The ferrireductase paraferritin contains divalent metal transporter as well as mobilferrin

Inorganic iron can be transported into cells in the absence of transferrin. Ferric iron enters cells utilizing an integrin-mobilferrin-paraferritin pathway, whereas ferrous iron uptake is facilitated by divalent metal transporter-1 (DMT-1). Immunoprecipitation studies using antimobilferrin antibody...

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Bibliographic Details
Published in:American journal of physiology: Gastrointestinal and liver physiology 2002-03, Vol.282 (3), p.G534-G539
Main Authors: Umbreit, Jay N, Conrad, Marcel E, Hainsworth, Lucille N, Simovich, Marcia
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological Transport
Blotting, Western
Carrier Proteins - analysis
Carrier Proteins - chemistry
Cation Transport Proteins
Electrophoresis, Polyacrylamide Gel
Ferric Compounds - metabolism
Ferritins - chemistry
Ferrous Compounds - metabolism
FMN Reductase
Humans
Immunosorbent Techniques
Iron-Binding Proteins
Leukemia, Erythroblastic, Acute
Molecular Sequence Data
NADH, NADPH Oxidoreductases - chemistry
NADP - metabolism
Oxidation-Reduction
Tumor Cells, Cultured
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Summary:Inorganic iron can be transported into cells in the absence of transferrin. Ferric iron enters cells utilizing an integrin-mobilferrin-paraferritin pathway, whereas ferrous iron uptake is facilitated by divalent metal transporter-1 (DMT-1). Immunoprecipitation studies using antimobilferrin antibody precipitated the previously described large-molecular-weight protein complex named paraferritin. It was previously shown that paraferritin functions as an intracellular ferrireductase, reducing ferric iron to ferrous iron utilizing NADPH as the energy source. It functions in the pathway for the cellular uptake of ferric iron. This multipeptide protein contains a number of active peptides, including the ferric iron binding protein mobilferrin and a flavin monooxygenase. The immunoprecipitates and purified preparations of paraferritin also contained DMT-1. This identifies DMT-1 as one of the peptides constituting the paraferritin complex. Since paraferritin functions to reduce newly transported ferric iron to ferrous iron and DMT-1 can transport ferrous iron, these findings suggest a role for DMT-1 in conveyance of iron from paraferritin to ferrochelatase, the enzyme utilizing ferrous iron for the synthesis of heme in the mitochondrion.
ISSN:0193-1857
1522-1547
DOI:10.1152/ajpgi.00199.2001