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Chavakis, T. et al.

Chavakis, Keiper, Matz-Westphal, Hersemeyer, Sachs, Nawroth, Preissner, Santoso,

The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo.

The third member of the family of junctional adhesion molecules (JAMs), JAM-3, also called JAM-C, was recently shown to be a novel counter-receptor on platelets for the leukocyte beta(2)-integrin Mac-1 (alphaMbeta(2), CD11b/CD18). Here, new functional aspects of the role of endothelial cell JAM-C were investigated. Endothelial cells express JAM-C, which is predominantly localized within junctions at interendothelial contacts, since it codistributes with a tight junction component, zonula occludens-1. Whereas JAM-C does not participate in neutrophil adhesion to endothelial cells, it mediates neutrophil transmigration in a Mac-1-dependent manner. In particular, inhibition of JAM-C significantly reduced neutrophil transendothelial migration, and the combination of JAM-C and platelet/endothelial cell adhesion molecule-1 blockade almost completely abolished neutrophil transendothelial migration in vitro. In vivo, inhibition of JAM-C with soluble mouse JAM-C resulted in a 50% reduction of neutrophil emigration in the mouse model of acute thioglycollate-induced peritonitis. Thus, JAM-C participates in neutrophil transmigration and thereby provides a novel molecular target for antagonizing interactions between vascular cells that promote inflammatory vascular pathologies.[1]

References

The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo. Chavakis, T., Keiper, T., Matz-Westphal, R., Hersemeyer, K., Sachs, U.J., Nawroth, P.P., Preissner, K.T., Santoso, S. J. Biol. Chem. (2004) [Pubmed]

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