Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi.
J Biol Chem
; 275(11): 8220-5, 2000 Mar 17.
Article
en En
| MEDLINE
| ID: mdl-10713147
ABSTRACT
The American trypanosome Trypanosoma cruzi is exposed to toxic oxygen metabolites that are generated by drug metabolism and immune responses in addition to those produced by endogenous processes. However, much remains to be resolved about the parasite oxidative defense system, including the mechanism(s) of peroxide reduction. Here we show that reduction of peroxides in T. cruzi is catalyzed by two distinct trypanothione-dependent enzymes. These were localized to the cytosol and mitochondrion. Both are members of the peroxiredoxin family of antioxidant proteins and are characterized by the presence of two conserved domains containing redox active cysteines. The role of these proteins in protecting T. cruzi from peroxide-mediated damage was demonstrated following overexpression of enzyme activity. The parasite-specific features of T. cruzi cytoplasmic peroxiredoxin and T. cruzi mitochondrial peroxiredoxin may be exploitable in terms of drug development.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Peroxidasas
/
Trypanosoma cruzi
/
Espermidina
/
Citosol
/
Glutatión
/
Mitocondrias
Límite:
Animals
Idioma:
En
Revista:
J Biol Chem
Año:
2000
Tipo del documento:
Article