Detection of toxic effects of Cd2+ on different fish species via liver cytochrome P450-dependent monooxygenase activities and FTIR spectroscopy

Mária Henczová, Aranka Kiss Deér, Viktória Komlósi, J. Mink

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The in vivo and in vitro effects of Cd2+ and the CYP1A inductor β-naphthoflavone(β-NF) on the hepatic cytochrome P450 (Cyt 450) monooxygenases were studied in silver carp (Hypophthalmichtys molitrix V.), wels (Silurus glanis L.), and carp (Cyprinus carpio). In vivo treatment of carp with a high dose of Cd2+ (10 mg kg-1, for 3 days) caused a strong inhibition of 7-ethoxyresorufin-O-deethylase (EROD) and a lower inhibition of 7-ethoxycoumarin-O-deethylase (ECOD) activity. The low-dose cadmium treatment (2 mg kg-1 Cd2+, for 6+3 days) resulted in 4-fold increase in EROD and a 3-fold increase in ECOD activity. The combined treatment with Cd2+ and β-NF in both cases led to a loss of EROD inducibility. The silver carp and wels were treated with 10 mg L-1 Cd2+ for 72 h in water. The Cyt P450 content in the wels liver microsomes was increased significantly after treatment for 48 h, whereas there was only a slight, not significant increase in Cyt P450 content in the silver carp microsomes. While the Cd2+ treatment resulted in inhibition of the CYP1A isoenzymes (EROD and ECOD), the APND (aminopyrene-N-demethylase, CYP2B or CYP3A isoenzyme) activity was increased 3- to 4-fold in both fish species. In vitro experiments of the effect of Cd2+ led to a concentration-dependent inhibition in all three investigated fish species. The ECOD isoenzyme of silver carp was the most sensitive to Cd2+. The lowest concentration of Cd2+ resulted in 50% inhibition. The APND isoenzyme was similarly sensitive to Cd2+ in all three investigated fish species. The most sensitive species was the wels, and the least sensitive were the carp isoenzyme. FTIR spectroscopy confirmed that cadmium caused damage to the protein structure. These results support the enzyme activity measurements measured in vivo and in vitro.

Original languageEnglish
Pages (from-to)652-659
Number of pages8
JournalAnalytical and Bioanalytical Chemistry
Volume385
Issue number3
DOIs
Publication statusPublished - Jun 2006

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7-Alkoxycoumarin O-Dealkylase
Carps
Poisons
Fourier Transform Infrared Spectroscopy
Mixed Function Oxygenases
Cytochrome P-450 CYP1A1
Liver
Fish
Cytochrome P-450 Enzyme System
Isoenzymes
Spectrum Analysis
Fishes
Silver
Spectroscopy
Cadmium
N Demethylating Oxidoreductases
Cytochrome P-450 CYP3A
Enzyme activity
Liver Microsomes
Microsomes

Keywords

  • Cd acetate
  • Cytochrome P450
  • Freshwater fish
  • IR spectroscopy
  • Monooxygenases

ASJC Scopus subject areas

  • Analytical Chemistry
  • Clinical Biochemistry

Cite this

Detection of toxic effects of Cd2+ on different fish species via liver cytochrome P450-dependent monooxygenase activities and FTIR spectroscopy. / Henczová, Mária; Deér, Aranka Kiss; Komlósi, Viktória; Mink, J.

In: Analytical and Bioanalytical Chemistry, Vol. 385, No. 3, 06.2006, p. 652-659.

Research output: Contribution to journalArticle

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AU - Mink, J.

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N2 - The in vivo and in vitro effects of Cd2+ and the CYP1A inductor β-naphthoflavone(β-NF) on the hepatic cytochrome P450 (Cyt 450) monooxygenases were studied in silver carp (Hypophthalmichtys molitrix V.), wels (Silurus glanis L.), and carp (Cyprinus carpio). In vivo treatment of carp with a high dose of Cd2+ (10 mg kg-1, for 3 days) caused a strong inhibition of 7-ethoxyresorufin-O-deethylase (EROD) and a lower inhibition of 7-ethoxycoumarin-O-deethylase (ECOD) activity. The low-dose cadmium treatment (2 mg kg-1 Cd2+, for 6+3 days) resulted in 4-fold increase in EROD and a 3-fold increase in ECOD activity. The combined treatment with Cd2+ and β-NF in both cases led to a loss of EROD inducibility. The silver carp and wels were treated with 10 mg L-1 Cd2+ for 72 h in water. The Cyt P450 content in the wels liver microsomes was increased significantly after treatment for 48 h, whereas there was only a slight, not significant increase in Cyt P450 content in the silver carp microsomes. While the Cd2+ treatment resulted in inhibition of the CYP1A isoenzymes (EROD and ECOD), the APND (aminopyrene-N-demethylase, CYP2B or CYP3A isoenzyme) activity was increased 3- to 4-fold in both fish species. In vitro experiments of the effect of Cd2+ led to a concentration-dependent inhibition in all three investigated fish species. The ECOD isoenzyme of silver carp was the most sensitive to Cd2+. The lowest concentration of Cd2+ resulted in 50% inhibition. The APND isoenzyme was similarly sensitive to Cd2+ in all three investigated fish species. The most sensitive species was the wels, and the least sensitive were the carp isoenzyme. FTIR spectroscopy confirmed that cadmium caused damage to the protein structure. These results support the enzyme activity measurements measured in vivo and in vitro.

AB - The in vivo and in vitro effects of Cd2+ and the CYP1A inductor β-naphthoflavone(β-NF) on the hepatic cytochrome P450 (Cyt 450) monooxygenases were studied in silver carp (Hypophthalmichtys molitrix V.), wels (Silurus glanis L.), and carp (Cyprinus carpio). In vivo treatment of carp with a high dose of Cd2+ (10 mg kg-1, for 3 days) caused a strong inhibition of 7-ethoxyresorufin-O-deethylase (EROD) and a lower inhibition of 7-ethoxycoumarin-O-deethylase (ECOD) activity. The low-dose cadmium treatment (2 mg kg-1 Cd2+, for 6+3 days) resulted in 4-fold increase in EROD and a 3-fold increase in ECOD activity. The combined treatment with Cd2+ and β-NF in both cases led to a loss of EROD inducibility. The silver carp and wels were treated with 10 mg L-1 Cd2+ for 72 h in water. The Cyt P450 content in the wels liver microsomes was increased significantly after treatment for 48 h, whereas there was only a slight, not significant increase in Cyt P450 content in the silver carp microsomes. While the Cd2+ treatment resulted in inhibition of the CYP1A isoenzymes (EROD and ECOD), the APND (aminopyrene-N-demethylase, CYP2B or CYP3A isoenzyme) activity was increased 3- to 4-fold in both fish species. In vitro experiments of the effect of Cd2+ led to a concentration-dependent inhibition in all three investigated fish species. The ECOD isoenzyme of silver carp was the most sensitive to Cd2+. The lowest concentration of Cd2+ resulted in 50% inhibition. The APND isoenzyme was similarly sensitive to Cd2+ in all three investigated fish species. The most sensitive species was the wels, and the least sensitive were the carp isoenzyme. FTIR spectroscopy confirmed that cadmium caused damage to the protein structure. These results support the enzyme activity measurements measured in vivo and in vitro.

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KW - Cytochrome P450

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KW - IR spectroscopy

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