Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0024530 (malaria)
 44,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Chloroquine is a weak base which has been shown to inhibit lysosomal acidification. Chloroquine inhibits iron uptake in reticulocytes at a concentration of 0.5 mM. It is also effective in the control of malaria and other parasitic diseases. We now report that chloroquine inhibits NADH diferric transferrin reductase as well as the proton release stimulated by diferric transferrin from liver and HeLa cells. Ammonium chloride which also inhibits endosome acidification does not significantly inhibit the NADH diferric transferrin reduction. NADH diferric transferrin reductase of isolated rat liver plasma membrane is inhibited by chloroquine at concentrations similar to those required for inhibition of diferric transferrin reduction by whole cells. Ferricyanide reduction by whole cells is also inhibited by chloroquine. These observations provide an alternative mechanism for chloroquine control of acidification of endosomes and suggests a new approach to control of protozoal parasites through inhibition of a transmembrane oxidoreductase which controls transmembrane proton movement.
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PMID:Transplasma membrane electron and proton transport is inhibited by chloroquine. 217 87

Diferric transferrin reductase, assayed by formation of ferrous - bathophenanthroline, is detectable in the plasmamembrane of intact mature erythrocytes infected with Plasmodium falciparum. The absence of this transmembrane redox system in uninfected mature erythrocytes suggests its synthesis and incorporation by the intraerythrocytic parasite. The presence of diferric transferrin reductase, together with parasite-derived transferrin-receptor in the erythrocyte membrane, suggests a transferrin receptor-mediated uptake of iron by the malaria parasite.
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PMID:Diferric transferrin reductase in Plasmodium falciparum-infected erythrocytes. 264 31