Inhibition of glutathione S-transferase catalyzed xenobiotic detoxication by organotin compounds in tropical marine fish tissues

The inhibition of glutathione S-transferase (GST) activities by tributyltin (TBT), triphenyltin (TPT), dibutyltin dichloride (DBT) and tin is presented from toxicity studies on Siganus canaliculatus and Sparus sarba captured from the Arabian gulf coast bordering Abu Dhabi. Comparison of the constitu...

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Bibliographic Details
Published in:Bulletin of environmental contamination and toxicology 1999-02, Vol.62 (2), p.207-213
Main Authors: AL-GHAIS, S. M, ALI, B
Format: Article
Language:English
Subjects:
Agnatha. Pisces
Animal tissues
Animal, plant and microbial ecology
Animals
Applied ecology
Biodegradation, Environmental
Biological and medical sciences
Ecotoxicology, biological effects of pollution
Effects of pollution and side effects of pesticides on vertebrates
Fishes - physiology
Fundamental and applied biological sciences. Psychology
Glutathione Transferase - drug effects
Glutathione Transferase - metabolism
Inactivation, Metabolic
Marine
Marine fish
Organotin Compounds - pharmacology
Water Pollutants, Chemical - toxicity
Xenobiotics - pharmacokinetics
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Summary:The inhibition of glutathione S-transferase (GST) activities by tributyltin (TBT), triphenyltin (TPT), dibutyltin dichloride (DBT) and tin is presented from toxicity studies on Siganus canaliculatus and Sparus sarba captured from the Arabian gulf coast bordering Abu Dhabi. Comparison of the constitutive levels of hepatic and renal GST activities towards CDNB (1-chloro-2,4-dinitrobenzene), a non-specific substrate, demonstrated that S. canaliculatus was 4 and 2 times more efficient than S. sarba in the GST-dependent detoxication of xenobiotics in the liver and kidney, respectively. K50 values showed all organotins inhibited GST activity in-vitro at uM concentrations in both fish species, with a 2-3 fold higher inhibition in S. canaliculatus. Enzyme inhibitory potency of organotins was in the order of TBT, TPT and DBT. Tin did not cause any significant change in the level of inhibition indicating a reversible nature of the inhibition. The results were consistent with the effectiveness and pattern of in-vitro inhibition of rat liver GST by TBT and TPT, also shown to be reversible. There were marked species, tissue and organotin structure-related differences in the magnitude of GST inhibition.
ISSN:0007-4861
1432-0800
DOI:10.1007/s001289900861