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*Substance via MeSH
The Journal of Immunology, 2004, 172: 7060-7068.
Copyright © 2004 by The American Association of Immunologists

Intracellular and Cell Surface Localization of a Complex between {alpha}M{beta}2 Integrin and Promatrix Metalloproteinase-9 Progelatinase in Neutrophils1

Michael Stefanidakis2,*, Terhi Ruohtula*, Niels Borregaard{dagger}, Carl G. Gahmberg* and Erkki Koivunen*

* Department of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland; and {dagger} Granulocyte Research Laboratory, Department of Hematology, The National University Hospital, Rigshospitalet, Copenhagen, Denmark

We have recently demonstrated that promatrix metalloproteinases (proMMPs), particularly proMMP-9, are potent ligands of the leukocyte {beta}2 integrins. We studied here the complex formation between proMMP-9 and {alpha}M{beta}2, the major MMP and integrin of neutrophils. On resting neutrophils, the proMMP-9/{alpha}M{beta}2 complex was primarily detected in intracellular granules, but after cellular activation it became localized to the cell surface, as demonstrated by immunoprecipitation and double immunofluorescence. Further indication of the complex formation was that neutrophils and {alpha}M{beta}2-transfected L cells, but not the wild-type L cells or leukocyte adhesion deficiency cells, bound to immobilized proMMP-9 or its recombinant catalytic domain in a {beta}2 integrin-dependent manner. Peptides that bound to the {alpha}M integrin-I domain and inhibited its complex formation with proMMP-9 prevented neutrophil migration in a transendothelial assay in vitro and in a thioglycolate-elicited peritonitis in vivo. These results suggest that the translocating proMMP-9/{alpha}M{beta}2 complex may be part of the cell surface machinery guiding neutrophil migration.




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