Diferric transferrin reduction stimulates the Na+H+ antiport of HeLa cells

Sun, I. L.; García-Cañero, R.; Liu, W.; Toole-Simms, W.; Crane, F.L.; Morré, D. James; Löw, H.

doi:10.1016/0006-291x(87)91344-1

Cited by 38 publications

(7 citation statements)

References 17 publications

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“…Associated with this redox system is a protonpumping activity directing an efflux of protons from the cell. The proton efflux seems to occur via the plasma membrane Na+/H+ antiport [40,41]. The oxidoreductase readily reduces extracellular ferricyanide and apparently also transferrin-bound iron [37].…”

Section: Thorstensen Unpublished Work)mentioning

confidence: 99%

“…alkalinization of the cytosol through proton extrusion via the Na+/H+ antiport [84], increase in cytosolic free calcium concentration [84], changes in intracellular NAD+/NADH ratio [85] and activation of 'immediate early genes' (e.g. c-myc and c-fos) [86] -may be triggered by stimulation of the NADH:ferricyanide oxidoreductase [40,41,[87][88][89][90].…”

Section: Transferrin and The Regulation Of Cell Growthmentioning

confidence: 99%

“…Finally, transferrin stimulates the redox system and induces proton efflux via the Na+/H+ antiport [40,41,96], whereas some antibodies against the transferrin receptor inhibit the redox system [97]. Thus, variations in the cell's Vol.…”

Section: Transferrin and The Regulation Of Cell Growthmentioning

confidence: 99%

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The role of transferrin in the mechanism of cellular iron uptake

Thorstensen

Romslo

1990

Biochemical Journal

187

106

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INTRODUCTIONThe role of transferrin and its cell surface receptor in cellular iron metabolism has received considerable interest during the last decade. Hence, over this period several reviews covering various aspects of the topic have been published.In this review we attempt to summarize the new knowledge and controversies encountered during the last 4-5 years. The focus is on iron metabolism by the hepatocyte. We also view the concept of transferrin-cell interactions from angles which previously may not have been given particular attention, and we include some aspects of iron metabolism not normally covered by reviews of this type. Central parts of what may be regarded as well-established knowledge either have been entirely omitted, or are only briefly described or mentioned to the extent considered relevant to the particular topic discussed. Important aspects of iron metabolism such as iron adsorption, haemochromatosis, ferritin iron and iron in infection and neoplasia are not covered in the present paper. Instead, the reader is referred to one or more of the recently published reviews [1-5] and references therein.

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Section: Thorstensen Unpublished Work)mentioning

confidence: 99%

Section: Transferrin and The Regulation Of Cell Growthmentioning

confidence: 99%

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The role of transferrin in the mechanism of cellular iron uptake

Thorstensen

Romslo

1990

Biochemical Journal

187

106

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“…Nevertheless, in these studies as well as others (Egyed, 1988;Morgan, 1988;Sturrock, et al, 1990) iron has been demonstrated to cross the plasma membrane. Acidification of the microenvironment at the hepatocyte surface may be required as well but may be mediated through a Na+/H + exchanger (Sun et al, 1987a). The processes in these systems are similar in that iron crosses the membrane to gain access to the cytosol.…”

Section: Discussionmentioning

confidence: 97%

Kinetics of iron passage through subcellular compartments of rabbit reticulocytes

et al. 1991

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The kinetics of the separate processes of Fe2(III)-transferrin binding to the transferrin receptor, transferrin-receptor internalization, iron dissociation from transferrin, iron passage through the membrane, and iron mobilization into the cytoplasm were studied by pulse-chase experiments using rabbit reticulocytes and 59Fe, 125I-labeled rabbit transferrin. The binding of 59Fe-transferrin to transferrin receptors was rapid with an apparent rate constant of 2 x 10(5) M-1 sec-1. The rate of internalization of 59Fe-transferrin was directly measured at 520 +/- 100 molecules of Fe2(III)-transferrin internalized/sec/cell with 250 +/- 43 sec needed to internalize the entire complement of reticulocyte transferrin receptors. Subsequent to Fe2(III)-transferrin internalization the flux of 59Fe was followed through three compartments: internalized transferrin, membrane, and cytosol. A process preceding iron dissociation from transferrin and a reaction involving membrane-associated iron required 17 +/- 2 sec and 34 +/- 5 sec, respectively. Apparent rate constants of 0.0075 +/- 0.002 sec-1 and 0.0343 +/- 0.0118 sec-1 were obtained for iron dissociation from transferrin and iron mobilization into the cytosol, respectively. Iron dissociation from transferrin is the rate-limiting step. An apparent rate constant of 0.0112 +/- 0.0025 sec-1 was obtained for processes involving iron transport through the membrane although at least two reactions are likely to be involved. Based on mechanistic considerations, iron transport through the membrane may be attributed to an iron reduction step followed by a translocation step. These data indicate that the uptake of iron in reticulocytes is a sequential process, with steps after the internalization of Fe2(III)-transferrin that are distinct from the handling of transferrin.

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“…In hepatocytes, ferricyanide is a distinct inhibitor of iron uptake, while it is without any effect in reticulocytes [16, 171. Amiloride inhibited iron release as well as iron uptake, although to a far lesser extent (Table 1). Uptake inhibition may be due to unspecific effects of this inhibitor due to uptake by the cells [40], but protonization of transferrin by sodiumproton exchange may be necessary for efficient reduction of transferrin iron at the plasma membrane [41]. Amiloride has been shown to inhibit transferrin endocytosis and iron uptake in reticulocytes, albeit at much higher concentrations [42].…”

Section: Discussionmentioning

confidence: 99%

Plasma membrane Fe₂‐transferrin reductase and iron uptake in K562 cells are not directly related

Goldenberg

Dodel

Seidl

1990

European Journal of Biochemistry

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Receptor‐mediated endocytosis and recycling of transferrin is partly inhibited by the ferrous iron chelator bipyridine, which almost completely blocks iron uptake. Bipyridine causes iron release at the cell surface, but inhibition of iron uptake is also due to a blockage of its passage through the endosomal membrane. The rate of release of iron to bipyridine is decreased by the competing electron acceptor ferricyanide and by amiloride, but not by iron uptake inhibiting acidotropic amines. Transferrin reduction at the plasma membrane may be artificially induced by presence of a ferrous chelator and caused by low‐affinity transmembrane NAD(P)H oxidoreductase.

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Diferric transferrin reduction stimulates the Na+H+ antiport of HeLa cells

Cited by 38 publications

References 17 publications

The role of transferrin in the mechanism of cellular iron uptake

The role of transferrin in the mechanism of cellular iron uptake

Kinetics of iron passage through subcellular compartments of rabbit reticulocytes

Plasma membrane Fe₂‐transferrin reductase and iron uptake in K562 cells are not directly related

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Diferric transferrin reduction stimulates the Na+H+ antiport of HeLa cells

Cited by 38 publications

References 17 publications

The role of transferrin in the mechanism of cellular iron uptake

The role of transferrin in the mechanism of cellular iron uptake

Kinetics of iron passage through subcellular compartments of rabbit reticulocytes

Plasma membrane Fe2‐transferrin reductase and iron uptake in K562 cells are not directly related

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Product

Resources

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Plasma membrane Fe₂‐transferrin reductase and iron uptake in K562 cells are not directly related