The host-protein-independent iron uptake by Tritrichomonas foetus
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
9769245
DOI
10.1006/expr.1998.4327
PII: S0014-4894(98)94327-2
Knihovny.cz E-resources
- MeSH
- Amiloride pharmacology MeSH
- Antiprotozoal Agents pharmacology MeSH
- Iron Chelating Agents metabolism pharmacology MeSH
- Ammonium Chloride pharmacology MeSH
- Chloroquine pharmacology MeSH
- Sodium Fluoride pharmacology MeSH
- Ascorbic Acid pharmacology MeSH
- Nitrilotriacetic Acid analogs & derivatives metabolism MeSH
- Lactoferrin metabolism MeSH
- Oxidation-Reduction MeSH
- Cattle MeSH
- Transferrin metabolism MeSH
- Tritrichomonas foetus metabolism MeSH
- Ferric Compounds metabolism MeSH
- Iron metabolism MeSH
- Animals MeSH
- Check Tag
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Amiloride MeSH
- Antiprotozoal Agents MeSH
- Iron Chelating Agents MeSH
- Ammonium Chloride MeSH
- Chloroquine MeSH
- ferric nitrilotriacetate MeSH Browser
- Sodium Fluoride MeSH
- Ascorbic Acid MeSH
- Nitrilotriacetic Acid MeSH
- Lactoferrin MeSH
- Transferrin MeSH
- Ferric Compounds MeSH
- Iron MeSH
Iron uptake from a low-molecular-weight chelate Fe(III)-nitriloacetate (Fe-NTA) by anaerobic protozoan parasite Tritrichomonas foetus was investigated and compared with that from iron-saturated lactoferrin and transferrin. The results showed that the iron uptake from Fe-NTA was saturable (Km = 2.7 microM, Vmax = 21.7 fmol. microg-1.min-1) and time, and temperature dependent, thus suggesting involvement of a membrane transport carrier. The accumulation of iron from 59Fe-NTA was inhibited by NaF and iron chelators. Amilorid and inhibitors of endosome acidification did not influence the process. Ascorbate stimulated the uptake while a membrane impermeable chelator of bivalent iron (bathophenanthroline disulfonic acid) was inhibitory, suggesting that prior to transport iron is reduced extracellularly. In accord with this assumption, the reduction of ferric to ferrous iron in the presence of intact T. foetus cells was demonstrated. Dynamics and properties of uptake of iron released from transferrin were similar to those from Fe-NTA, indicating involvement of common mechanisms. Iron uptake from lactoferrin displayed profoundly different characteristics consistent with receptor-mediated endocytosis. Metronidazole-resistant derivative of the investigated T. foetus strain showed marked deficiency in iron acquisition from Fe-NTA and transferrin while its iron uptake from lactoferrin was higher than that of the parent strain. The results presented show that T. foetus possesses at least two independent mechanisms that mediate acquisition of iron.
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