The Journal of Experimental Medicine
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Published online 14 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}Mß2-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

Correspondence to: Edward F. Plow, Department of Molecular Cardiology (NB50), Cleveland Clinic Foundation, 9500 Euclid Ave./NB50, Cleveland, OH 44195. Tel:216-445-8200 Fax:216-445-8204 E-mail:plowe{at}ccf.org.

Leukocyte migration is the hallmark of inflammation, and integrin {alpha}Mß2 and its ligand fibrinogen (Fg) are key participants in this cellular response. Cells expressing wild-type or mutant {alpha}Mß2 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}Mß2 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 ß2 subunit, supported migration poorly, thus, the {alpha}MI domain is necessary but not sufficient to support chemotaxis, and efficient migration requires the ß2 subunit and {alpha}MI domain; and (c) in addition to supporting cell migration, P2 enhanced {alpha}Mß2-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}Mß2 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


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