Glutathione Reductase and Thioredoxin Reductase: Novel Antioxidant Enzymes from Plasmodium berghei.
10.3347/kjp.2009.47.4.421
- Author:
Gaurav KAPOOR
1
;
Harjeet Singh BANYAL
Author Information
1. Laboratory of Parasitology and Immunology, Department of Biosciences, Himachal Pradesh University, Shimla 171005, India. hsbanyal@yahoo.co.in
- Publication Type:Brief Communication ; Research Support, Non-U.S. Gov't
- Keywords:
Plasmodium berghei;
glutathione reductase;
thioredoxin reductase;
antioxidant;
antibiotics
- MeSH:
Animals;
Antioxidants/*isolation & purification/*metabolism;
Cell Fractionation;
Cytosol/enzymology;
Erythrocytes/parasitology;
Glutathione Reductase/*isolation & purification/*metabolism;
Mice;
Plasmodium berghei/*enzymology;
Thioredoxin-Disulfide Reductase/*isolation & purification/*metabolism
- From:The Korean Journal of Parasitology
2009;47(4):421-424
- CountryRepublic of Korea
- Language:English
-
Abstract:
Malaria parasites adapt to the oxidative stress during their erythrocytic stages with the help of vital thioredoxin redox system and glutathione redox system. Glutathione reductase and thioredoxin reductase are important enzymes of these redox systems that help parasites to maintain an adequate intracellular redox environment. In the present study, activities of glutathione reductase and thioredoxin reductase were investigated in normal and Plasmodium berghei-infected mice red blood cells and their fractions. Activities of glutathione reductase and thioredoxin reductase in P. berghei-infected host erythrocytes were found to be higher than those in normal host cells. These enzymes were mainly confined to the cytosolic part of cell-free P. berghei. Full characterization and understanding of these enzymes may promise advances in chemotherapy of malaria.
