The involvement of cytochrome P450 system in the fate of 2,4,6-trinitrotoluene (TNT) in European eel [Anguilla anguilla (Linnaeus, 1758)]

2006 ◽  
Vol 34 (6) ◽  
pp. 1228-1230 ◽  
Author(s):  
C. Della Torre ◽  
I. Corsi ◽  
L. Alcaro ◽  
E. Amato ◽  
S. Focardi
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome C ◽  
Phase Ii ◽  
Reductase Activity ◽  
Anguilla Anguilla ◽  
European Eel ◽  
Cytochrome P450 System ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nadph Cytochrome C Reductase

TNT (2,4,6-trinitrotoluene) was the most common nitro aromatic explosive available in World War II ammunitions. The presence of ordnance dumped at sea might represent a great concern for marine species living close to dumping sites and the toxicological properties of the chemicals released into the marine environments need to be evaluated. The aim of the present study is to investigate the involvement of CYP (cytochrome P450) system in the metabolism of TNT in marine organisms by using the European eel [Anguilla anguilla (Linnaeus, 1758)] as model species. In vivo exposure to sublethal concentration of TNT (0.5, 1 and 2.5 mg/l) leads to a significant decrease in the phase I CYP1A catalytic activities such as EROD (7-ethoxyresorufin-O-de-ethylase) and MROD (7-methoxyresorufin-O-de-ethylase). On the opposite, a significant increase in NADPH cytochrome c reductase activity as well as phase II UDP-glucuronosyltransferase activity is observed. An inhibition at enzyme level is hypothesized for both CYP1A enzymes, also confirmed by a similar decrease observed after in vitro exposure. An active role of NADPH cytochrome c reductase and phase II enzymes in the TNT metabolism may also be hypothesized.

scholarly journals Étude de l’effet du cadmium et du benzo[a]pyrène sur des enzymes de phase I et phase II de biotransformation chez le polychète Nereisdiversicolor

2009 ◽  
Vol 22 (3) ◽  
pp. 451-459
Author(s):  
Zied Bouraoui ◽  
Jihene Ghedira ◽  
Jamel Jebali ◽  
Mohamed Banni ◽  
Cristelle Clerendeau ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Phase I ◽  
Phase Ii ◽  
Nereis Diversicolor ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nadph Cytochrome C Reductase

Résumé Le présent travail reporte l’effet du cadmium (Cd), du benzo[a]pyrène (B[a]P) ainsi que leur mélange (Cd/B[a]P), à 1 µM, sur les activités d’enzymes impliqués dans la phase I et la phase II de biotransformation chez le polychète Nereis diversicolor en fonction du temps (après 12, 24, 36 et 48 h). L’effet d’une contamination aiguë par du cadmium à une dose de 1 µM après 12, 24 et 36 h montre une inhibition de l’activité NADPH cytochrome C réductase chez les individus contaminés comparés à leurs témoins relatifs, alors que le seul effet du cadmium sur l’activité glutathion-S-transférase n’est enregistré qu’après 36 h d’exposition. Quant au benzo[a]pyrène, les résultats montrent une augmentation significative de l’activité NADPH cytochrome C réductase après 12, 24 et 36 h d’exposition, alors que pour l’activité glutathion-S‑transférase, la variation significative entre les animaux témoins et traités n’est enregistrée qu’à 36 h d’exposition. Le mélange (Cd/B[a]P) inhibe l’activité NADPH cytochrome C réductase chez les individus traités par comparaison aux témoins relatifs et montre un effet inducteur sur l’activité GST sauf après 36 h d’exposition. Ces résultats montrent ainsi les interactions entre les polluants ainsi que leurs effets sur les organismes.

Temperature Influence on Basal Activity and Induction of Mixed Function Oxygenase Activity in Fundulus heteroclitus

1979 ◽  
Vol 36 (11) ◽  
pp. 1400-1405 ◽  
Author(s):  
John J. Stegeman
Keyword(s):  
Cytochrome C ◽  
Fundulus Heteroclitus ◽  
Reductase Activity ◽  
Control Fish ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Pyrene Hydroxylase ◽  
Mixed Function Oxygenase ◽  
Cytochrome P 450 ◽  
Nadph Cytochrome C Reductase

Treatment of Fundulus heteroclitus acclimated to 6.5 °C with benzo(a)pyrene did not elicit any change in the levels of hepatic microsomal NADH- or NADPH-cytochrome c reductase activity, nor in the levels of cytochrome P-450 or its catalytic activities. However, the same treatment offish at 16 5 °C resulted in a marked induction of benzo(a)pyrene hydroxylase and NADPH-cytochrome c reductase. Cytochrome P-450 content was also higher in the warm, treated fish and the Soret maximum of reduced, CO-treated microsomes was shifted to the violet. Levels of aminopyrine demethylase and NADH-cytochrome c reductase activities did not show a significant treatment effect. At neither temperature could treated and control fish be distinguished on the basis of in vitro inhibition of benzo(a)pyrene hydroxylase activity by 7,8-benzoflavone. Levels of NADPH-cytochrome c reductase and benzo(a)pyrene hydroxylase activities were greater in control Fundulus acclimated to 6.5 °C than to 16.5 °C, when normalized to microsomal protein, but not when based on body weight. The results indicate that habitat temperature alone may not affect the capacity for initial hydrocarbon metabolism in fish, but that it can strongly influence the induction of cytochrome P-450. Key words: temperature, cytochrome P-450, hydrocarbon metabolism, mixed-function oxygenase, Fundulus heteroclitus

A chimeric iron-sulfur flavoprotein endowed with NADPH-cytochrome c reductase activity

1996 ◽  
Vol 24 (1) ◽  
pp. 22S-22S ◽  
Author(s):  
Giuliana Zanetti ◽  
Luciano Piubelli ◽  
Roberta Zucca Tanci ◽  
Alessandro Aliverti
Keyword(s):  
Cytochrome C ◽  
Reductase Activity ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Iron Sulfur ◽  
Nadph Cytochrome C Reductase

scholarly journals PRODUCTION OF MEMBRANE WHORLS IN RAT LIVER BY SOME INHIBITORS OF PROTEIN SYNTHESIS

1974 ◽  
Vol 62 (1) ◽  
pp. 20-31 ◽  
Author(s):  
Kou M. Hwang ◽  
Linda C. Yang ◽  
Christine K. Carrico ◽  
Rose A. Schulz ◽  
John B. Schenkman ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Synthesis ◽  
Cytochrome C ◽  
Peptide Synthesis ◽  
Reductase Activity ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Nascent Peptide ◽  
Membrane Bound ◽  
Nadph Cytochrome C Reductase

Inhibitors of protein synthesis capable of differential effects on nascent peptide synthesis on membrane-bound and free polyribosomes were employed to investigate the structure and function of cellular membranes of liver. The formation of membranous whorls in the cytoplasm and distension of nuclear membranes were induced by inhibitors of protein synthesis (i.e., cycloheximide and emetine) which predominantly interfere with nascent peptide synthesis on membrane-bound polyribosomes in situ. Other inhibitors of protein synthesis such as puromycin and fusidic acid, which inhibit nascent peptide synthesis on both free and membrane-bound polyribosomes, and chloramphenicol, which inhibits mitochondrial protein synthesis, did not induce these alterations. Cycloheximide, puromycin, and chloramphenicol produce some common cellular lesions as reflected by similar alterations in morphology, such as swelling of mitochondria, degranulation of rough endoplasmic reticulum, and aggregation of free ribosomes. The process of whorl formation in the cytoplasm, the incorporation of [3H]leucine and of [3H]choline into endoplasmic reticulum and the total NADPH-cytochrome c reductase activity of the endoplasmic reticulum were determined. During maximum formation of membranous whorls, [3H]leucine incorporation into cytoplasmic membranes was inhibited, while [3H]choline incorporation into these structures was increased; maximum inhibition of protein synthesis and stimulation of choline incorporation into endoplasmic reticulum, however, preceded whorl formation. Cycloheximide decreased the activity of NADPH-cytochrome c reductase of rough endoplasmic reticulum, but increased NADPH-cytochrome c reductase activity of smooth endoplasmic reticulum. In addition, cycloheximide decreased the content of hemoprotein in both the microsomal and mitochondrial fractions of rat liver, and the activities of mixed function oxidase and of oxidative phosphorylation were impaired to different degrees. Succinate-stimulated microsomal oxidation was also inhibited. The possible mechanisms involved in the formation of membranous whorls, as well as their functions, are discussed.

scholarly journals Role of mixed-function amine oxidase in N-hydroxylation of 2-acetamidofluorene by hamster liver microsomal preparations

1973 ◽  
Vol 136 (4) ◽  
pp. 1137-1140 ◽  
Author(s):  
Prabhakar D. Lotlikar ◽  
Kathleen Wertman ◽  
Leida Luha
Keyword(s):  
Cytochrome C ◽  
Amine Oxidase ◽  
Reductase Activity ◽  
Comparative Data ◽  
Oxide Formation ◽  
Cytochrome C Reductase ◽  
Nadph Cytochrome ◽  
Cytochrome P 450 ◽  
Nadph Cytochrome C Reductase

Pretreatment of hamsters with 3-methylcholanthrene (100mg/kg body wt.) 24h before death did not appreciably change the extent of N-oxide formation when hepatic microsomal preparations were incubated with NN-dimethylaniline as substrate. In contrast, the N-hydroxylation of 2-acetamidofluorene was increased severalfold in hepatic microsomal preparations from pretreated animals. Under these conditions there were no appreciable changes in cytochrome P-450 content and NADPH–cytochrome c reductase activity. On the basis of these comparative data, it is suggested that amine oxidase is not involved in N-hydroxylation of 2-acetamidofluorene.

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