemeproteins Liver Neoplasms, Experimental Male Mice Microsomes, Liver Models, Biological Oxidation-Reduction p-Dimethylaminoazobenzene Precancerous Conditions Prodrugs Sulfatases Tryptophan Oxygenase Chemically induced and spontaneous liver tumors share some metabolic alterations. The decline in hemoprotein levels during hepatocarcinogenesis may result from a diminution of the intracellular heme pool. To elucidate if the onset of the pre-initiation stage alters the natural regulation mechanism of heme pathway, animals were fed with p-dimethylaminoazobenzene (DAB) and treated or not with 2-allylisopropylacetamide (AIA). The induction of 6-Aminolevulinic acid synthase (ALA-S) activity and the diminution in microsomal heme oxygenase (MHO) did not change when DAB fed animals were treated with AIA. Cytochrome P-450 (P-450) levels and glutathione S-transferase activity were increased in all the groups tested. Tryptophan pyrrolase, sulphatase and β-glucuronidase activities were altered in DAB fed animals but AIA treatment did not produce any effect. Changes in drug metabolizing enzymes in livers of DAB fed animals could be the result of a primary deregulation of heme metabolism. These results give additional support to our hypothesis about a mechanism for the onset of hepatocarcinogenesis. Fil:Vazquez, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gerez, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Batlle, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1999 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03057232_v17_n1-2_p25_Vazquez http://hdl.handle.net/20.500.12110/paper_03057232_v17_n1-2_p25_Vazquez |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
δ-Aminolevulinic acid synthase 2-allylisopropyl-acetamide Cytochrome P-450 Gluthatione S-transferase Hepatocarcinogenesis Microsomal heme oxygenase 4 dimethylaminoazobenzene 5 aminolevulinate synthase allylisopropylacetamide beta glucuronidase carcinogen cytochrome P450 enzyme inhibitor glutathione transferase heme heme oxygenase hemoprotein prodrug sulfatase tryptophan 2,3 dioxygenase animal article biological model biotransformation cell transformation chemically induced disorder comparative study drug antagonism drug effect drug resistance enzyme induction enzymology liver microsome liver tumor male metabolism mouse oxidation reduction reaction physiology precancer 5-Aminolevulinate Synthetase Allylisopropylacetamide Animals Biotransformation Carcinogens Cell Transformation, Neoplastic Cytochrome P-450 Enzyme System Drug Resistance Enzyme Induction Enzyme Inhibitors Glucuronidase Glutathione Transferase Heme Heme Oxygenase (Decyclizing) Hemeproteins Liver Neoplasms, Experimental Male Mice Microsomes, Liver Models, Biological Oxidation-Reduction p-Dimethylaminoazobenzene Precancerous Conditions Prodrugs Sulfatases Tryptophan Oxygenase |
| spellingShingle |
δ-Aminolevulinic acid synthase 2-allylisopropyl-acetamide Cytochrome P-450 Gluthatione S-transferase Hepatocarcinogenesis Microsomal heme oxygenase 4 dimethylaminoazobenzene 5 aminolevulinate synthase allylisopropylacetamide beta glucuronidase carcinogen cytochrome P450 enzyme inhibitor glutathione transferase heme heme oxygenase hemoprotein prodrug sulfatase tryptophan 2,3 dioxygenase animal article biological model biotransformation cell transformation chemically induced disorder comparative study drug antagonism drug effect drug resistance enzyme induction enzymology liver microsome liver tumor male metabolism mouse oxidation reduction reaction physiology precancer 5-Aminolevulinate Synthetase Allylisopropylacetamide Animals Biotransformation Carcinogens Cell Transformation, Neoplastic Cytochrome P-450 Enzyme System Drug Resistance Enzyme Induction Enzyme Inhibitors Glucuronidase Glutathione Transferase Heme Heme Oxygenase (Decyclizing) Hemeproteins Liver Neoplasms, Experimental Male Mice Microsomes, Liver Models, Biological Oxidation-Reduction p-Dimethylaminoazobenzene Precancerous Conditions Prodrugs Sulfatases Tryptophan Oxygenase Vázquez, Elba Susana Gerez, Esther Noemí Batlle, Alcira María del Carmen Drug metabolizing enzyme system and heme pathway in hepatocarcinogenesis |
| topic_facet |
δ-Aminolevulinic acid synthase 2-allylisopropyl-acetamide Cytochrome P-450 Gluthatione S-transferase Hepatocarcinogenesis Microsomal heme oxygenase 4 dimethylaminoazobenzene 5 aminolevulinate synthase allylisopropylacetamide beta glucuronidase carcinogen cytochrome P450 enzyme inhibitor glutathione transferase heme heme oxygenase hemoprotein prodrug sulfatase tryptophan 2,3 dioxygenase animal article biological model biotransformation cell transformation chemically induced disorder comparative study drug antagonism drug effect drug resistance enzyme induction enzymology liver microsome liver tumor male metabolism mouse oxidation reduction reaction physiology precancer 5-Aminolevulinate Synthetase Allylisopropylacetamide Animals Biotransformation Carcinogens Cell Transformation, Neoplastic Cytochrome P-450 Enzyme System Drug Resistance Enzyme Induction Enzyme Inhibitors Glucuronidase Glutathione Transferase Heme Heme Oxygenase (Decyclizing) Hemeproteins Liver Neoplasms, Experimental Male Mice Microsomes, Liver Models, Biological Oxidation-Reduction p-Dimethylaminoazobenzene Precancerous Conditions Prodrugs Sulfatases Tryptophan Oxygenase |
| description |
Chemically induced and spontaneous liver tumors share some metabolic alterations. The decline in hemoprotein levels during hepatocarcinogenesis may result from a diminution of the intracellular heme pool. To elucidate if the onset of the pre-initiation stage alters the natural regulation mechanism of heme pathway, animals were fed with p-dimethylaminoazobenzene (DAB) and treated or not with 2-allylisopropylacetamide (AIA). The induction of 6-Aminolevulinic acid synthase (ALA-S) activity and the diminution in microsomal heme oxygenase (MHO) did not change when DAB fed animals were treated with AIA. Cytochrome P-450 (P-450) levels and glutathione S-transferase activity were increased in all the groups tested. Tryptophan pyrrolase, sulphatase and β-glucuronidase activities were altered in DAB fed animals but AIA treatment did not produce any effect. Changes in drug metabolizing enzymes in livers of DAB fed animals could be the result of a primary deregulation of heme metabolism. These results give additional support to our hypothesis about a mechanism for the onset of hepatocarcinogenesis. |
| author |
Vázquez, Elba Susana Gerez, Esther Noemí Batlle, Alcira María del Carmen |
| author_facet |
Vázquez, Elba Susana Gerez, Esther Noemí Batlle, Alcira María del Carmen |
| author_sort |
Vázquez, Elba Susana |
| title |
Drug metabolizing enzyme system and heme pathway in hepatocarcinogenesis |
| title_short |
Drug metabolizing enzyme system and heme pathway in hepatocarcinogenesis |
| title_full |
Drug metabolizing enzyme system and heme pathway in hepatocarcinogenesis |
| title_fullStr |
Drug metabolizing enzyme system and heme pathway in hepatocarcinogenesis |
| title_full_unstemmed |
Drug metabolizing enzyme system and heme pathway in hepatocarcinogenesis |
| title_sort |
drug metabolizing enzyme system and heme pathway in hepatocarcinogenesis |
| publishDate |
1999 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03057232_v17_n1-2_p25_Vazquez http://hdl.handle.net/20.500.12110/paper_03057232_v17_n1-2_p25_Vazquez |
| work_keys_str_mv |
AT vazquezelbasusana drugmetabolizingenzymesystemandhemepathwayinhepatocarcinogenesis AT gerezesthernoemi drugmetabolizingenzymesystemandhemepathwayinhepatocarcinogenesis AT batllealciramariadelcarmen drugmetabolizingenzymesystemandhemepathwayinhepatocarcinogenesis |
| _version_ |
1768543994016432128 |