Selenium Sources Affect Protein Concentration, Thioredoxin Reductase Activity and Selected Production Parameters in Reovirus Infected Broiler Chickens

2006 ◽  
Vol 5 (9) ◽  
pp. 822-829 ◽  
Author(s):  
Sigfrido Burgos ◽  
F. Edens . ◽  
J. Read-Snyder . ◽  
A. Cantor . ◽  
Sergio A. Burgos .
Keyword(s):  
Broiler Chickens ◽  
Protein Concentration ◽  
Reductase Activity ◽  
Thioredoxin Reductase ◽  
Production Parameters

scholarly journals Fluorogenic probes for thioredoxin reductase activity

2021 ◽  
Vol 3 ◽  
pp. 100127
Author(s):  
Tendai J. Mafireyi ◽  
Jorge O. Escobedo ◽  
Robert M. Strongin
Keyword(s):  
Reductase Activity ◽  
Thioredoxin Reductase ◽  
Fluorogenic Probes

scholarly journals Inhibition of Glutathione and Thioredoxin Metabolism Enhances Sensitivity to Perifosine in Head and Neck Cancer Cells

2009 ◽  
Vol 2009 ◽  
pp. 1-10 ◽  
Author(s):  
Andrean L. Simons ◽  
Arlene D. Parsons ◽  
Katherine A. Foster ◽  
Kevin P. Orcutt ◽  
Melissa A. Fath ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Head And Neck Cancer ◽  
Head And Neck ◽  
Neck Cancer ◽  
Reductase Activity ◽  
Thioredoxin Reductase ◽  
Buthionine Sulfoximine ◽  
Human Head ◽  
Akt Inhibitor ◽  
Simultaneous Treatment

The hypothesis that the Akt inhibitor, perifosine (PER), combined with inhibitors of glutathione (GSH) and thioredoxin (Trx) metabolism will induce cytotoxicity via metabolic oxidative stress in human head and neck cancer (HNSCC) cells was tested. PER induced increases in glutathione disulfide (%GSSG) in FaDu, Cal-27, and SCC-25 HNSCCs as well as causing significant clonogenic cell killing in FaDu and Cal-27, which was suppressed by simultaneous treatment with N-acetylcysteine (NAC). An inhibitor of GSH synthesis, buthionine sulfoximine (BSO), sensitized Cal-27 and SCC-25 cells to PER-induced clonogenic killing as well as decreased total GSH and increased %GSSG. Additionally, inhibition of thioredoxin reductase activity (TrxRed) with auranofin (AUR) was able to induce PER sensitization in SCC-25 cells that were initially refractory to PER. These results support the conclusion that PER induces oxidative stress and clonogenic killing in HNSCC cells that is enhanced with inhibitors of GSH and Trx metabolism.

scholarly journals A direct and continuous assay for the determination of thioredoxin reductase activity in cell lysates

2013 ◽  
Vol 443 (1) ◽  
pp. 34-40 ◽  
Author(s):  
Brian Cunniff ◽  
Gregg W. Snider ◽  
Nicholas Fredette ◽  
Robert J. Hondal ◽  
Nicholas H. Heintz
Keyword(s):  
Reductase Activity ◽  
Thioredoxin Reductase ◽  
Cell Lysates ◽  
Continuous Assay

Recombinant putative glutathione reductase of Plasmodium falciparum exhibits thioredoxin reductase activity

1996 ◽  
Vol 80 (2) ◽  
pp. 215-219 ◽  
Author(s):  
Sylke Müller ◽  
Tim-Wolf Gilberger ◽  
Petra M. Färber ◽  
Katja Becker ◽  
R. Heiner Schirmer ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Glutathione Reductase ◽  
Reductase Activity ◽  
Thioredoxin Reductase

scholarly journals The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex

2003 ◽  
Vol 160 (7) ◽  
pp. 1139-1150 ◽  
Author(s):  
Ryan Ratts ◽  
Huiyan Zeng ◽  
Eric A. Berg ◽  
Clare Blue ◽  
Mark E. McComb ◽  
...  
Keyword(s):  
T Cell ◽  
Diphtheria Toxin ◽  
Essential Role ◽  
Reductase Activity ◽  
Translocation Factor ◽  
Thioredoxin Reductase ◽  
Cell Extracts ◽  
Human T Cell ◽  
Early Endosomes

In vitro delivery of the diphtheria toxin catalytic (C) domain from the lumen of purified early endosomes to the external milieu requires the addition of both ATP and a cytosolic translocation factor (CTF) complex. Using the translocation of C-domain ADP-ribosyltransferase activity across the endosomal membrane as an assay, the CTF complex activity was 650–800-fold purified from human T cell and yeast extracts, respectively. The chaperonin heat shock protein (Hsp) 90 and thioredoxin reductase were identified by mass spectrometry sequencing in CTF complexes purified from both human T cell and yeast. Further analysis of the role played by these two proteins with specific inhibitors, both in the in vitro translocation assay and in intact cell toxicity assays, has demonstrated their essential role in the productive delivery of the C-domain from the lumen of early endosomes to the external milieu. These results confirm and extend earlier observations of diphtheria toxin C-domain unfolding and refolding that must occur before and after vesicle membrane translocation. In addition, results presented here demonstrate that thioredoxin reductase activity plays an essential role in the cytosolic release of the C-domain. Because analogous CTF complexes have been partially purified from mammalian and yeast cell extracts, results presented here suggest a common and fundamental mechanism for C-domain translocation across early endosomal membranes.

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