Engineering tolerance and hyperaccumulation of arsenic in plants by combining arsenate reductase and γ-glutamylcysteine synthetase expression

2002 ◽  
Vol 20 (11) ◽  
pp. 1140-1145 ◽  
Author(s):  
Om Parkash Dhankher ◽  
Yujing Li ◽  
Barry P. Rosen ◽  
Jin Shi ◽  
David Salt ◽  
...  
Keyword(s):  
Arsenate Reductase ◽  
Glutamylcysteine Synthetase

scholarly journals Some Properties of γ-Glutamylcysteine Synthetase

1960 ◽  
Vol 235 (6) ◽  
pp. PC27
Author(s):  
David H. Strumeyer ◽  
Konrad Bloch
Keyword(s):  
Glutamylcysteine Synthetase

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.

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