Transferrin and iron distribution in subcellular fractions of K562 cells in the early stages of transferrin endocytosis

Vyoral, Daniel; Hradilek, A; Neuwirt, J

doi:10.1016/0167-4889(92)90196-i

Cited by 30 publications

(10 citation statements)

References 28 publications

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“…It has been suggested that the 'mobile' iron forms lowmolecular-mass complexes with nucleotides, nucleic acids, polyphosphates, amino acids, citrate or peptides (Jacobs, 1977;Bohnke & Matzanke, 1995;Weaver & Pollack, 1989). However, increasing evidence indicates that 'mobile' iron is (with low affinity) bound to compounds most likely to be proteins with a molecular mass greater than 20 000 Da (Petrák & Vyoral, 2001;Vyoral & Petrák, 1998a, b;Vyoral et al, 1992). This view is supported by our results using ultrafiltration of iron-labelled cytosol of Tt.…”

Section: Discussionmentioning

confidence: 99%

Incorporation of iron into Tritrichomonas foetus cell compartments reveals ferredoxin as a major iron-binding protein in hydrogenosomes

et al. 2003

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The intracellular transport of iron and its incorporation into organelles are poorly understood processes in eukaryotes and virtually unknown in parasitic protists. The transport of iron is of particular interest in trichomonads, which possess hydrogenosomes instead of mitochondria. The metabolic functions of hydrogenosomes, which contain a specific set of FeS proteins, entirely depend on iron acquisition. In this work the incorporation of iron into the cattle parasite Tritrichomonas foetus was monitored. Iron was efficiently taken up from 59Fe-nitrilotriacetic acid and accumulated in the cytosol (88·9 %) and hydrogenosomes (4·7 % of the total radioactivity). Using atomic absorption spectrophotometry, an unusually high steady-state iron concentration in hydrogenosomes was determined [54·4±1·1 nmol Fe (mg protein)−1]. The concentration of iron in the cytosol was 13·4±0·5 nmol Fe (mg protein)−1. Qualitative analysis of incorporated iron was performed using native gradient PAGE. The majority of the 59Fe in the cytosol appeared as the labile-iron pool, which represents weakly bound iron associated with compounds of molecular mass ranging from 5000 to 30 000 Da. Ferritin was not observed in Tt. foetus, nor in two other anaerobic protists, Entamoeba histolytica and Giardia intestinalis. Analysis of Tt. foetus hydrogenosomes showed at least nine iron-binding compounds, which were absent in metronidazole-resistant mutants. The major iron-binding compound was identified as [2Fe–2S] ferredoxin of the adrenodoxin type.

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Section: Discussionmentioning

confidence: 99%

Incorporation of iron into Tritrichomonas foetus cell compartments reveals ferredoxin as a major iron-binding protein in hydrogenosomes

et al. 2003

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“…As yet, such iron chaperone molecules remain elusive, although Vyoral et al (31) identified a high M r intermediate that appeared to donate its iron to ferritin after incubation of K562 cells with Tf. More recently, a protein known as poly (rC)-binding protein 1 has been identified that donates iron to ferritin and may play an important role in this process (32).…”

Section: Regulation Of Cellular Iron Homeostasismentioning

confidence: 99%

Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol

Richardson

Lane

Becker

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

436

383

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The mitochondrion is well known for its key role in energy transduction. However, it is less well appreciated that it is also a focal point of iron metabolism. Iron is needed not only for heme and iron sulfur cluster (ISC)-containing proteins involved in electron transport and oxidative phosphorylation, but also for a wide variety of cytoplasmic and nuclear functions, including DNA synthesis. The mitochondrial pathways involved in the generation of both heme and ISCs have been characterized to some extent. However, little is known concerning the regulation of iron uptake by the mitochondrion and how this is coordinated with iron metabolism in the cytosol and other organelles (e.g., lysosomes). In this article, we discuss the burgeoning field of mitochondrial iron metabolism and trafficking that has recently been stimulated by the discovery of proteins involved in mitochondrial iron storage (mitochondrial ferritin) and transport (mitoferrin-1 and -2). In addition, recent work examining mitochondrial diseases (e.g., Friedreich's ataxia) has established that communication exists between iron metabolism in the mitochondrion and the cytosol. This finding has revealed the ability of the mitochondrion to modulate whole-cell ironprocessing to satisfy its own requirements for the crucial processes of heme and ISC synthesis. Knowledge of mitochondrial ironprocessing pathways and the interaction between organelles and the cytosol could revolutionize the investigation of iron metabolism.iron sulfur cluster | heme | Friedreich's ataxia | frataxin | sideroblastic anemia

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“…Although the identity of LIP substituents remains elusive, it has been suggested that iron in this pool is bound to amino acids, nucleotides, and sugars (Jacobs, 1977). However, little low molecular weight iron is present within cells, suggesting that such a pool must exist in very low concentrations or may not be present (Vyoral et al, 1992;Richardson et al, 1996). In fact, several models of intracellular iron transport have been proposed that do not involve the presence of low molecular weight species of iron (Zhang et al, 2005).…”

Section: The Labile Iron Pool and Iron Storagementioning

confidence: 99%

The Evolution of Iron Chelators for the Treatment of Iron Overload Disease and Cancer

2005

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Transferrin and iron distribution in subcellular fractions of K562 cells in the early stages of transferrin endocytosis

Cited by 30 publications

References 28 publications

Incorporation of iron into Tritrichomonas foetus cell compartments reveals ferredoxin as a major iron-binding protein in hydrogenosomes

Incorporation of iron into Tritrichomonas foetus cell compartments reveals ferredoxin as a major iron-binding protein in hydrogenosomes

Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol

The Evolution of Iron Chelators for the Treatment of Iron Overload Disease and Cancer

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