Journal
BLOOD
Volume 108, Issue 4, Pages 1388-1394Publisher
AMER SOC HEMATOLOGY
DOI: 10.1182/blood-2006-02-003681
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Funding
- NCI NIH HHS [R24 CA086307, R24 CA86307] Funding Source: Medline
- NHLBI NIH HHS [R01 HL074247] Funding Source: Medline
- NIDDK NIH HHS [R01 DK062474] Funding Source: Medline
- NIGMS NIH HHS [T32 GM07753, T32 GM007753] Funding Source: Medline
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Iron and copper are essential for all organisms, assuming critical roles as cofactors in many enzymes. In eukaryotes, the transmembrane transport of these elements is a highly regulated process facilitated by the single electron reduction of each metal. Previously, we identified a mammalian ferrireductase, Steap3, critical for erythroid iron homeostasis. Now, through homology, expression, and functional studies, we characterize all 4 members of this protein family and demonstrate that 3 of them, Steap2, Steap3, and Steap4, are not only ferrireductases but also cupric reductases that stimulate cellular uptake of both iron and copper in vitro. Finally, the pattern of tissue expression and subcellular localization of these proteins suggest they are physiologically relevant cupric reductases and ferrireductases in vivo.
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