The Journal of Experimental Medicine
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Published online 21 May 2001.
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© The Rockefeller University Press, 0022-1007/2001/5/1123/ $5.00
The Journal of Experimental Medicine, Volume 193, Number 10, May 21, 2001 1123-1134

Original Article

Integrin {alpha}Mβ2-Mediated Cell Migration to Fibrinogen and Its Recognition Peptides

Christopher B. Forsytha, Dmitry A. Solovjova, Tatiana P. Ugarovaa, and Edward F. Plowa

a Joseph J. Jacobs Center for Thrombosis and Vascular Biology, and the Department of Molecular Cardiology, Cleveland Clinic Foundation, Cleveland, Ohio 44195
Department of Molecular Cardiology (NB50), Cleveland Clinic Foundation, 9500 Euclid Ave./NB50, Cleveland, OH 44195.216-445-8204216-445-8200

plowe{at}ccf.org

Leukocyte migration is the hallmark of inflammation, and integrin {alpha}Mβ2 and its ligand fibrinogen (Fg) are key participants in this cellular response. Cells expressing wild-type or mutant {alpha}Mβ2 and Fg or its derivatives have been used to dissect the molecular requirements for this receptor–ligand pair to mediate cell migration. The major conclusions are that (a) Fg, its D fragment, and its P1 and P2 {alpha}Mβ2 recognition peptides support a chemotactic response; (b) when the I domain of {alpha}L was replaced with the I domain of {alpha}M, the chimeric receptor supported cell migration to Fg; however, the {alpha}M subunit, containing the I domain but lacking the β2 subunit, supported migration poorly, thus, the {alpha}MI domain is necessary but not sufficient to support chemotaxis, and efficient migration requires the β2 subunit and {alpha}MI domain; and (c) in addition to supporting cell migration, P2 enhanced {alpha}Mβ2-mediated chemotaxis to Fg and the P1 peptide. This activation was associated with exposure of the activation-dependent epitope recognized by monoclonal antibody 7E3 and was observed also with human neutrophils. Taken together, these data define specific molecular requirements for {alpha}Mβ2 to mediate cell migration to Fg derivatives and assign a novel proinflammatory activity to the P2 peptide.

Key Words: adhesion molecules • fibrinogen • integrin • CD11b/CD18 • inflammation

Abbreviations used in this paper: Fg, fibrinogen; Fn, fibronectin; HPF, high power field; ICAM, intercellular adhesion molecule; MIDAS, metal ion–dependent adhesion site; NIF, neutrophil inhibitory factor; WT, wild-type.

© 2001 The Rockefeller University Press


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