Studies on glutathione S-transferase in Helicoverpa ( = Heliothis) zea

Chien, C.; Dauterman, W.C.

doi:10.1016/0020-1790(91)90092-s

Cited by 42 publications

(12 citation statements)

References 34 publications

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“…In addition, increased levels of GSTs in insecticideresistant strains of various insects have been reported (Yu 1984;Reidy et al 1990;Hasspieler et al 1990;Chien and Dauterman 1991 ;Wang et al 1991 ;Ottea and Plapp 1984;Fournier et al 1992). Many of the inducers and insecticides studied share a similar prooxidant mechanism, implying that GSTs act to protect insects by participating in the repair of peroxidative damage.…”

Section: Discussionmentioning

confidence: 88%

“…In addition, 10 species within the genus Aedes have been shown to express two subunits that cross-react with antisera to one of the three subunits isolated from A. aegypti (Grant 199 1). While several reports suggest the existence of only one isozyme in some species (Chien and Dauterman 1991;Cochrane et al 1987;Wood et al 1986), it is important to note that the application of different isolation procedures to these same species has in at least two cases demonstrated the presence of multiple forms (Toung and Tu 1992;Yu 1989). Clearly, structural complexity is a feature shared by mammalian and insect GSTs.…”

Section: Introductionmentioning

confidence: 95%

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Genetic and biochemical analysis of glutathione-S-transferase in the oxygen defense system of Drosophila melanogaster

Parkes¹,

Hilliker²,

Phillips³

1993

Genome

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Aerobic organisms possess an array of enzymatic defense mechanisms against the toxic effects of active oxygen species. These include CuZn superoxide dismutase (CuZn SOD), catalase (CAT), and glutathione peroxidase (GPOX). Insects, however, lack an independent GPOX enzyme and instead rely on the activity of the more general detoxification enzyme, glutathione-S-transferase (GST), to carry out a peroxidase function. We report here the developmental profile of GST in Drosophila melanogaster and show that GST is induced by paraquat, a known free-radical generating agent. We also report that glutathione (GSH) depletion induced by administration of buthionine sulfoximine (BSO) selectively reduces the viability of mutants lacking CuZnSOD. By measuring GST specific activity in flies carrying deficiencies for the 87B region, we confirm an earlier report that this region contains active GST-encoding genes. Finally, through a biochemical analysis of representative alleles of known lethal complementation gene. The implications of these findings to the role of GSH and GST in D. melanogaster oxygen defense are discussed.

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Section: Discussionmentioning

confidence: 88%

Section: Introductionmentioning

confidence: 95%

Genetic and biochemical analysis of glutathione-S-transferase in the oxygen defense system of Drosophila melanogaster

Parkes¹,

Hilliker²,

Phillips³

1993

Genome

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“…The decrease in absorbance was recorded at 340 nm at 30°C. GSTs were extracted and estimated according to the method of Chien and Dauterman (1991). The homogenate (2% w/v) was prepared in 0.1 M sodium phosphate buffer (pH 7.6) containing 0.1 mM phenyl thiourea.…”

Section: Experiments 2: Biochemical Analysis Of Enzymesmentioning

confidence: 99%

Bioactivity of pyrogallol against melon fruit fly, Bactrocera cucurbitae

Sohal

Sharma

2011

Phytoparasitica

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The insecticidal effects of pyrogallol were studied by treating eggs and larvae of the melon fruit fly, Bactrocera cucurbitae (Coquillett) (Tephritidae: Diptera), with various concentrations (1, 5, 25, 125, 625 and 3125 ppm) of the phenolic compound. Although egg hatching decreased following treatment of 0-8-h old eggs with pyrogallol, the decrease was not significantly different from the control. Larval period and total development period declined significantly in 64-72-h-old and 88-96-h-old B. cucurbitae larvae fed on pyrogallol-treated diet. However, in the 44-48-h-old larvae, the larval period and total development period were not affected by pyrogallol treatment at any of the tested concentrations. None of them survived up to the pupal stage at the highest concentration. Number of pupae formed and adult emergence decreased significantly in all larval instars following feeding on pyrogallol-treated diet. The analysis of enzymes in 64-72-h-old larvae treated with LC 40 concentration (16.21 ppm) of pyrogallol at three time intervals, i.e., 24 h, 48 h and 72 h, showed significant induction in the activities of ascorbate peroxidase (APOX) and glutathione S-transferases (GSTs) at 24 h but a decrease was observed following prolonged treatment. On the other hand, superoxide dismutase (SOD) and peroxidases (POX) activity remained suppressed during the initial treatment interval but increased with prolonged treatment in 136-144-h-old larvae. The catalase (CAT) activity was suppressed at all treatment durations whereas glutathione reductase (GR) activity was not affected by pyrogallol treatment. An increase in the activities of ascorbate peroxidase, superoxide dismutase, peroxidases and glutathione S-transferases indicates an induction of defensive response of the melon fruit fly to the toxic effects produced by ingestion of pyrogallol. Although the effects of the compound on enzyme activity were tested on second instar, it would be interesting to see the effects on other instars too.

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“…24, 48 and 72 h. Activity determination of esterases was based on the methodology outlined by Katzenellenbogen and Kafatos (1971). Glutathione S-transferase (GST) activity was obtained by using sodium phosphate buffer (0.1 M, pH 7.6) as an extraction buffer and 10 mM 1-chloro-2,4-dinitrobenzene in 95% ethanol as a substrate solution according to the methodology given by Chien and Dauterman (1991). The activity of acid and alkaline phosphatases was assessed by the procedure given by McIntyre (1971) using the substrate 5 mM sodium a-naphthyl phosphate in 0.05 M acetate buffer (pH 5.0).…”

Section: Enzyme Assaysmentioning

confidence: 99%

Biopotency of partially purified protease inhibitor from peas on the larval growth, development and enzyme system of Bactrocera cucurbitae (Diptera: Tephritidae)

Kaur

Sohal

2012

Int. J. Trop. Insect Sci.

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Plant protease inhibitors (PI) constitute a major class of defence proteins being selected as an important strategy towards insect herbivory. With the objective of assessing the effect of PI towards larval growth and development, an artificial diet bioassay using partially purified PI obtained from peas was performed on the melon fruit fly Bactrocera cucurbitae (Coquillett). Larval growth and developmental parameters were assessed at different concentrations (namely 12.5, 25, 50, 100, 200 and 400 mg/ml) on the second-instar larvae of B. cucurbitae. Growth and survival responses determined the antiinsect potential of this PI even in its partially purified state. Larval and total development periods were found to be significantly prolonged for the larvae fed on an artificial diet incorporated with pea PI when compared with those fed with a control diet. Furthermore, when compared with the effect of the control diet (no inhibitor), the partially purified pea PI in the diet reduced larval weight gain, mean larval growth rate and food assimilated with respect to the control of the second-instar larvae tested at the same range of concentrations. The relative effectiveness of pea PI on these parameters is in agreement with the results obtained for percentage of pupation and percentage of adult emergence, as these parameters were significantly affected by the increase in the PI concentration in the artificial diet. Feeding the second-instar larvae a diet containing a range of concentrations (50, 100, 200 and 400 mg/ml) of partially purified pea PI significantly reduced the activities of digestive enzymes (trypsin, chymotrypsin, elastase and leucine aminopeptidase) and significantly affected the activities of other non-digestive enzymes (esterase, acid and alkaline phosphatases, glutathione S-transferase, superoxide dismutase and catalase).

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Studies on glutathione S-transferase in Helicoverpa ( = Heliothis) zea

Cited by 42 publications

References 34 publications

Genetic and biochemical analysis of glutathione-S-transferase in the oxygen defense system of Drosophila melanogaster

Genetic and biochemical analysis of glutathione-S-transferase in the oxygen defense system of Drosophila melanogaster

Bioactivity of pyrogallol against melon fruit fly, Bactrocera cucurbitae

Biopotency of partially purified protease inhibitor from peas on the larval growth, development and enzyme system of Bactrocera cucurbitae (Diptera: Tephritidae)

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