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Blood, 15 February 2006, Vol. 107, No. 4, pp. 1643-1650. Prepublished online as a Blood First Edition Paper on October 20, 2005; DOI 10.1182/blood-2005-06-2509. This Article Full Text Full Text (PDF) All Versions of this Article: 2005-06-2509v1 107/4/1643    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 Yakubenko, V. P. Articles by Ugarova, T. P. Search for Related Content PubMed PubMed Citation Articles by Yakubenko, V. P. Articles by Ugarova, T. P. Related Collections Hemostasis, Thrombosis, and Vascular Biology Phagocytes Cell Adhesion and Motility Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  PHAGOCYTES Integrin D2, an adhesion receptor up-regulated on macrophage foam cells, exhibits multiligand-binding properties Valentin P. Yakubenko, Satya P. Yadav, and Tatiana P. Ugarova From the Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic Foundation, OH. Integrin D2, the most recently discovered member of the 2 subfamily of integrin adhesion receptors, is up-regulated on macrophage foam cells. Although other members of the subfamily have been subjects of extensive research, the recognition specificity and the molecular basis for D2 ligand binding remain unknown. Based on the high extent of structural homology between D2 and the major myeloid-cell-specific integrin M2 (Mac-1), noted for its capacity to bind multiple ligands, we considered that the 2 integrins have similar recognition specificity. In this study, using recombinant and natural D2-expressing cells, we demonstrate that D2 supports adhesion and migration to many extracellular matrix proteins in a fashion similar to M2. Consistent with these data, the recombinant DI-domain of the receptor bound selected ligands. The binding was activation-dependent because the DI-domain with its C-terminal 7 helix truncated, but not the form with the C-terminal part extended, bound ligands. When the DI-domain segment Lys244-Lys260 (highly homologous to its MI-domain counterpart Lys245-Arg261 responsible for M2 multiligand-binding properties) was inserted into the mono-specific LI-domain, the chimeric protein bound many ligands with affinities similar to those of wild-type DI-domain. These results establish integrin D2 as a multiligand receptor and indicate that the mechanism whereby D2 exhibits broad ligand specificity resembles that used by M2, the most promiscuous member of the integrin family. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. R. Barthel, M. W. Johansson, D. M. McNamee, and D. F. Mosher Roles of integrin activation in eosinophil function and the eosinophilic inflammation of asthma J. Leukoc. Biol., January 1, 2008; 83(1): 1 - 12. [Abstract] [Full Text] [PDF] Y. Miyazaki, M. Bunting, D. M. Stafforini, E. S. Harris, T. M. McIntyre, S. M. Prescott, V. S. Frutuoso, F. C. Amendoeira, D. de Oliveira Nascimento, A. Vieira-de-Abreu, et al. Integrin {alpha}D 2 Is Dynamically Expressed by Inflamed Macrophages and Alters the Natural History of Lethal Systemic Infections J. Immunol., January 1, 2008; 180(1): 590 - 600. [Abstract] [Full Text] [PDF] V. K. Lishko, T. Burke, and T. Ugarova Antiadhesive effect of fibrinogen: a safeguard for thrombus stability Blood, February 15, 2007; 109(4): 1541 - 1549. [Abstract] [Full Text] [PDF]

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