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Blood, 15 January 2007, Vol. 109, No. 2, pp. 802-810. Prepublished online as a Blood First Edition Paper on September 19, 2006; DOI 10.1182/blood-2006-04-014878. This Article Full Text (PDF) Supplemental Figure All Versions of this Article: blood-2006-04-014878v1 109/2/802    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Ihanus, E. Articles by Gahmberg, C. G. Search for Related Content PubMed PubMed Citation Articles by Ihanus, E. Articles by Gahmberg, C. G. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted April 5, 2006 Accepted August 17, 2006 Red cell ICAM-4 is a ligand for the monocyte/macrophage integrin CD11c/CD18: Characterization of the binding sites on ICAM-4 Eveliina Ihanus, Liisa M. Uotila, Anne Toivanen, Minna Varis, and Carl G. Gahmberg* Faculty of Biosciences, Division of Biochemistry, University of Helsinki, Helsinki, Finland * Corresponding author; email: carl.gahmberg{at}helsinki.fi. Intercellular adhesion molecule-4 (ICAM-4) is a unique member of the ICAM family due to its specific expression on erythroid cells and ability to interact with several types of integrins expressed on blood and endothelial cells. The first reported receptors for ICAM-4 were CD11a/CD18 and CD11b/CD18. In contrast to these two, the cellular ligands and the functional role of the third 2-integrin, CD11c/CD18, have not been well defined. Here we show that ICAM-4 functions as a ligand for the monocyte/macrophage specific CD11c/CD18. Deletion of the individual immunoglobulin domains of ICAM-4 demonstrated that both its domains contain binding sites for CD11c/CD18. Analysis of a panel of ICAM-4 point mutants identified residues that affected binding to the integrin. By molecular modeling the important residues were predicted to cluster in two distinct but spatially close regions of the first domain with an extension to the second domain spatially distant from the other residues. We also identified two peptides derived from sequences of ICAM-4 that are capable of modulating the binding to CD11c/CD18. CD11c/CD18 is expressed on macrophages in spleen and bone marrow. Inhibition of erythrophagocytosis by anti-ICAM-4 and anti-integrin antibodies suggests a role for these interactions in removal of senescent red cells. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: R. Carreno, D. Li, M. Sen, I. Nira, T. Yamakawa, Q. Ma, and G. B. Legge A Mechanism for Antibody-mediated Outside-in Activation of LFA-1 J. Biol. Chem., April 18, 2008; 283(16): 10642 - 10648. [Abstract] [Full Text] [PDF] R. Zennadi, B. J. Moeller, E. J. Whalen, M. Batchvarova, K. Xu, S. Shan, M. Delahunty, M. W. Dewhirst, and M. J. Telen Epinephrine-induced activation of LW-mediated sickle cell adhesion and vaso-occlusion in vivo Blood, October 1, 2007; 110(7): 2708 - 2717. [Abstract] [Full Text] [PDF] C. Sadhu, H. J. Ting, B. Lipsky, K. Hensley, L. F. Garcia-Martinez, S. I. Simon, and D. E. Staunton CD11c/CD18: novel ligands and a role in delayed-type hypersensitivity J. Leukoc. Biol., June 1, 2007; 81(6): 1395 - 1403. [Abstract] [Full Text] [PDF]

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