Regulation of hepatic glutathione S-transferase expression in flounder

Scott, Karen; Leaver, Michael J.; George, Stephen

doi:10.1016/0141-1136(92)90113-z

Cited by 17 publications

(5 citation statements)

References 3 publications

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Section: Discussionmentioning

confidence: 62%

“…Fish liver glutathione S-transferase-A cDNA characterization and expression observed in the closely related flounder, Platichthysflesus (Scott et al, 1992). We have also observed in the flounder that inducers such as the polyaromatic hydrocarbon 3-methylcholanthrene, which act at the [Ah] locus (Nebert et al, 1990), do not affect or may even suppress mRNA for GST-A in this species, whereas trans-stilbene oxide induces GST-A mRNA in both plaice and flounder (Scott et al, 1992). This spectrum of inducer action differs from that observed in mammals, where both trans-stilbene oxide and polyaromatic hydrocarbons induce the Alpha class GST-1 of rats and Mu class GST of mouse (DiSimplicio et al, 1989;Hayes et al, 1991;Rushmore et al, 1991), again supporting the conclusion from the sequence, substrate specificity, ligand binding and immunological data (above and George and Buchanan, 1990;George et al, 1989) that plaice GST-A is not an Alpha or Mu class orthologue.…”

Section: Discussionmentioning

confidence: 62%

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Cloning and characterization of the major hepatic glutathione S-transferase from a marine teleost flatfish, the plaice (Pleuronectes platessa), with structural similarities to plant, insect and mammalian Theta class isoenzymes

Leaver

Scott

George

1993

Biochemical Journal

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A cDNA clone (PLGSTA) of 896 bp, containing an open reading frame encoding a 225-amino-acid polypeptide of M(r) 25,723, was isolated from a cDNA library constructed in lambda gt11 from the liver of a marine teleost flatfish, the plaice (Pleuronectes platessa). The identification of this cDNA as that coding for the subunit of the major cytosolic glutathione S-transferase of plaice liver, GST-A, was supported by its heterologous expression in and purification of its protein product from Escherichia coli. The recombinant-derived protein exhibited identical M(r) and immunoreactivity and a similar substrate specificity to GST-A previously isolated from plaice liver. Comparison of the deduced amino acid sequence of the plaice GST-A polypeptide with the primary structures of GSTs from other Phyla revealed that it showed the greatest similarity to plant, insect and mammalian Theta class GSTs. Southern blot analysis of plaice DNA hybridized to the PLGSTA cDNA showed a banding pattern indicative of the presence of a single gene. Northern blot analysis of a variety of plaice tissues showed hybridizing bands of approx. 1100 nucleotides in all tissues tested, with the highest relative amounts in liver and intestinal mucosa. A marked increase in hybridization intensity was observed in hepatic RNA samples from plaice treated with trans-stilbene oxide, suggesting that GST-A is induced by epoxides in this species.

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Section: Discussionmentioning

confidence: 62%

Section: Discussionmentioning

confidence: 62%

Cloning and characterization of the major hepatic glutathione S-transferase from a marine teleost flatfish, the plaice (Pleuronectes platessa), with structural similarities to plant, insect and mammalian Theta class isoenzymes

Leaver

Scott

George

1993

Biochemical Journal

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“…As GST são predominantemente enzimas de fração citosólica (95%), e uma pequena porção (5%) pertence à fração microssomal (retículo endoplasmático) e mitocondrial. As GSTs estão largamente distribuídas na natureza, podendo ser encontradas em plantas, bactérias, moluscos, insetos, peixes, anfíbios e mamíferos (RODRIGUES, 2003 Muitos estudos que analisaram a GST em fígado de peixe expostos a diferentes tipos inseticidas mostraram uma indução enzimática (ANDERSSON et al, 1985;LEAVER et al, 1992;RODRIGUEZ-ARIZA et al, 1991;SCOTT et al, 1992).…”

Section: 23) Atividade Da Glutationa S-transferaseunclassified

“…Segundo SCOTT et al (1992), linguados expostos a 3-MC (3-metilcolantreno) tiveram a glutationa S-transferase hepática reduzida sugerindo inibição do metabolismo, acredita-se que muitas variações entre populações de peixes nativos e entre a relação dose / resposta pode ser encontrada.…”

Section: E Emunclassified

Estresse de transporte em cascudos amazônicos ornamentais Cochliodon sp. (L145) e Hypostomus sp. (L28) (LORICARIIDAE)

et al. 2016

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In this study was evaluated the hematological response of ornamental Amazon plecos Cochliodon sp. (L145) and Hypostomus sp. (L28) submitted to transportation conditions. The erythrogram, leukogram, thrombogram, glucose and total plasma proteins (PPT) were determined at 0, 6, 24, 48 and 72 hours after 3-hours simulated transportation. For basal hematological profile, the blood was collected immediately to allow comparisons after the transport stress. Cochliodon sp. showed reduction in total erythrocyte after 6 and 24 hours of post-transport, and increase after 6 hours. Hypoglycemia were observed at 6 hours post-transport for Hypostomus sp. Thus, the Hypostomus sp. showed higher resistance compared to Cochliodon sp. when to the transport stress.

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“…There are reports indicating the role of induced GST activity in protection against the toxicity of xenobiotic-induced lipid peroxidation (Leaver and George, 1998). Many studies analysing GST activity in liver of fish exposed to different insecticides showed an enzymatic induction (Andersson et al, 1985;Rodriguez-Ariza et al, 1991;Leaver et al, 1992;Scott et al, 1992). Metabolites formed from detoxification of foreign compounds act as substrates for GST and modify the microsomal glutathione transferase covalently.…”

Section: Resultsmentioning

confidence: 99%

Antioxidant responses and lipid peroxidation in Mozambique tilapia (Oreochromis mossambicus) exposed to phenol and m-cresol

Varadarajan

Philip

2016

Indian J. Fish.

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The present study evaluated phenol and m-cresol induced oxidative stress responses in the teleost fish Oreochromis mossambicus in a semi-static test system in which water was renewed every 24 h. Fishes were exposed to sublethal (1/10 of LC 50 /96 h) concentration of phenol (3.12 mg l -1 ) and m-cresol (2.2 mg l -1 ) for a period of 21 days. Significant increases in catalase (CAT) and superoxide dismutase (SOD) activities in gills, liver and kidney of treated groups represent an adaptive response to free radical toxicity. Reduction in enzyme activity shows that all reactive oxygen species (ROS) are not being quenched. Glutathione-S-transferase (GST) activity was found to be highly elevated in liver which may be due to its important role in the detoxification of xenobiotics. Total reduced glutathione glutathiore peroxidase (GSH) level was found to be highest in liver which may be an adaptive mechanism to oxidative stress. An increased hydroperoxide (HP) level was observed in liver, kidney and muscle of both the treated groups which may be attributed to the decreased glutathione peroxidase (GPx) activity observed. Increased malondialdehyde (MDA) levels in gills and liver indicates that elevated antioxidant enzyme activities were not efficient enough to prevent lipid peroxidation in these tissues. Taken as a whole, the present results seem to implicate that phenolic compounds are potent mediators of free radical generation in fish.

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Regulation of hepatic glutathione S-transferase expression in flounder

Cited by 17 publications

References 3 publications

Cloning and characterization of the major hepatic glutathione S-transferase from a marine teleost flatfish, the plaice (Pleuronectes platessa), with structural similarities to plant, insect and mammalian Theta class isoenzymes

Cloning and characterization of the major hepatic glutathione S-transferase from a marine teleost flatfish, the plaice (Pleuronectes platessa), with structural similarities to plant, insect and mammalian Theta class isoenzymes

Estresse de transporte em cascudos amazônicos ornamentais Cochliodon sp. (L145) e Hypostomus sp. (L28) (LORICARIIDAE)

Antioxidant responses and lipid peroxidation in Mozambique tilapia (Oreochromis mossambicus) exposed to phenol and m-cresol

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