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The junctional adhesion molecules (JAMs) have been recently described as interendothelial junctional molecules and as integrin ligands. Here we show that JAM-B and JAM-C undergo heterophilic interaction in cell-cell contacts and that JAM-C is recruited and stabilized in junctional complexes by JAM-B. In addition, soluble JAM-B dissociates soluble JAM-C homodimers to form JAM-B/JAM-C heterodimers. This suggests that the affinity of JAM-C monomers to form dimers is higher for JAM-B than for JAM-C. Using antibodies against JAM-C, the formation of JAM-B/JAM-C heterodimers can be abolished. This liberates JAM-C from its vascular binding partner JAM-B and makes it available on the apical side of vessels for interaction with its leukocyte counter-receptor alpha(M)beta2 integrin. We demonstrate that the modulation of JAM-C localization in junctional complexes is a new regulatory mechanism for alpha(M)beta2-dependent adhesion of leukocytes.

Original publication

DOI

10.1091/mbc.e05-04-0310

Type

Journal article

Journal

Mol Biol Cell

Publication Date

10/2005

Volume

16

Pages

4992 - 5003

Keywords

Animals, Cell Adhesion, Cell Adhesion Molecules, Cell Line, Coculture Techniques, Cricetinae, Cricetulus, Endothelium, Green Fluorescent Proteins, Humans, Immunoglobulins, Intercellular Junctions, Leukocytes, Macrophage-1 Antigen, Mice, Mice, Inbred C57BL, Microscopy, Immunoelectron, Oligopeptides, Peptides, Recombinant Fusion Proteins