| |
|
|
|
|
|
|
|||
|
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.
HEMATOPOIESIS The macrophage CD163 surface glycoprotein is an erythroblast adhesion receptor1 Department of Molecular Cell Biology, Vrije Universiteit Medical Center, Amsterdam, the Netherlands; 2 Department of Molecular and Cellular Neurobiology, Research Institute Neurosciences, Faculty of Biology, Vrije Universiteit, Amsterdam, the Netherlands; 3 Department of Oral Biochemistry, Academic Center for Dentistry (ACTA), Amsterdam, the Netherlands; 4 Department of Immunology and Microbiology, Dartmouth Medical School, Lebanon, NH; 5 Department of Immunology, University Medical Center Utrecht, the Netherlands; 6 Department of Anatomy, Dokkyo University, School of Medicine, Tochigi, Japan; 7 Department of Medical Biochemistry, University of Aarhus, Denmark; 8 Department of Blood Cell Research, Sanquin Research and Landsteiner Laboratory, Academic Medical Center (AMC), University of Amsterdam, the Netherlands 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 13amino 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.
Related Article in Blood Online:
This article has been cited by other articles:
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Copyright © 2007 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||