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Dual interaction of JAM-C with JAM-B and alpha(M)beta2 integrin: function in junctional complexes and leukocyte adhesion

Brown, James
Gilbert, R. J.
Jones, E. Y.
Kiefer, Friedemann
Ruga, Pilar
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Published in Molecular Biology of the Cell. 2005, vol. 16, no. 10, p. 4992-5003
Abstract 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.
Keywords AnimalsCell Adhesion/ physiologyCell Adhesion Molecules/genetics/ metabolismCell LineCoculture TechniquesCricetinaeCricetulusEndothelium/physiology/ultrastructureGreen Fluorescent Proteins/geneticsHumansImmunoglobulins/genetics/ metabolismIntercellular Junctions/ physiology/ultrastructureLeukocytes/ physiology/ultrastructureMacrophage-1 Antigen/ metabolismMiceMice, Inbred C57BLMicroscopy, ImmunoelectronPeptides/geneticsRecombinant Fusion Proteins/genetics/metabolism
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PMID: 16093349
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