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Cited by 169Iron Metabolism and DisordersTrace Elements in HealthPlant Micronutrient Interactions and Effects

Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mkmice

Canonne-Hergaux, François, Zhang, An-Sheng, Ponka, Prem, Gros, Philippe·2001·Blood
DOI 10.1182/blood.v98.13.3823
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Abstract

Divalent metal transporter 1 (DMT1) is the major transferrin-independent iron uptake system at the apical pole of intestinal cells, but it may also transport iron across the membrane of acidified endosomes in peripheral tissues. Iron transport and expression of the 2 isoforms of DMT1 was studied in erythroid cells that consume large quantities of iron for biosynthesis of hemoglobin. In mk/mk mice that express a loss-of-function mutant variant of DMT1, reticulocytes have a decreased cellular iron uptake and iron incorporation into heme. Interestingly, iron release from transferrin inside the endosome is normal in mk/mkreticulocytes, suggesting a subsequent defect in Fe++ transport across the endosomal membrane. Studies by immunoblotting using membrane fractions from peripheral blood or spleen from normal mice where reticulocytosis was induced by erythropoietin (EPO) or phenylhydrazine (PHZ) treatment suggest that DMT1 is coexpressed with transferrin receptor (TfR) in erythroid cells. Coexpression of DMT1 and TfR in reticulocytes was also detected by double immunofluorescence and confocal microscopy. Experiments with isoform-specific anti-DMT1 antiserum strongly suggest that it is the non–iron-response element containing isoform II of DMT1 that is predominantly expressed by the erythroid cells. As opposed to wild-type reticulocytes, mk/mk reticulocytes express little if any DMT1, despite robust expression of TfR, suggesting a possible effect of the mutation on stability and targeting of DMT1 isoform II in these cells. Together, these results provide further evidence that DMT1 plays a central role in iron acquisition via the transferrin cycle in erythroid cells.

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  • Later reports of HH pedigrees observed the C282Y mutation in both alleles of the HFE gene with a prevalence of between 60% and 100%.

    “Later reports of HH pedigrees also observed this mutation in both alleles of the HFE gene that encodes a tyrosine instead of the normal cysteine at codon 282 (C282Y), as having a prevalence of between 60% and 100% (40, 147, 150).”

    From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [40]

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Authors
Canonne-Hergaux, F., Zhang, A.-S., Ponka, P., & Gros, P.
Affiliations
  • From the Departments of Biochemistry, Physiology, and Medicine, McGill University, and the Lady Davis Institute for Medical Research, Jewish General Hospital, Montreal, QC, Canada.
  • Jewish General Hospital (CA)
ORCID
Venue
Blood
Publisher
American Society of Hematology
Published
2001-12-15
Volume
98
Issue
13
Pages
3823-3830
ISSN
  • 0006-4971 (ISSN-L)
  • 1528-0020
DOI
10.1182/blood.v98.13.3823
OpenAlex
W1984912112
Cited by
169
References
43
Citations by year
2026: 6 · 2025: 6 · 2024: 5 · 2023: 4 · 2022: 5 · 2021: 2 · 2020: 10 · 2019: 3 · 2018: 3 · 2017: 3 · 2016: 3 · 2015: 4 · 2014: 12 · 2013: 6 · 2012: 8
FWCI
3.38
Type
journal article
Language
en
Open access
closed
Locations
  • Blood (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Allergy and Infectious Diseases (AI355237)
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
DMT1, iron transport, reticulocytes, erythroid cells, transferrin receptor, heme biosynthesis, reticulocytosis, erythropoiesis, phenylhydrazine, erythropoietin
MeSH terms
Solute Carrier Family 11, Member 2, Anemia, Animals, Biological Transport, Erythrocyte Membrane, Erythrocytes, Leukemia, Erythroblastic, Acute, Erythropoietin, Fluorescent Antibody Technique, Cricetinae, Heme, Hemoglobins, Homozygote, Iron, Mice, Mutant Strains, Mutation, Phenylhydrazines, Endosomes, Reticulocytes, Spleen, Transferrin, Tumor Cells, Cultured, Erythroid Precursor Cells, CHO Cells, Reticulocyte Count, Microscopy, Confocal, Protein Isoforms, Cation Transport Proteins, Iron-Binding Proteins, Mice

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