Glutathione S-transferase activity and genetic polymorphisms associated with exposure to organochloride pesticides in Todos Santos, BCS, Mexico: a preliminary study

Abstract Fast protein liquid chromatography (anion exchange) was used to separate glutathione S-transferase isozymes in nontreated etiolated maize shoots and those treated with the herbicide safener CGA -1542814-(dichloroacetyl)-3,4-dihydro-3-methyl-2 H-1 ,4-benzoxazine. Nontreated shoots contained isozymes active with the following substrates: trans-cinnamic acid (1 isozyme), atrazine (3 isozymes), 1-chloro-2,4-dinitrobenzene (1 isozyme), metolachlor (2 isozymes) and the sulfoxide derivative of S-ethyl dipropylcarbamothioate (2 isozymes). Pretreatment of shoots with the safener CGA -154281 (1 μM) had no effect on the activity of the isozymes selective for trans-cinnamic acid and atrazine but increased the activity of the constitutively-expressed isozymes that exhibit activity with 1-chloro-2,4-dinitrobenzene, metolachlor and the sulfoxide derivative of S-ethyl dipropylcarbamothioate. The safener pretreatment also caused the appearance of one new isozyme active with 1-chloro-2,4-dinitrobenzene and one new isozyme active with metolachlor. The results illustrate the complexity of glutathione S-transferase activity in etiolated maize shoots, and the selective enhancement of glutathione S-transferase isozymes by the safener CGA -154281.

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Urinary thioethers in workers exposed to the asphalt: An impairment of glutathione s‐transferase activity?

Journal of Toxicology and Environmental Health ◽

10.1080/15287398709531041 ◽

1987 ◽

Vol 21 (4) ◽

pp. 533-534 ◽

Cited By ~ 9

Author(s):

Amalia Lafuente ◽

Jordi Mallol

Keyword(s):

Transferase Activity ◽

Glutathione S Transferase ◽

Urinary Thioethers

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The distribution, induction and isoenzyme profile of glutathione S-transferase and glutathione peroxidase in isolated rat liver parenchymal, Kupffer and endothelial cells

Biochemical Journal ◽

10.1042/bj2640737 ◽

1989 ◽

Vol 264 (3) ◽

pp. 737-744 ◽

Cited By ~ 18

Author(s):

P Steinberg ◽

H Schramm ◽

L Schladt ◽

L W Robertson ◽

H Thomas ◽

...

Keyword(s):

Endothelial Cells ◽

Glutathione Peroxidase ◽

Rat Liver ◽

Peroxidase Activity ◽

Cell Types ◽

Transferase Activity ◽

Glutathione Peroxidase Activity ◽

Glutathione S Transferase ◽

Liver Parenchymal ◽

Parenchymal Cells

The distribution and inducibility of cytosolic glutathione S-transferase (EC 2.5.1.18) and glutathione peroxidase (EC 1.11.1.19) activities in rat liver parenchymal, Kupffer and endothelial cells were studied. In untreated rats glutathione S-transferase activity with 1-chloro-2,4-dinitrobenzene and 4-hydroxynon-2-trans-enal as substrates was 1.7-2.2-fold higher in parenchymal cells than in Kupffer and endothelial cells, whereas total, selenium-dependent and non-selenium-dependent glutathione peroxidase activities were similar in all three cell types. Glutathione S-transferase isoenzymes in parenchymal and non-parenchymal cells isolated from untreated rats were separated by chromatofocusing in an f.p.l.c. system: all glutathione S-transferase isoenzymes observed in the sinusoidal lining cells were also detected in the parenchymal cells, whereas Kupffer and endothelial cells lacked several glutathione S-transferase isoenzymes present in parenchymal cells. At 5 days after administration of Arocolor 1254 glutathione S-transferase activity was only enhanced in parenchymal cells; furthermore, selenium-dependent glutathione peroxidase activity decreased in parenchymal and non-parenchymal cells. At 13 days after a single injection of Aroclor 1254 a strong induction of glutathione S-transferase had taken place in all three cell types, whereas selenium-dependent glutathione peroxidase activity remained unchanged (endothelial cells) or was depressed (parenchymal and Kupffer cells). Hence these results clearly establish that glutathione S-transferase and glutathione peroxidase are differentially regulated in rat liver parenchymal as well as non-parenchymal cells. The presence of glutathione peroxidase and several glutathione S-transferase isoenzymes capable of detoxifying a variety of compounds in Kupffer and endothelial cells might be crucial to protect the liver from damage by potentially hepatotoxic substances.

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