Effects of the Herbicide Pretilachlor and the Safener Fenclorim on Glutathione Content and Glutathione-Dependent Enzyme Activity of Rice

1991 ◽  
Vol 46 (9-10) ◽  
pp. 861-865 ◽  
Author(s):  
Seong Han ◽  
Kriton K. Hatzios
Keyword(s):  
Enzyme Activity ◽  
Time Course ◽  
Reduced Glutathione ◽  
Oryza Sativa L ◽  
Rice Seedlings ◽  
Glutathione S Transferase ◽  
Simultaneous Application ◽  
Related Enzyme ◽  
Time Course Study ◽  
Gst Activity

Abstract The influence of individual or combined treatments of the chloroacetanilide herbicide preti­lachlor and the safener fenclorim on glutathione content and the activity of glutathione reduc­tase (GR, EC 1.6.4.2) and glutathione-S-transferase (GST, EC 2.5.1.18) of rice (Oryza sativa L., var. Lamont) was investigated in a time-course study including 0, 12, 24, 48, and 72 h peri­ods after treatment. Pretilachlor applied alone at 2 μM did not influence the levels of total or reduced glutathione of germinating rice seedlings. Fenclorim applied alone at 20 μM increased significantly the levels of total and reduced glutathione of rice seedlings at 12, 24, and 72 h after treatment. The combination of pretilachlor and fenclorim increased the levels of total and reduced glutathione of rice at all time periods. GR activity extracted from pretilachlor-treated rice seedlings was significantly lower than that extracted from untreated rice seedlings. Pretreatment of rice seedlings with the safener fenclorim increased GR activity at 12 and 24 h, but not at 48 and 72 h after treatment. GR activity extracted from rice seedlings treated with the combination of pretilachlor and fenclorim was significantly higher than that of untreated controls at 12, 24, and 48 h after treatment. Pretreatment of rice seedlings with pretilachlor reduced the activity of GST which catalyzes the conjugation of this herbicide with reduced glutathione at time intervals greater than 24 h. Pretreatment with fenclorim did not have any effect on GST activity of rice seedlings. Pretreatment with the combination of pretilachlor and fenclorim increased GST activity of rice seedlings at the 48 and 72 h periods. These results suggest that a simultaneous application of pretilachlor and fenclorim is critical for the enhance­ment of glutathione and glutathione-related enzyme activity and the protection of rice from pretilachlor injury.

scholarly journals Differential regulation of antioxidant enzymes in Frankliniella occidentalis (Thysanoptera: Thripidae) exposed to thermal stress

PeerJ ◽  
2021 ◽  
Vol 9 ◽  
pp. e12089
Author(s):  
Jia-Wen Yuan ◽  
Yutao Zheng ◽  
Ya-Wen Chang ◽  
Jing Bai ◽  
Jing Qin ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Antioxidant Enzymes ◽  
Time Course ◽  
Frankliniella Occidentalis ◽  
Insect Pest ◽  
Expression Patterns ◽  
Global Scale ◽  
Antioxidant Genes ◽  
Agronomic Crops ◽  
Time Course Study

Frankliniella occidentalis is an invasive insect pest that incites damage to ornamental and agronomic crops on a global scale. In this study, the effects of temperature on gene expression and enzyme activity were studied for superoxide dismutase (SOD), peroxidase (POD), and glutathione-S-transferase (GST) in F. occidentalis. SOD, POD and GST enzyme activity increased significantly at 35–37 °C but declined as the temperature increased to 41 °C. In a time course study at 35 °C, SOD, POD and GST activities were significantly elevated at 0.5, 1 and 2 h in comparison to the control at 26 °C. Expression patterns were evaluated for the three antioxidant genes under high and low temperature stress. In a time course study at –4 °C, SOD, POD and GST expression peaked at 1 h and declined at 2 h of exposure. In contrast, when transcription was monitored at 35 °C, expression was lowest at 1 h and increased at 2 h. The results provide data that will be useful in deciphering the role of antioxidant enzymes in the adaptation of F. occidentalis to climate change.

scholarly journals Time Course of Starch Biosynthesis Enzymes Activity and Root Tuber Starch of Four Cassava Cultivars

2017 ◽  
Vol 5 (1) ◽  
pp. 103
Author(s):  
Huifang Huang ◽  
Yanchun Luo ◽  
Qiang Huang ◽  
Yinong Tian ◽  
Huimin Li ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Enzyme Activities ◽  
Time Course ◽  
Starch Content ◽  
Growth Period ◽  
Sucrose Phosphate Synthase ◽  
Soluble Starch ◽  
Root Tuber ◽  
Related Enzyme ◽  
Total Starch

To understand the accumulation rule of cassava root tuber starch, the amylose, amylopectin and total starch content of fresh root tuber, the enzyme activities of sucrose synthase (SuS, EC 2.4.1.13) and sucrose phosphate synthase (SPS, EC 2.4.1.14) of leaves, the enzyme activities of ADP-glucose pyrophosphorylase (AGPase, EC 2.7.7.27), soluble starch synthase (SSS, EC 2.4.1.21) and starch branching enzyme (SBE, EC. 2.4.1.18) of tubers were assessed by using cultivars SC201, SC205, GR891 and GR911 leaves and root tubers during their growth period, respectively. The results as follows: the enzyme activity of leaf SPS and the synthesis direction of SuS showed the highest at August, 2010, however the enzyme activity of the decomposing direction of SuS formed parabolic curve; the enzyme activity of tuber AGPase showed an increased then decreased single peak curve, the enzyme activity of tuber SSS oscillating decreased, while the enzyme activity of SBE was relatively stable; the amylose, amylopectin and total starch contents of fresh cassava tuber were all gradually increased along with the growth period. This research would enrich our knowledge of the time course of amylose, amylopectin and total starch contents of fresh cassava tuber, and above related enzyme activities.

Influence of Oxime Ether Safeners on Glutathione Content and Glutathione-Related Enzyme Activity in Seeds and Seedlings of Grain Sorghum

1990 ◽  
Vol 45 (1-2) ◽  
pp. 96-106 ◽  
Author(s):  
Samuel P. Yenne ◽  
Kriton K. Hatzios
Keyword(s):  
Glutathione Reductase ◽  
Reduced Glutathione ◽  
Reductase Activity ◽  
Grain Sorghum ◽  
Transferase Activity ◽  
Glutathione S Transferase ◽  
Oxime Ether ◽  
Reaction Solution ◽  
Glutathione Reductase Activity ◽  
Related Enzyme

The influence of the oxime ether safeners, oxabetrinil and CGA-133205, on glutathione content, glutathione reductase (EC 1.6.4.2), and glutathione-S-transferase (EC 2.5.1.18) activity in seeds and seedlings of grain sorghum (Sorghum bicolor (L.) Moench. var. Funk G-522-DR) was investigated. Plant material for these experiments was derived from seed that was either untreated, or treated with 1.25 or 0.4g ai/kg seed of oxabetrinil or CGA-133205, respectively. Measurements were conducted at 0, 1, 2, 4, 8 , 12, 24, 36, and 72 h after the initiation of germination. In safener-treated sorghum seeds, the levels of total and reduced glutathione decreased gradually after the initiation of germination reaching a low at 8 to 12 h and then increased continuously reaching a maximum at 48 h. The greatest increases in glutathione levels were observed in oxabetrinil-treated sorghum seedlings. Glutathione reductase activity was consistently higher in untreated seeds of grain sorghum for the first 24 h of imbibition, but at 36 to 72 h glutathione reductase activity increased in the safener-treated tissues. CGA-133205 appeared to have a greater stimulatory influence on the activity of glutathione reductase than did oxabetrinil. For the first 8 h after germination was initiated, glutathione-S-transferase activity in oxabetrinil- and CGA-133205-treated seeds remained enhanced compared to that of untreated seeds, but was at or below the levels of the activity of glutathione-S-transferase extracted from untreated seeds for the remainder of the experiment. Non-enzymatic conjugation of metolachlor with reduced glutathione increased as the pH of the reaction solution increased from 6.0 to 8.0. Oxabetrinil at 1 to 40 μM and CGA-133205 at 1 to 160 μm enhanced nonenzymatic conjugation of m etolachlor with glutathione. At 80 and 160 |j.m , oxabetrinil reduced the am oun t of non-enzym atic conjugation of metolachlor. Oxabetrinil conjugated with reduced glutathione at low rates either enzymatically or non-enzymatically at pH 8.0 while CGA-133205 did not at any pH. In the presence of metolachlor, the amount of non-enzymatic conjugation of oxabetrinil was decreased, indicating that metolachlor is more reactive towards glutathione than is oxabetrinil. Overall, these data suggest that during the early stages of seed germination and seedling development of grain sorghum , oxim e ether safeners can enhance the detoxication of the herbicide, metolachlor, through enzymatic or non-enzymatic conjugation to reduced glutathione by enhancing either the level of reduced glutathione and/or the activity of glutathione-related enzymes.

scholarly journals Effect of Endogenous Selenium on Arsenic Uptake and Antioxidative Enzymes in As-Exposed Rice Seedlings

2019 ◽  
Vol 16 (18) ◽  
pp. 3350 ◽  
Author(s):  
Aboubacar Younoussa Camara ◽  
Yanan Wan ◽  
Yao Yu ◽  
Qi Wang ◽  
Kang Wang ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Human Health ◽  
Oryza Sativa L ◽  
Human Consumption ◽  
Rice Seedlings ◽  
Simultaneous Application ◽  
Arsenic Uptake ◽  
Rice Roots ◽  
Mda Content ◽  
As Toxicity

Arsenic (As) and selenium (Se) are two metalloids found in the environment. As it poses a significant threat to human health and plant growth due to its prevalence and toxicity, however Se is a required micronutrient for human health. In this study hydroponic experiments were performed to investigate whether endogenous Se can mitigate As toxicity in rice (Oryza sativa L.). We found that As uptake by rice roots increased by pretreatment with selenateSe(VI) or selenite Se(IV). However, co-application of arsenate As(V) or arsenite As(III) with selenate markedly reduced the uptake of As by roots. Co- or pretreatment with Se with five µM of As(V) or one µM of As(III) significantly decreased shoot As content. Conversely, Se pretreatment before the addition of five µM of As(III) or one µM of As(V) resulted in As accumulation in the shoot compared to As and Se co-application. As translocation to the shoot was lower whereas the transfer factor was higher upon the simultaneous application of Se and As compared to Se pretreatment. Se supplementation with As(III) or pretreatment increased antioxidant enzymes: Superoxide dismutase (SOD), catalase (CAT), and peroxidase (POD) increased in the root and shoot, but decreased glutathione (GSH) and malondialdehyde (MDA) contents in the shoot. Plants under As(V) treatment showed the same trend except that CAT content decreased in the root and shoot, while MDA content increased in the shoot. These results suggest that cultivating rice in the presence of Se can reduce the accumulation of toxic As in seedlings, thus ensuring the safety of this important crop for human consumption.

Hepatic enzymatic activities of the european eel Anguilla anguilla as a tool for biomonitoring freshwater streams: laboratory and field caging studies

1996 ◽  
Vol 33 (6) ◽  
pp. 321-329 ◽  
Author(s):  
H. Fenet ◽  
C. Casellas ◽  
J. Bontoux
Keyword(s):  
Time Course ◽  
Anguilla Anguilla ◽  
Field Studies ◽  
Erod Activity ◽  
Polluted Site ◽  
European Eel ◽  
Glutathione S Transferase ◽  
Monooxygenase Activity ◽  
Hepatic Monooxygenase ◽  
Time Course Study

Hepatic monooxygenase activity and conjugation enzyme activity were studied in young european eel (Anguilla anguilla). Laboratories studies were performed by treatment with β-naphtoflavone (β-NF). Two sources of eels, wild and reared eels were compared during a time-course study. MO activities measured as 7-ethoxyresorufin O-deethylase (EROD) were induced by β-NF, peak values were reached 2 and 4 days after treatment. The time-course induction of EROD activity was similar for wild and reared eels. In contrast, the conjugation reaction enzymes measured as glutathione-S-transferase (GST) didn't respond to this treatment. During field studies, EROD and GST activities were studied in wild and reared eels held in cages upstream and downstream of a PAH polluted area. Similar induction of EROD activity was observed in the polluted site after 14 days of caging. The period of caging was studied and EROD activities were significantly induced in wild eels caged in the polluted site after 7 and 14 days. GST activities were not affected by the caging in the polluted site. The results indicate the usefulness of EROD activity as a biomarker of PAH contamination in the model of wild eels caging in the field.

Induction of Maize Glutathione S-Transferase by Herbicide Safener and their Effect on Enzyme Activity against Chlorsulfuron

2012 ◽  
Vol 518-523 ◽  
pp. 5480-5483 ◽  
Author(s):  
Li Xia Zhao ◽  
Cheng Guo Liu ◽  
Ying Fu ◽  
Zhi Yong Xing ◽  
Fei Ye ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Recovery Rate ◽  
Acetolactate Synthase ◽  
Kinetic Constants ◽  
Glutathione S Transferase ◽  
Chiral Compound ◽  
Herbicide Safener ◽  
Gst Activity

The acetolactate synthase(ALS) activity, glutathione S-transferase(GST) activity and glutathione(GSH) content in maize was investigated in response to treatments with safener (S)-3-dichloroacetyl-2,2-dimethyl-4-ethyl-1,3-oxazolidine. When induced by the chiral compound, the GSH content in root and shoot of maize increased 91.10% and 71.66%, respectively, the recovery rate of ALS activity reached 77%, and the GST activity increased 103.77%. The activity of maize GST was also assayed towards chlorsulfuron in vitro; the results showed that the induction of GST activity against chlorsulfuron of 14.54% was obtained. The enhancement of GST activity was found to be concomitant with changes in kinetic constants, which was related directly to the enzyme affinity for the CDNB substrate.

scholarly journals Characterization of methylation of rat liver cytosolic glutathione S-transferases by using reverse-phase h.p.l.c. and chromatofocusing

1990 ◽  
Vol 270 (2) ◽  
pp. 483-489 ◽  
Author(s):  
J A Johnson ◽  
T L Neal ◽  
J H Collins ◽  
F L Siegel
Keyword(s):  
Rat Liver ◽  
Time Course ◽  
Glutathione S Transferase ◽  
Reverse Phase ◽  
Cytosolic Glutathione ◽  
Glutathione S Transferases ◽  
Rat Liver Cytosol ◽  
Gst Activity

Glutathione S-transferase (GST) subunits in rat liver cytosol were separated by reverse-phase h.p.l.c.; five major proteins were isolated and identified as subunits 1, 2, 3, 4 and 8. F.p.l.c. chromatofocusing resolved the affinity-purified GST pool into nine different isoenzymes. The five basic (Alpha class) dimeric peaks of GST activity were 1-1, 1-2a, 1-2b, 2-2a and 2-2b. Reverse-phase h.p.l.c. analysis revealed that subunit 8 was also present in the protein peaks designated 1-1, 1-2a and 1-2b. The four neutral (Mu class) isoenzymes were 3-3, 3-4, 3-6 and 4-4. The GST pool was methylated in vitro before reverse-phase h.p.l.c. or f.p.l.c. chromatofocusing. Chromatofocusing indicated that the Mu class isoforms (3-3, 3-4 and 4-4) were the primary GSTs methylated, and h.p.l.c. analysis confirmed that subunits 3 and 4 were the major methyl-accepting GST subunits. The addition of calmodulin stimulated the methylation in vitro of GST isoenzymes 3-3, 3-4 and 4-4 by 3.0-, 7.5- and 9.9-fold respectively. Reverse-phase h.p.l.c. also indicated that only the methylation of GST subunits 3 and 4 was stimulated by calmodulin. Basic GST isoenzymes were minimally methylated and the methylation was not enhanced by calmodulin. Investigation of the time course of methylation of GST subunits 3 and 4 indicated that at incubation times less than 4 h the methylation of both Mu class subunits was stimulated by calmodulin, and that under such conditions subunit 4 was the preferred substrate. In contrast, there was essentially no calmodulin-stimulated methylation at incubation times of 4 or 6 h, and the methylation of subunit 3 was predominant. Kinetic parameters at 2 h of incubation were determined in the presence and in the absence of calmodulin. The addition of calmodulin doubled the Vmax. for methylation of both subunits 3 and 4 and decreased the Km of subunit 4 for S-adenosyl-L-methionine 3.6-fold. Finally, methylation was substoichiometric and after 6 h of incubation ranged from 2.8 to 7.6% on a mole-to-mole basis for subunits 4 and 3 respectively.

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