Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targets
Membrane glutathione S-transferases from the class of membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG) form a superfamily of detoxification enzymes that catalyze the conjugation of reduced glutathione (GSH) to a broad spectrum of xenobiotics and hydrophobic electrophiles...
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Shared Science Publishers OG
2014-10-01
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| Series: | Microbial Cell |
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| Online Access: | http://microbialcell.com/researcharticles/plasmodium-spp-membrane-glutathione-s-transferases-detoxification-units-and-drug-targets/ |
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| author | Andreas Martin Lisewski |
| author_facet | Andreas Martin Lisewski |
| author_sort | Andreas Martin Lisewski |
| collection | DOAJ |
| description | Membrane glutathione S-transferases from the class of membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG) form a superfamily of detoxification enzymes that catalyze the conjugation of reduced glutathione (GSH) to a broad spectrum of xenobiotics and hydrophobic electrophiles. Evolutionarily unrelated to the cytosolic glutathione S-transferases, they are found across bacterial and eukaryotic domains, for example in mammals, plants, fungi and bacteria in which significant levels of glutathione are maintained. Species of genus Plasmodium, the unicellular protozoa that are commonly known as malaria parasites, do actively support glutathione homeostasis and maintain its metabolism throughout their complex parasitic life cycle. In humans and in other mammals, the asexual intraerythrocytic stage of malaria, when the parasite feeds on hemoglobin, grows and eventually asexually replicates inside infected red blood cells (RBCs), is directly associated with host disease symptoms and during this critical stage GSH protects the host RBC and the parasite against oxidative stress from parasite-induced hemoglobin catabolism. In line with these observations, several GSH-dependent Plasmodium enzymes have been characterized including glutathione reductases, thioredoxins, glyoxalases, glutaredoxins and glutathione S-transferases (GSTs); furthermore, GSH itself have been found to associate spontaneously and to degrade free heme and its hydroxide, hematin, which are the main cytotoxic byproducts of hemoglobin catabolism. However, despite the apparent importance of glutathione metabolism for the parasite, no membrane associated glutathione S-transferases of genus Plasmodium have been previously described. We recently reported the first examples of MAPEG members among Plasmodium spp. |
| format | Article |
| id | doaj-art-de7b335a2e38426a83aa49921d2ce66f |
| institution | DOAJ |
| issn | 2311-2638 |
| language | English |
| publishDate | 2014-10-01 |
| publisher | Shared Science Publishers OG |
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| series | Microbial Cell |
| spelling | doaj-art-de7b335a2e38426a83aa49921d2ce66f2025-08-20T02:57:39ZengShared Science Publishers OGMicrobial Cell2311-26382014-10-0111138738910.15698/mic2014.11.177Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targetsAndreas Martin Lisewski0Department of Molecular and Human Genetics, Computational and Integrative Biomedical Research Center, Baylor College of Medicine, Houston, TX 77030, USA.Membrane glutathione S-transferases from the class of membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG) form a superfamily of detoxification enzymes that catalyze the conjugation of reduced glutathione (GSH) to a broad spectrum of xenobiotics and hydrophobic electrophiles. Evolutionarily unrelated to the cytosolic glutathione S-transferases, they are found across bacterial and eukaryotic domains, for example in mammals, plants, fungi and bacteria in which significant levels of glutathione are maintained. Species of genus Plasmodium, the unicellular protozoa that are commonly known as malaria parasites, do actively support glutathione homeostasis and maintain its metabolism throughout their complex parasitic life cycle. In humans and in other mammals, the asexual intraerythrocytic stage of malaria, when the parasite feeds on hemoglobin, grows and eventually asexually replicates inside infected red blood cells (RBCs), is directly associated with host disease symptoms and during this critical stage GSH protects the host RBC and the parasite against oxidative stress from parasite-induced hemoglobin catabolism. In line with these observations, several GSH-dependent Plasmodium enzymes have been characterized including glutathione reductases, thioredoxins, glyoxalases, glutaredoxins and glutathione S-transferases (GSTs); furthermore, GSH itself have been found to associate spontaneously and to degrade free heme and its hydroxide, hematin, which are the main cytotoxic byproducts of hemoglobin catabolism. However, despite the apparent importance of glutathione metabolism for the parasite, no membrane associated glutathione S-transferases of genus Plasmodium have been previously described. We recently reported the first examples of MAPEG members among Plasmodium spp.http://microbialcell.com/researcharticles/plasmodium-spp-membrane-glutathione-s-transferases-detoxification-units-and-drug-targets/Plasmodiummalariadetoxificationglutathioneartemisinin |
| spellingShingle | Andreas Martin Lisewski Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targets Microbial Cell Plasmodium malaria detoxification glutathione artemisinin |
| title | Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targets |
| title_full | Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targets |
| title_fullStr | Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targets |
| title_full_unstemmed | Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targets |
| title_short | Plasmodium spp. membrane glutathione S-transferases: detoxification units and drug targets |
| title_sort | plasmodium spp membrane glutathione s transferases detoxification units and drug targets |
| topic | Plasmodium malaria detoxification glutathione artemisinin |
| url | http://microbialcell.com/researcharticles/plasmodium-spp-membrane-glutathione-s-transferases-detoxification-units-and-drug-targets/ |
| work_keys_str_mv | AT andreasmartinlisewski plasmodiumsppmembraneglutathionestransferasesdetoxificationunitsanddrugtargets |