scholarly journals Stress Tolerance in Transgenic Tobacco Seedlings that Overexpress Glutathione S-Transferase/Glutathione Peroxidase

2000 ◽  
Vol 41 (11) ◽  
pp. 1229-1234 ◽  
Author(s):  
Virginia P. Roxas ◽  
Sundus A. Lodhi ◽  
Daniel K. Garrett ◽  
James R. Mahan ◽  
Randy D. Allen
Keyword(s):  
Glutathione Peroxidase ◽  
Stress Tolerance ◽  
Transgenic Tobacco ◽  
Glutathione S Transferase ◽  
Tobacco Seedlings

Overexpression of glutathione S-transferase/glutathioneperoxidase enhances the growth of transgenic tobacco seedlings during stress

1997 ◽  
Vol 15 (10) ◽  
pp. 988-991 ◽  
Author(s):  
Virginia P. Roxas ◽  
Roger K. Smith ◽  
Eric R. Allen ◽  
Randy D. Allen
Keyword(s):  
Transgenic Tobacco ◽  
Glutathione S Transferase ◽  
Tobacco Seedlings

scholarly journals Effect of Cross-Sex Hormonal Replacement on Antioxidant Enzymes in Rat Retroperitoneal Fat Adipocytes

2016 ◽  
Vol 2016 ◽  
pp. 1-12 ◽  
Author(s):  
Israel Pérez-Torres ◽  
Verónica Guarner-Lans ◽  
Alejandra Zúñiga-Muñoz ◽  
Rodrigo Velázquez Espejel ◽  
Alfredo Cabrera-Orefice ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Superoxide Dismutase ◽  
Antioxidant Enzymes ◽  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Enzymatic Activities ◽  
Glutathione S Transferase ◽  
Control Groups ◽  
Intact Female ◽  
Hormonal Replacement

We report the effect of cross-sex hormonal replacement on antioxidant enzymes from rat retroperitoneal fat adipocytes. Eight rats of each gender were assigned to each of the following groups: control groups were intact female or male (F and M, resp.). Experimental groups were ovariectomized F (OvxF), castrated M (CasM), OvxF plus testosterone (OvxF + T), and CasM plus estradiol (CasM + E2) groups. After sacrifice, retroperitoneal fat was dissected and processed for histology. Adipocytes were isolated and the following enzymatic activities were determined: Cu-Zn superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPx), glutathione-S-transferase (GST), and glutathione reductase (GR). Also, glutathione (GSH) and lipid peroxidation (LPO) were measured. In OvxF, retroperitoneal fat increased and adipocytes were enlarged, while in CasM rats a decrease in retroperitoneal fat and small adipocytes are observed. The cross-sex hormonal replacement in F rats was associated with larger adipocytes and a further decreased activity of Cu-Zn SOD, CAT, GPx, GST, GR, and GSH, in addition to an increase in LPO. CasM + E2exhibited the opposite effects showing further activation antioxidant enzymes and decreases in LPO. In conclusion, E2deficiency favors an increase in retroperitoneal fat and large adipocytes. Cross-sex hormonal replacement in F rats aggravates the condition by inhibiting antioxidant enzymes.

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.

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

1989 ◽  
Vol 264 (3) ◽  
pp. 737-744 ◽  
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.

Ectopic expression of a fruit phytoene synthase from Citrus paradisi Macf. promotes abiotic stress tolerance in transgenic tobacco

2012 ◽  
Vol 39 (12) ◽  
pp. 10201-10209 ◽  
Author(s):  
Luciana C. Cidade ◽  
Tahise M. de Oliveira ◽  
Amanda F. S. Mendes ◽  
Amanda F. Macedo ◽  
Eny I. S. Floh ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Stress Tolerance ◽  
Transgenic Tobacco ◽  
Abiotic Stress Tolerance ◽  
Ectopic Expression ◽  
Phytoene Synthase ◽  
Citrus Paradisi

Glutathione peroxidase, glutathione reductase, glutathione S-transferase, and γ-glutamyltranspeptidase activities in the human early pregnancy placenta

1983 ◽  
Vol 29 (2) ◽  
pp. 143-148 ◽  
Author(s):  
Carmine Di Ilio ◽  
Giovanni Polidoro ◽  
Arduino Arduini ◽  
Antonio Muccini ◽  
Giorgio Federici
Keyword(s):  
Glutathione Peroxidase ◽  
Glutathione Reductase ◽  
Early Pregnancy ◽  
Glutathione S Transferase

Circadian variations in glutathione-S-transferase and glutathione peroxidase activities in the mouse

1983 ◽  
Vol 19 (1-2) ◽  
pp. 23-27 ◽  
Author(s):  
M.H. Davies ◽  
H.P. Bozigian ◽  
B.A. Merrick ◽  
D.F. Birt ◽  
R.C. Schnell
Keyword(s):  
Glutathione Peroxidase ◽  
Glutathione S Transferase ◽  
Circadian Variations

Leaf-specific overexpression of plastidic glutamine synthetase stimulates the growth of transgenic tobacco seedlings

Planta ◽  
2000 ◽  
Vol 210 (2) ◽  
pp. 252-260 ◽  
Author(s):  
Andrea Migge ◽  
Elisa Carrayol ◽  
Bertrand Hirel ◽  
Thomas W. Becker
Keyword(s):  
Glutamine Synthetase ◽  
Transgenic Tobacco ◽  
Tobacco Seedlings
Sign in / Sign up

Export Citation Format

Share Document