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Blood, 15 June 2007, Vol. 109, No. 12, pp. 5223-5229.
Prepublished online as a Blood First Edition Paper on March 12, 2007; DOI 10.1182/blood-2006-08-036467.
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Submitted August 8, 2006
Accepted December 20, 2006
The macrophage CD163 surface glycoprotein is an
erythroblast adhesion receptor
Babs O Fabriek, Machteld MJ Polfliet, Rianka PM Vloet, Roel C van der Schors, Antoon JM Ligtenberg, Lehn K Weaver, Christiaan Geest, Kenjiro Matsuno, Soren K Moestrup, Christien D Dijkstra, and Timo K van den Berg*
Dept of Molecular Cell Biology, Vrije Universiteit medical center, Amsterdam, Netherlands
Dept of Molecular & Cellular Neurobiology, Research Institute Neurosciences, Faculty of Biology, Vrije Universiteit, Amsterdam, Netherlands
Dept of Oral Biochemistry, Academic Center for Dentistry (ACTA), Amsterdam, Netherlands
Dept of Immunology & Microbiology, Dartmouth Medical School, Lebanon, NH, United States
Dept of Immunology, Universitary Medical Center Utrecht, Utrecht, Netherlands
Dept of Anatomy, Dokkyo University, School of Medicine, Tochigi, Japan
Dept of Medical Biochemistry, University of Aarhus, Aarhus, Denmark
Dept of Blood Cell Research, Sanquin Research & Landsteiner Laboratory, AMC, University of Amsterdam, Amsterdam, Netherlands
* Corresponding author; email: t.k.vandenberg{at}sanquin.nl.
Erythropoiesis occurs in erythroblastic islands where developing erythroblasts closely interact with macrophages. The adhesion molecules that govern macrophage-erythroblast contact have only been partially defined. Our previous work has implicated the rat ED2 antigen, which is highly expressed on the surface of macrophages in erythroblastic islands, in erythroblast binding. In particular, the monoclonal antibody ED2 was found to inhibit erythroblast binding to bone marrow macrophages. Here, we identify the ED2 antigen as the rat CD163 surface glycoprotein, a member of the group B scavenger receptor cysteine-rich (SRCR) family that has previously been shown to function as a receptor for hemoglobin-haptoglobin (Hb-Hp) complexes and is believed to contribute to the clearance of free hemoglobin. CD163 transfectants and recombinant protein containing the extracellular domain of CD163 supported the adhesion of erythroblastic cells. Furthermore, we identified a 13 amino acid motif (CD163p2) corresponding to a putative interaction site within the second scavenger receptor domain of CD163 that could mediate erythroblast binding. Finally, CD163p2 promoted erythroid expansion in vitro, suggesting that it enhanced erythroid proliferation and/or survival, but did not affect differentiation. These findings identify CD163 on macrophages as an adhesion receptor for erythroblasts in erythroblastic islands and suggest a regulatory role for CD163 during erythropoiesis.
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