Protein Information

ID 1206
Name Lactoferrin
Synonyms GIG12; Growth inhibiting protein 12; HLF 2; HLF2; LF; LTF; Lactoferrin; Lactotransferrin…

Compound Information

ID 1388
Name sodium fluoride
CAS sodium fluoride (NaF)

Reference

PubMed Abstract RScore(About this table)
9769245 Tachezy J, Suchan P, Schrevel J, Kulda J: The host-protein-independent iron uptake by Tritrichomonas foetus. Exp Parasitol. 1998 Oct;90(2):155-63.
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.
3(0,0,0,3)