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Prepublished online as a Blood First Edition Paper on October 24, 2002; DOI 10.1182/blood-2002-09-2742.
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Blood, 1 March 2003, Vol. 101, No. 5, pp. 2008-2014
RED CELLS
Heterotypic interactions between transferrin receptor and
transferrin receptor 2
Todd M. Vogt,
Aaron D. Blackwell,
Anthony M. Giannetti,
Pamela J. Bjorkman, and
Caroline A. Enns
From the Department of Cell and Developmental
Biology, Oregon Health and Science University, Portland OR; Howard
Hughes Medical Institute and the Division of Biology, California
Institute of Technology, Pasadena, CA.
Cellular iron uptake in most tissues occurs via endocytosis of
diferric transferrin (Tf) bound to the transferrin receptor (TfR).
Recently, a second transferrin receptor, transferrin receptor 2 (TfR2),
has been identified and shown to play a critical role in iron
metabolism. TfR2 is capable of Tf-mediated iron uptake and mutations in
this gene result in a rare form of hereditary hemochromatosis unrelated
to the hereditary hemochromatosis protein, HFE. Unlike TfR, TfR2
expression is not controlled by cellular iron concentrations and little
information is currently available regarding the role of TfR2 in
cellular iron homeostasis. To investigate the relationship between TfR
and TfR2, we performed a series of in vivo and in vitro experiments
using antibodies generated to each receptor. Western blots demonstrate
that TfR2 protein is expressed strongest in erythroid/myeloid cell
lines. Metabolic labeling studies indicate that TfR2 protein levels are
approximately 20-fold lower than TfR in these cells. TfR and TfR2 have
similar cellular localizations in K562 cells and coimmunoprecipitate to only a very limited extent. Western analysis of the receptors under
nonreducing conditions reveals that they can form heterodimers.
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