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Regulation of the transferrin-independent iron transport system in cultured cells.
Open accessAbstract
Mammalian cells accumulate iron via the binding of transferrin to high affinity surface receptors, or through a transferrin-independent pathway which involves the uptake of iron-organic anion chelates by a membrane-based transport system. Previously we determined that the transferrin-independent transport system was present on a wide variety of cultured cells (Sturrock, A., Alexander, J., Lamb, J., Craven, C. M., and Kaplan, J. (1990) J. Biol. Chem. 265, 3139-3145). In this communication we demonstrate that the transferrin-independent iron uptake system is regulated differently than the transferrin-mediated pathway. The activity of the transferrin-independent system was unaffected by changes in cellular growth rate, induction of DNA synthesis and cell division, or depletion of cellular iron. Exposure of cells to ferric or ferrous iron, however, resulted in a time-dependent increase in transport activity, due to a change in Vmax with no change in Km. Increased transport activity was seen in a variety of cultured cell types, occurred in the presence of cycloheximide, and persisted for hours after removal of iron. The ability of other transition metals to induce changes in transport, or to compete with iron for accumulation by the transferrin-independent uptake system, was critically dependent on the composition of the media in which the cells were incubated. Metals such as Cu2+ or Zn2+, but not Cd2+ or Mn2+, when dissolved in a balanced salt solution buffered with 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid, induced changes in the transferrin-independent iron transport system. The same metals which induced changes in transport were ineffective in media containing amino acids, ascorbate, or N-[2-hydroxy-1,1-bis(hydroxymethyl)ethyl]glycine. The Vmax of the transferrin-independent iron transport system was also elevated by increases in intracellular Ca2+. The effect of iron on transport activity, however, did not result from an iron-induced release of intracellular Ca2+. These results suggest a novel form of regulation in which the presence of extracellular iron induces the appearance of previously cryptic transporters and thus accelerates the clearance of potentially toxic molecules.
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“Studies of non-transferrin bound iron uptake by cultured cells support this conclusion.”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [69]
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“In this scenario, iron would be directly taken up by cells in a manner that is independent of Tf, and the “free” iron would be quite redox active (Kaplan et al. , 1991).”
Role of the clathrin adaptor PICALM in normal hematopoiesis and polycythemia vera pathophysiology
Ishikawa, Y., Maeda, M., Pasham, M. R., Aguet, F., Tacheva-Grigorova, S. K., Masuda, T., Yi, H. F., Lee, S.-U., Xu, J., Teruya‐Feldstein, J., et al. (2014) · Haematologica · doi:10.3324/haematol.2014.119537 · Cited by 44
“Ferric ammonium citrate incorporates into cells through “TfR-independent” mechanisms.(24) Importantly, treatment with ferric ammonium citrate dose-dependently restored development of Picalmdeficient mature erythroblasts (Figure 6G), indicating that lack of TfR-mediated iron uptake is the primary cause of erythroid def…”
Oshiro, S., Kawamura, K., Zhang, C., Sone, T., Morioka, M. S., Kobayashi, S., & Nakajima, K. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.12.002 · Cited by 44
Lane, D. J. R., Bae, D.-H., Siafakas, A. R., Rahmanto, Y. S., Al-Akra, L., Jansson, P. J., Casero, R. A., & Richardson, D. R. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.05.007 · Cited by 41
“Cells were incubated with control medium, or this medium containing the well-characterized iron chelators, 311 (25 μM), or DFO (100 μM) [15, 16, 29, 40], or the cellular iron donor, FAC (100 μg/mL) [46, 56, 57]), for 24 or 48 h/37°C (Figs.”
BackgroundDifferential accumulation of non-transferrin-bound iron by cardiac myocytes and fibroblasts
Liu, Y. (2003) · Journal of Molecular and Cellular Cardiology · doi:10.1016/s0022-2828(03)00072-5 · Cited by 42
Characterization of Fe2+ and Fe3+ transport by iron-loaded cardiac myocytes
Parkes, J. G. (1997) · Toxicology · doi:10.1016/s0300-483x(96)03566-4 · Cited by 43
Regulation of Oxidant Production in Acute Lung Injury
Sanders, K. A., Huecksteadt, T. P., Xu, P., Sturrock, A., & Hoidal, J. R. (1999) · CHEST Journal · doi:10.1378/chest.116.suppl_1.56s · Cited by 41
Oshiro, S., Kawahara, M., Mika, S. S., Muramoto, K., Kobayashi, K., Ishige, R., Nozawa, K., Hori, M., Yung, C., Kitajima, S., et al. (1998) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a021914 · Cited by 41
“is observed in human skin fibroblasts (3).”
BackgroundOshiro, S., Nakajima, H., Markello, T. C., Krasnewich, D. M., Bernardini, I. M., & Gahl, W. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80581-x · Cited by 41
Sánchez‐López, R., & Haldar, K. (1992) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(92)90122-z · Cited by 40
Intracellular and Extracellular Labile Iron Pools
Cabantchik, Z. I., Kakhlon, O., Epsztejn, S., Zanninelli, G., & Breuer, W. V. (2002) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0593-8_4 · Cited by 39
Influence of Copper Depletion on Iron Uptake Mediated by SFT, a Stimulator of Fe Transport
Yu, J., & Wessling‐Resnick, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.6909 · Cited by 38
Transferrin receptor expression in myelin deficient (md)rats
Roskams, A. J., & Connor, J. R. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490310304 · Cited by 39
Chaudhary, A., & Poonia, K. (2021) · Inorganic Chemistry Communications · doi:10.1016/j.inoche.2021.109044 · Cited by 40
The role of iron and iron binding proteins in lymphocyte physiology and pathology
Kemp, J. D. (1993) · Journal of Clinical Immunology · doi:10.1007/bf00919264 · Cited by 37
Ghio, A. J., Soukup, J. M., Dailey, L. A., & Madden, M. C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.007 · Cited by 39
Characterisation of citrate and iron citrate uptake by cultured rat hepatocytes
Graham, R. M., Morgan, E. H., & Baker, E. (1998) · Journal of Hepatology · doi:10.1016/s0168-8278(98)80156-6 · Cited by 36
Aluminum exposure affects transferrin-dependent and -independent iron uptake by K562 cells
Pérez, G., Pregi, N., Vittori, D. C., Risio, C. D., Garbossa, G., & Nesse, A. B. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.12.002 · Cited by 35
“The mechanisms that can be proposed to explain NTBI uptake modulation in response to Al exposure may involve the appearance of previously cryptic carriers [10] or the increase in the synthesis of transport proteins since Al proved to be able to translocate into the nucleus and interact with genetic material [29,30].”
BackgroundEtiologies, Consequences, and Treatment of Iron Overload
Gordeuk, V. R., McLaren, G. D., Samowitz, W. S., & Rouault, T. A. (1994) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408369409084674 · Cited by 35
Brown, J. X., Buckett, P. D., & Wessling‐Resnick, M. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.02.016 · Cited by 33
New Perspectives on Iron Uptake in Eukaryotes
Sherman, H. G., Jovanovic, C., Stolnik, S., Baronian, K. H. R., Downard, A. J., & Rawson, F. J. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00097 · Cited by 33
“It was stated that to deal with increases in extracellular iron, this upregulation of non-transferrin transport was required (Kaplan et al., 1991).”
BackgroundMRI Susceptibility Changes Suggestive of Iron Deposition in the Thalamus after Ischemic Stroke
van Etten, E. S., van der Grond, J., Dumas, E. M., van den Bogaard, S. J. A., van Buchem, M. A., & Wermer, M. J. H. (2015) · Cerebrovascular Diseases · doi:10.1159/000433560 · Cited by 32
Metadata
- Authors
- Kaplan, J., Jordan, I., & Sturrock, A.
- Affiliations
- University of Utah (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-02
- Volume
- 266
- Issue
- 5
- Pages
- 2997-3004
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1587837383
- Cited by
- 198
- References
- 26
- Citations by year
- 2026: 2 · 2024: 1 · 2023: 1 · 2021: 1 · 2020: 2 · 2019: 2 · 2018: 8 · 2016: 3 · 2015: 3 · 2014: 4 · 2013: 8 · 2012: 5
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk020630-22)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK20630, DK30534)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Micronutrient Interactions and Effects
- Keywords
- iron uptake regulation, transferrin receptor, extracellular iron, copper, zinc, intracellular calcium, iron accumulation, cultured cells
- MeSH terms
- Biological Transport, Cadmium, Calcium, Copper, Cycloheximide, Ferritins, HeLa Cells, Humans, Iron, Manganese, Transferrin, Zinc
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