scholarly journals Detection of Anti-Trypanosoma Cruzi Antibodies among Donors at A Blood Bank from Southern Mexico, Using an Iron Superoxide Dismutase Excreted (Fe-Sode) as Antigen

2017 ◽  
Author(s):  
Concha-Valdez F ◽  
Marín C ◽  
Cañas-Ruíz R ◽  
Sosa-Matú C ◽  
Escobedo-Ortegón J ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Trypanosoma Cruzi ◽  
Blood Bank ◽  
Southern Mexico ◽  
Iron Superoxide Dismutase

Efficient Inhibition of Iron Superoxide Dismutase and of Trypanosoma cruzi Growth by Benzo[g]phthalazine Derivatives Functionalized with One or Two Imidazole Rings

2008 ◽  
Vol 51 (6) ◽  
pp. 1962-1966 ◽  
Author(s):  
Ana M. Sanz ◽  
Fernando Gómez-Contreras ◽  
Pilar Navarro ◽  
Manuel Sánchez-Moreno ◽  
Samira Boutaleb-Charki ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Trypanosoma Cruzi ◽  
Iron Superoxide Dismutase

scholarly journals An in vitro iron superoxide dismutase inhibitor decreases the parasitemia levels of Trypanosoma cruzi in BALB/c mouse model during acute phase

2015 ◽  
Vol 5 (3) ◽  
pp. 110-116 ◽  
Author(s):  
Francisco Olmo ◽  
Kristína Urbanová ◽  
Maria Jose Rosales ◽  
Ruben Martín-Escolano ◽  
Manuel Sánchez-Moreno ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Mouse Model ◽  
Trypanosoma Cruzi ◽  
Acute Phase ◽  
Iron Superoxide Dismutase

scholarly journals Mitochondrial superoxide radicals mediate programmed cell death in Trypanosoma cruzi: cytoprotective action of mitochondrial iron superoxide dismutase overexpression

2007 ◽  
Vol 403 (2) ◽  
pp. 323-334 ◽  
Author(s):  
Lucía Piacenza ◽  
Florencia Irigoín ◽  
María Noel Alvarez ◽  
Gonzalo Peluffo ◽  
Martin C. Taylor ◽  
...  
Keyword(s):  
Cell Death ◽  
Superoxide Dismutase ◽  
Programmed Cell Death ◽  
Trypanosoma Cruzi ◽  
Early Period ◽  
Pentose Phosphate ◽  
Iron Superoxide Dismutase ◽  
Mitochondrial Superoxide ◽  
Glucose Flux ◽  
Mitochondrial Aconitase

Trypanosoma cruzi undergo PCD (programmed cell death) under appropriate stimuli, the mechanisms of which remain to be established. In the present study, we show that stimulation of PCD in T. cruzi epimastigotes by FHS (fresh human serum) results in rapid (<1 h) externalization of phosphatidylserine and depletion of the low molecular mass thiols dihydrotrypanothione and glutathione. Concomitantly, enhanced generation of oxidants was established by EPR and immuno-spin trapping of radicals using DMPO (5,5-dimethylpyrroline-N-oxide) and augmentation of the glucose flux through the pentose phosphate pathway. In the early period (<20 min), changes in mitochondrial membrane potential and inhibition of respiration, probably due to the impairment of ADP/ATP exchange with the cytosol, were observed, conditions that favour the generation of O2•−. Accelerated rates of mitochondrial O2•− production were detected by the inactivation of the redox-sensitive mitochondrial aconitase and by oxidation of a mitochondrial-targeted probe (MitoSOX). Importantly, parasites overexpressing mitochondrial FeSOD (iron superoxide dismutase) were more resistant to the PCD stimulus, unambiguously indicating the participation of mitochondrial O2•− in the signalling process. In summary, FHS-induced PCD in T. cruzi involves mitochondrial dysfunction that causes enhanced O2•− formation, which leads to cellular oxidative stress conditions that trigger the initiation of PCD cascades; moreover, overexpression of mitochondrial FeSOD, which is also observed during metacyclogenesis, resulted in cytoprotective effects.

Synthetic single and double aza-scorpiand macrocycles acting as inhibitors of the antioxidant enzymes iron superoxide dismutase and trypanothione reductase in Trypanosoma cruzi with promising results in a murine model

RSC Advances ◽  
2014 ◽  
Vol 4 (110) ◽  
pp. 65108-65120 ◽  
Author(s):  
F. Olmo ◽  
M. P. Clares ◽  
C. Marín ◽  
J. González ◽  
M. Inclán ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Antioxidant Enzymes ◽  
Survival Rate ◽  
Trypanosoma Cruzi ◽  
Murine Model ◽  
Trypanothione Reductase ◽  
Iron Superoxide Dismutase

Synthetic scorpiand-like azamacrocycles selectively inhibit SOD and TR enzymes of Trypanosoma cruzi in mice causing death of the parasites and increasing the mouse survival rate after infection and treatment.

Effect of Hubs in Amino Acid Network on Iron Superoxide Dismutase Stability

2015 ◽  
Vol 10 (2) ◽  
pp. 232-239
Author(s):  
Yanrui Ding ◽  
Xueqin Wang ◽  
Zhaolin Mou
Keyword(s):  
Superoxide Dismutase ◽  
Amino Acid ◽  
Iron Superoxide Dismutase

The iron content of iron superoxide dismutase: determination by anomalous scattering

1983 ◽  
Vol 218 (1210) ◽  
pp. 119-126 ◽  
Keyword(s):  
Superoxide Dismutase ◽  
Iron Content ◽  
Three Dimensional ◽  
Anomalous Scattering ◽  
Total Iron Content ◽  
Iron Site ◽  
Iron Superoxide Dismutase ◽  
Density Map ◽  
The Difference ◽  
Electron Density Map

The number of iron atoms in the dimeric iron-containing superoxide dismutase from Pseudomonas ovalis and their atomic positions have been determined directly from anomalous scattering measurements on crystals of the native enzyme. To resolve the long-standing question of the total amount of iron per molecule for this class of dismutase, the occupancy of each site was refined against the measured Bijvoet differences. The enzyme is a symmetrical dimer with one iron site in each subunit. The iron position is 9 ņ from the intersubunit interface. The total iron content of the dimer is 1.2±0.2 moles per mole of protein. This is divided between the subunits in the ratio 0.65:0.55; the difference between them is probably not significant. Since each subunit contains, on average, slightly more than half an iron atom we conclude that the normal state of this enzyme is two iron atoms per dimer but that some of the metal is lost during purification of the protein. Although the crystals are obviously a mixture of holo- and apo-enzymes, the 2.9 Å electron density map is uniformly clean, even at the iron site. We conclude that the three-dimensional structures of the iron-bound enzyme and the apoenzyme are identical.

scholarly journals A tetrameric iron superoxide dismutase from the eucaryote Tetrahymena pyriformis.

1990 ◽  
Vol 265 (29) ◽  
pp. 17680-17687
Author(s):  
D Barra ◽  
M E Schininà ◽  
F Bossa ◽  
K Puget ◽  
P Durosay ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Tetrahymena Pyriformis ◽  
Iron Superoxide Dismutase
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