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Prepublished online as a Blood First Edition Paper on May 31, 2002; DOI 10.1182/blood-2002-04-1182.
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Blood, 1 October 2002, Vol. 100, No. 7, pp. 2617-2622
PHAGOCYTES
Iron transporter Nramp2/DMT-1 is associated with the membrane of
phagosomes in macrophages and Sertoli cells
Nada Jabado,
François Canonne-Hergaux,
Samantha Gruenheid,
Virgine Picard, and
Philippe Gros
From the Department of Biochemistry, McGill University,
Montreal, Quebec, Canada.
Nramp2 (DMT1) is a pH-dependent divalent cation transporter that
acts as the transferrin-independent iron uptake system at the
intestinal brush border and also transports iron released from
transferrin across the membrane of acidified endosomes. In this study,
RAW264.7 macrophages and 2 independently derived murine Sertoli cells
lines, TM4 and 15P-1, were used to further study the subcellular
localization of Nramp2/DMT1 in phagocytic cells, including possible
recruitment to the phagosomal membrane. Nramp2/DMT1 was localized
primarily to the EEA1-positive recycling endosome compartment, with
some overlapping staining with Lamp1-positive late endosomes. After
phagocytosis, immunofluorescence analysis and in vitro biochemical
studies using purified latex bead-containing phagosomes indicated
Nramp2/DMT1 recruitment to the membrane of Lamp1, cathepsin D, and
rab7-positive phagosomes. Nramp2/DMT1 was also found associated with
erythrocyte-containing phagosomes in RAW macrophages and with the
periphery of sperm-containing phagosomes in Sertoli cells. These
results suggest that, as for the macrophage-specific Nramp1 protein,
Nramp2/DMT1 may transport divalent metals from the phagosomal space.

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