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Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 October 2001, Vol. 98, No. 8, pp. 2448-2455 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY The alternatively spliced EC domain of human fibrinogen-420 is a novel ligand for leukocyte integrins M2 and X2 Valeryi K. Lishko, Valentin P. Yakubenko, Kathe M. Hertzberg, Gerd Grieninger, 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, Cleveland, OH; and the Lindsley F. Kimball Research Institute of the New York Blood Center, New York, NY. The interaction of human plasma fibrinogen with leukocyte integrins M2 (CD11b/CD18, Mac-1) and X2 (CD11c/CD18, p150,95) is an important component of the inflammatory response. Previously, it was demonstrated that binding of fibrinogen to these integrins is mediated by C, the globular C-terminal domain of the  chain. In this study, evidence was found of another fibrinogen domain that can serve as a ligand for the 2 leukocyte integrins: EC, a homologous domain that extends the  chains in a recently discovered subclass of fibrinogen known as fibrinogen-420. Recombinant EC supported strong adhesion and migration of cells expressing M2 and X2, including nonactivated and activated U937 and THP-1 monocytoid cells, and neutrophils. Cells transfected with complementary DNA for these integrins also bound EC. The specificity of interaction was substantiated by inhibition of cell adhesion with antibodies against M, X, and 2 subunits. Also, neutrophil inhibitory factor, a specific inhibitor of M2 and X2 function, efficiently blocked cell adhesion to EC. In M2 and X2, the I domain is the binding site for EC, since EC bound to recombinant M I and XI domains in a dose-dependent and saturable manner. Synthetic peptides that duplicated sequences 190 to 202 and 377 to 395, previously considered putative binding sites in C, effectively inhibited M2- and X2-mediated adhesion to EC, suggesting that recognition of EC by the I domain involves structural features in common with those of C. These findings identify EC as a second domain in fibrinogen-420 that binds M2 and X2 and can mediate leukocyte adhesion and migration. © 2001 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: E. A. Lefevre, W. R. Hein, Z. Stamataki, L. S. Brackenbury, E. A. Supple, L. G. Hunt, P. Monaghan, G. Borhis, Y. Richard, and B. 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