Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi
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Wilkinson, Shane R., Temperton, Nigel J., Mondragon, Angeles and Kelly, John M. (2000) Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi. The Journal of Biological Chemistry, 275 (11). pp. 8220-8225. ISSN 0021-9258 (print), 1083-351X (on-line)
Full text not available from this repository.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.
| Item Type: | Article |
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| Additional Information: | [1] This article is free access [2] The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AJ006226 (TcMPX) and AJ012101 (TcCPX). |
| Uncontrolled Keywords: | proteins, T. cruzi, peroxide-mediated damage, enzyme activity, cytoplasmic peroxiredoxin, mitochondrial peroxiredoxin |
| Subjects: | Q Science > QH Natural history > QH301 Biology R Medicine > RC Internal medicine |
| School / Department / Research Groups: | Medway School of Pharmacy |
| Related URLs: | |
| Last Modified: | 16 Jul 2012 14:54 |
| URI: | http://gala.gre.ac.uk/id/eprint/8569 |
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