Gene- and organ-specific impact of paracetamol on Solanun nigrum L.’s γ-glutamylcysteine synthetase and glutathione S-transferase and consequent phytoremediation fitness

2021 ◽  
Vol 43 (4) ◽  
Author(s):  
Leonor Martins ◽  
Jorge Teixeira
Keyword(s):  
Glutathione S Transferase ◽  
Glutamylcysteine Synthetase ◽  
Organ Specific ◽  
Specific Impact

Reductant substrate for glutathione peroxidase modulates oxidant inhibition of Ca2+ signaling in endothelial cells

1995 ◽  
Vol 268 (1) ◽  
pp. H278-H287 ◽  
Author(s):  
S. J. Elliott ◽  
T. N. Doan ◽  
P. N. Henschke
Keyword(s):  
Endothelial Cells ◽  
Glutathione Peroxidase ◽  
Oxidant Stress ◽  
Glutathione S Transferase ◽  
Glutathione Redox Cycle ◽  
Tert Butyl Hydroperoxide ◽  
Intracellular Glutathione ◽  
Glutamylcysteine Synthetase ◽  
Dependent Signal

Oxidant stress mediated by tert-butyl hydroperoxide (t-BOOH) inhibits agonist-stimulated Ca2+ entry and internal store Ca2+ release in cultured endothelial cells. The role of intracellular glutathione in modulating the effects of oxidant stress on Ca2+ signaling was determined in cells preincubated with buthionine-[S,R]-sulfoximine (BSO), an inhibitor of gamma-glutamylcysteine synthetase, or 1-chloro-2,4-dinitrobenzene (CDNB), a cosubstrate for glutathione-S-transferase. BSO and CDNB decreased endothelial cell glutathione content by 85 and 97%, respectively (control glutathione, 21.5 +/- 2.3 nmol/mg protein). Each agent accelerated the time-dependent effects of t-BOOH on Ca2+ signaling in fura 2-loaded cells and potentiated the inhibition of bradykinin-stimulated 45Ca2+ efflux induced by t-BOOH. These results indicate that decreased availability of reduced glutathione, the primary cosubstrate for glutathione peroxidase, potentiates the effect of hydroperoxide oxidant stress on receptor-operated Ca2+ entry across the plasmalemma and Ca2+ release from internal stores. The present findings suggest that intracellular glutathione availability and/or glutathione redox cycle activity are critically important modulators of oxidant inhibition of Ca(2+)-dependent signal transduction.

Glutathione metabolism in heart and liver of the aging rat

1994 ◽  
Vol 72 (1-2) ◽  
pp. 58-61 ◽  
Author(s):  
M. Stio ◽  
T. Iantomasi ◽  
F. Favilli ◽  
P. Marraccini ◽  
B. Lunghi ◽  
...  
Keyword(s):  
Rat Heart ◽  
Reduced Glutathione ◽  
Age Groups ◽  
Glutathione Metabolism ◽  
Oxidized Glutathione ◽  
Glutathione S Transferase ◽  
Age Related ◽  
Glutamylcysteine Synthetase ◽  
Old Rats ◽  
Glucose 6 Phosphate Dehydrogenase

A comprehensive study on glutathione metabolism in rat heart and liver as a function of age was performed. In the heart, reduced glutathione, total glutathione, and the glutathione redox index showed a decrease during aging, while oxidized glutathione levels increased in 5-month-old rats with respect to the young animals and remained quite constant in 14- and 27-month-old rats. In the liver, the highest levels of reduced glutathione were found in the 2-month-old rats, while oxidized glutathione reached a peak at 5 months. Glutathione-associated enzymes showed age-related changes. Glutathione peroxidase, unaffected by aging in the heart, decreased in the liver of the 27-month-old rats. In the heart and the liver, the highest values of glutathione S-transferase were found at 5 months and 27 months, respectively. Glucose-6-phosphate dehydrogenase followed a similar trend in both heart and liver. Glutathione reductase also showed the same behaviour in heart and in liver, increasing in old rats with respect to the other age groups. A decrease in γ-glutamylcysteine synthetase was found in the heart and liver of 27-month-old rats in comparison with the 2-month-old ones. In conclusion, a decreased antioxidant capability has been demonstrated in both heart and liver of old rats.Key words: glutathione metabolism, age, rat heart, rat liver.

Relationship between anoxia exposure and antioxidant status in the frog Rana pipiens

1996 ◽  
Vol 271 (4) ◽  
pp. R918-R925 ◽  
Author(s):  
M. Hermes-Lima ◽  
K. B. Storey
Keyword(s):  
Skeletal Muscle ◽  
Lipid Peroxidation ◽  
Rana Pipiens ◽  
Thiobarbituric Acid ◽  
Leopard Frog ◽  
Antioxidant Defenses ◽  
Glutathione S Transferase ◽  
Glutathione Status ◽  
Organ Specific

The biochemical adaptations of cellular antioxidant defenses that permit anoxia-tolerant animals to deal effectively with rapid and large changes in oxygen availability, and hence oxidative stress, during transitions from anoxia to normoxia provide insights into the strategies of antioxidant defense that could help to minimize reperfusion injuries to mammalian organs after anoxia/ischemia stress. The present study analyzes the effects of 30 h anoxia exposure followed by reoxygenation on the antioxidant defenses (activities of five enzymes, glutathione status) and lipid peroxidation damage to organs of the leopard frog Rana pipiens (5 degrees C-adapted autumn frogs). Exposure to 30 h anoxia resulted in significant increases in the activities of skeletal muscle and heart catalase (by 53 and 47%), heart and brain glutathione peroxidase (by 75 and 30%), and brain glutathione S-transferase (by 66%). In most cases, enzyme activities had returned to the control values after 40 h aerobic recovery. Activities of superoxide dismutase and glutathione reductase were unaltered in all of the organs, and anoxia/recovery had no effect on any of the enzymes in liver. Glutathione equivalents (GSH-eq) were maintained in four organs during anoxia but decreased by 32% in brain during anoxia. Brain GSH-eq had recovered after 90 min reoxygenation, and, in addition, hepatic GSH-eq rose by 71% after 90 min reoxygenation. The ratio of oxidized glutathione to GSH-eq was also affected by anoxia in an organ-specific way. Lipid peroxidation, assessed as the content of thiobarbituric acid-reactive substances (TBARS), was unaltered in skeletal muscle and liver after 30 h anoxia exposure or short (25 and 90 min)- or long-term (40 h) periods of reoxygenation, indicating that cycles of natural and survivable anoxia/reoxygenation occur without significant increase in TBARS in selected organs. Overall, the data demonstrate that elements of the antioxidant system of R. pipiens are induced during anoxia exposures as a possible preparation for dealing with potentially harmful oxygen reperfusion stress.

scholarly journals Effect of 4-coumaric and 3,4-dihydroxybenzoic acid on oxidative DNA damage in rat colonic mucosa

2003 ◽  
Vol 89 (5) ◽  
pp. 581-587 ◽  
Author(s):  
Francesco Guglielmi ◽  
Cristina Luceri ◽  
Lisa Giovannelli ◽  
Piero Dolara ◽  
Maura Lodovici
Keyword(s):  
Dna Damage ◽  
Vitamin E ◽  
Oxidative Dna Damage ◽  
Colonic Mucosa ◽  
Protocatechuic Acid ◽  
Coumaric Acid ◽  
Glutathione S Transferase ◽  
Glutamylcysteine Synthetase ◽  
Oxidation Damage

The effect of 4-coumaric and 3,4-dihydroxybenzoic (protocatechuic) acid on the basal oxidative DNA damage of rat colonic mucosa in vivo was studied, relative to vitamin E. F344 rats were treated with 4-coumaric or protocatechuic acid mixed in the diet (25 or 50 mg/kg for 2 weeks). It was observed that 4-coumaric acid (50 mg/kg) significantly decreased the basal level of the oxidative damage assessed as 8-OH-2′-deoxyguanosine levels in DNA and by the comet assay. Moreover, it was found that vitamin E (10 mg/kg) had no effect on colonic mucosa oxidation damage, whereas at a higher dose (55 mg/kg) it actually enhanced oxidative stress. The effect of 4-coumaric acid (50 mg/kg) on the expression of some glutathione-related enzymes (glutathione-S-transferase (GST)-P, GST-M2, GST-M1, γ-glutamylcysteine synthetase, glutathione peroxidase (GSPX)1 and GSPX4) was also investigated at the level of the colonic mucosa. Only the expression of GST-M2 was significantly induced by 4-coumaric acid, while protocatechuic acid was inactive. The data suggest that 4-coumaric acid acts as an antioxidant in the colonic mucosa in vivo.

scholarly journals Evaluation of Different Functional Antioxidant Groups and Protein Responses in Asian Seabass (Lates calcarifer Bloch, 1970) as an Early Indication of Fish Health in Aquaculture Farms.

2020 ◽  
Author(s):  
Mohamad Sofi Abu Hassan ◽  
Siti Nur Tahirah Jaafar ◽  
Nurulnadia Yusoff ◽  
Nik Nurasyikin Nik Azmi
Keyword(s):  
Antioxidant System ◽  
Strong Correlation ◽  
Slight Variation ◽  
Front Line ◽  
Glutathione S Transferase ◽  
Lates Calcarifer ◽  
Stress Evaluation ◽  
Organ Specific ◽  
Body Compartments ◽  
Early Indication

Abstract The study was conducted to investigate the organ-specific antioxidants and protein damages responses in Lates calcarifer inhabiting different aquaculture farms that susceptible to different threat of pollutions. Enzymes at the front line of antioxidant system superoxidase dismutase (SOD) and catalase (CAT) evidenced to work together but respond differently in different body compartment. High SOD responses were followed with lower CAT responses observed in muscle (p < 0.05) with opposite responses exhibited by both gill and liver. The responses of SOD and CAT in muscle also showed a significant strong correlation to each other (Setiu Wetland: 0.91, Semerak: 0.79) (p < 0.01). The glutathione-dependent enzymes, glutathione-s-transferase (GST) and glutathione reductase (GR) in body compartments responded with a strong correlation to each other especially in muscle (Tumpat; muscle: 0.89, gill: 0.95 and liver: 0.54 (p < 0.01, p < 0.05), (Setiu Wetland; muscle: 0.72 (p < 0.01) and Semerak; muscle: 0.79 (p < 0.01). Opposite results were found for both protein damages biomarkers, thiols (-SH-) and carbonyl (-CH-) in comparison to biomarkers responses. In contrary to (-SH-) inconsistent results were observed for the (-CH-) with muscle found to be most oxidised. The responses of SOD, CAT, GST, GR, thiols and carbonyl were all computed into the same scale through Integrated Biomarker Score (IBR) to classify each aquaculture farms based on biomarkers responses. There was a slight variation in deviation score (A) between organs within the range of (5-7). However, Tumpat overall showed the highest IBR score and significantly higher (p < 0.05) than Setiu Wetland with a total score of combining responses score in all three organs (IBR: 84, muscle: 31, gill: 24, and liver: 29) followed by intermediate score in Semerak (IBR: 72, muscle: 23, gill: 23 and liver: 26) and Setiu Wetland (IBR: 59, muscle: 18, gill: 23 and liver: 18). These results indicated that the responses of antioxidant enzymes and protein damages in L.calcarifer from different organs are heterogeneous. Therefore, biomarkers should be selected based on their sequential groups in the antioxidant system for a better explanation of the oxidative stress evaluation in fish.

Purification and characterization of a glutathione S-transferase Omega in pig: evidence for two distinct organ-specific transcripts

2001 ◽  
Vol 358 (1) ◽  
pp. 257-262 ◽  
Author(s):  
Patrick ROUIMI ◽  
Patricia ANGLADE ◽  
Anne BENZEKRI ◽  
Philippe COSTET ◽  
Laurent DEBRAUWER ◽  
...  
Keyword(s):  
Peptide Sequencing ◽  
Cross Reactivity ◽  
Glutathione S Transferase ◽  
Gene Encoding ◽  
Simple Method ◽  
Organ Specific ◽  
Cytosolic Glutathione ◽  
A Subunit ◽  
Internal Peptide

A cytosolic glutathione S-transferase (GST, EC 2.5.1.18) from the recently characterized Omega class [GSTO; Board et al. 2000, J. Biol. Chem. 275, 24798–24806] has been identified in pig organs. It was found widely distributed in the different tissues investigated and especially abundant in liver and muscle. The hepatic enzyme has been purified to homogeneity by using its selective affinity for S-hexylglutathione over GSH, thus providing a simple method to isolate mammalian GSTO. The dimeric protein has a subunit molecular mass of 27328Da as measured by electrospray ionization MS. Internal peptide sequencing and complete cDNA sequencing revealed strong similarities with its human recombinant orthologue and two rodent GST-like proteins with the ability to catalyse the GSH-dependent reduction of dehydroascorbate. Additional similarities, including the presence of a specific N-terminal extension and of immunological cross-reactivity, support the results. Moreover, this gene encoding GSTO generates two organ-specific transcripts, suggesting transcriptional mechanisms with a significance that is as yet uncharacterized.

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