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Blood, 15 February 2004, Vol. 103, No. 4, pp. 1503-1508. Prepublished online as a Blood First Edition Paper on October 16, 2003; DOI 10.1182/blood-2003-08-2792. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-08-2792v1 2003-08-2792v2 103/4/1503    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map 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 Mankelow, T. J. Articles by Anstee, D. J. Search for Related Content PubMed PubMed Citation Articles by Mankelow, T. J. Articles by Anstee, D. J. Related Collections Hemostasis, Thrombosis, and Vascular Biology Red Cells Cell Adhesion and Motility Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  RED CELLS Identification of critical amino-acid residues on the erythroid intercellular adhesion molecule-4 (ICAM-4) mediating adhesion to V integrins Tosti J. Mankelow, Frances A. Spring, Stephen F. Parsons, R. Leo Brady, Narla Mohandas, Joel A. Chasis, and David J. Anstee From the Bristol Institute for Transfusion Sciences, Bristol, United Kingdom; Department of Biochemistry, University of Bristol, Bristol, United Kingdom; New York Blood Center, New York, NY; and University of California Lawrence Berkeley National Laboratory, Berkeley, CA. Intercellular adhesion molecule-4 (ICAM-4, syn. LW glycoprotein) interacts with the integrins L2, M2, A41, the V family, and IIb3. Systematic mutagenesis of surface-exposed residues conserved between human and murine ICAM-4 defined 12 single amino-acid changes that affect the interaction of ICAM-4 with V integrins. Mutation of 10 of these residues, 8 of which are spatially close on the surface of the molecule, led to a reduction in adhesion. Moreover, peptides corresponding to regions of ICAM-4 involved in its interaction with V integrins inhibited these interactions. The other 2 mutations increased the extent of interaction of ICAM-4 with V integrins. These mutations appear to prevent glycosylation of N160, suggesting that changes in glycosylation may modulate ICAM-4–V integrin interactions. The region of ICAM-4 identified as the binding site for V integrins is adjacent to the binding sites for L2 and M2. Selective binding of ICAM-4 to different integrins may be important for a variety of normal red cell functions and also relevant to the pathology of thrombotic disorders and vasoocclusive events in sickle cell disease. Our findings suggest the feasibility of developing selective inhibitors of ICAM-4–integrin adhesion of therapeutic value in these diseases. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Cell adhesion: a partner for many Carl G. Gahmberg Blood 2004 103: 1183. [Full Text] [PDF] This article has been cited by other articles: M.-H. Odievre, V. Bony, M. Benkerrou, C. Lapoumeroulie, C. Alberti, R. Ducrocq, E. Jacqz-Aigrain, J. Elion, and J.-P. Cartron Modulation of erythroid adhesion receptor expression by hydroxyurea in children with sickle cell disease Haematologica, April 1, 2008; 93(4): 502 - 510. [Abstract] [Full Text] [PDF] T. J. Mankelow, N. Burton, F. O. Stefansdottir, F. A. Spring, S. F. Parsons, J. S. Pedersen, C. L. P. Oliveira, D. Lammie, T. Wess, N. Mohandas, et al. The Laminin 511/521 binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3 Blood, November 1, 2007; 110(9): 3398 - 3406. [Abstract] [Full Text] [PDF] E. M. Finnegan, G. A. Barabino, X.-d. Liu, H.-Y. Chang, A. Jonczyk, and D. K. Kaul Small-molecule cyclic {alpha}Vbeta3 antagonists inhibit sickle red cell adhesion to vascular endothelium and vasoocclusion Am J Physiol Heart Circ Physiol, August 1, 2007; 293(2): H1038 - H1045. [Abstract] [Full Text] [PDF] B. O. Fabriek, M. M. J. Polfliet, R. P. M. Vloet, R. C. van der Schors, A. J. M. Ligtenberg, L. K. Weaver, C. Geest, K. Matsuno, S. K. Moestrup, C. D. Dijkstra, et al. The macrophage CD163 surface glycoprotein is an erythroblast adhesion receptor Blood, June 15, 2007; 109(12): 5223 - 5229. [Abstract] [Full Text] [PDF] E. Ihanus, L. M. Uotila, A. Toivanen, M. Varis, and C. G. Gahmberg Red-cell ICAM-4 is a ligand for the monocyte/macrophage integrin CD11c/CD18: characterization of the binding sites on ICAM-4 Blood, January 15, 2007; 109(2): 802 - 810. [Abstract] [Full Text] [PDF] D. K. Kaul, X.-d. Liu, X. Zhang, T. Mankelow, S. Parsons, F. Spring, X. An, N. Mohandas, D. Anstee, and J. A. Chasis Peptides based on {alpha}V-binding domains of erythrocyte ICAM-4 inhibit sickle red cell-endothelial interactions and vaso-occlusion in the microcirculation Am J Physiol Cell Physiol, November 1, 2006; 291(5): C922 - C930. [Abstract] [Full Text] [PDF] G. Lee, A. Lo, S. A. Short, T. J. Mankelow, F. Spring, S. F. Parsons, K. Yazdanbakhsh, N. Mohandas, D. J. Anstee, and J. A. Chasis Targeted gene deletion demonstrates that the cell adhesion molecule ICAM-4 is critical for erythroblastic island formation Blood, September 15, 2006; 108(6): 2064 - 2071. [Abstract] [Full Text] [PDF]

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