ArticlePloS one2015
H-Ferritin Is Preferentially Incorporated by Human Erythroid Cells through Transferrin Receptor 1 in a Threshold-Dependent Manner.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Bioengineered ferritin-based lysosome-targeting chimera platform for tumor-targeted therapy.Nature communications · 2026Article
- TMPRSS11E-mediated TFR1 cleavage influences IFN-γR2 internalization and the macrophage innate response.Communications biology · 2025Article
- Transferrin receptors.Experimental & molecular medicine · 2025Review
- A novel view of ferritin in cancer.Biochimica et biophysica acta. Reviews on cancer · 2023Review
- Molecular mimicry of the receptor-binding domain of the SARS-CoV-2 spike protein: from the interaction of spike-specific antibodies with transferrin and lactoferrin to the antiviral effects of human recombinant lactoferrin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- Efficacy of Antibodies Targeting TfR1 in Xenograft Mouse Models of AIDS-Related Non-Hodgkin Lymphoma.Cancers · 2023Article
- Reversible atransferrinemia in a patient with chronic enteropathy: is transferrin mandatory for iron transport?Biochemia medica · 2023Article
- A Historical Review of Brain Drug Delivery.Pharmaceutics · 2022Review
- Article
- New Insights into the Role of Ferritin in Iron Homeostasis and Neurodegenerative Diseases.Molecular neurobiology · 2021Review
- Abnormal ferritin levels predict development of poor outcomes in cirrhotic outpatients: a cohort study.BMC gastroenterology · 2021Article
- Antibodies Targeting the Transferrin Receptor 1 (TfR1) as Direct Anti-cancer Agents.Frontiers in immunology · 2021Review
- Structural and functional relationship of mammalian and nematode ferritins.Biotechnologia · 2021Review
- Transferrin Receptors in Erythropoiesis.International journal of molecular sciences · 2020Review
- A holistic view of mammalian (vertebrate) cellular iron uptake.Metallomics : integrated biometal science · 2020Review
- Ferritin: An Inflammatory Player Keeping Iron at the Core of Pathogen-Host Interactions.Microorganisms · 2020Review
- Ferritin Nanocages for Protein Delivery to Tumor Cells.Molecules (Basel, Switzerland) · 2020Review
- Generation and Molecular Characterization of Human Ring Sideroblasts: a Key Role of Ferrous Iron in Terminal Erythroid Differentiation and Ring Sideroblast Formation.Molecular and cellular biology · 2019Article
- Cryo-EM structure of the human ferritin-transferrin receptor 1 complex.Nature communications · 2019Article
- Brain Iron Homeostasis: A Focus on Microglial Iron.Pharmaceuticals (Basel, Switzerland) · 2018Review
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ferritin is an iron-storage protein composed of different ratios of 24 light (L) and heavy (H) subunits. The serum level of ferritin is a clinical marker of the body's iron level. Transferrin receptor (TFR)1 is the receptor not only for transferrin but also for H-ferritin, but how it binds two different ligands and the blood cell types that preferentially incorporate H-ferritin remain unknown. To address these questions, we investigated hematopoietic cell-specific ferritin uptake by flow cytometry. Alexa Fluor 488-labeled H-ferritin was preferentially incorporated by erythroid cells among various hematopoietic cell lines examined, and was almost exclusively incorporated by bone marrow erythroblasts among human primary hematopoietic cells of various lineages. H-ferritin uptake by erythroid cells was strongly inhibited by unlabeled H-ferritin but was only partially inhibited by a large excess of holo-transferrin. On the other hand, internalization of labeled holo-transferrin by these cells was not inhibited by H-ferritin. Chinese hamster ovary cells lacking functional endogenous TFR1 but expressing human TFR1 with a mutated RGD sequence, which is required for transferrin binding, efficiently incorporated H-ferritin, indicating that TFR1 has distinct binding sites for H-ferritin and holo-transferrin. H-ferritin uptake by these cells required a threshold level of cell surface TFR1 expression, whereas there was no threshold for holo-transferrin uptake. The requirement for a threshold level of TFR1 expression can explain why among primary human hematopoietic cells, only erythroblasts efficiently take up H-ferritin.
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