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A more recent version of this article appeared on August 1, 2004
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Submitted on April 15, 2004
Revised on June 1, 2004
Accepted on June 4, 2004
, 
,
*Epithelial Pathobiology Research Unit, Department of Pathology and Laboratory Medicine, Emory University, Atlanta, Georgia 30322; Raven Biotechnologies, Inc, South San Francisco, California 94080
Monitoring Editor: Daniel Goodenough
Neutrophil (PMN) transepithelial migration is dependent on the leukocyte 
2 integrin CD11b/CD18, yet the identity of epithelial counterreceptors remains elusive. Recently, a JAM protein family member termed JAM-C was implicated in leukocyte adhesive interactions; however, its expression in epithelia and role in PMN-epithelial interactions are unknown. Here, we demonstrate that JAM-C is abundantly expressed basolaterally in intestinal epithelia and localizes to desmosomes but not tight junctions. Desmosomal localization of JAM-C was further confirmed by experiments aimed at selective disruption of tight junctions and desmosomes. In assays of PMN transepithelial migration, both JAM-C mAbs and JAM-C/Fc chimeras significantly inhibited the rate of PMN transmigration. Additional experiments revealed specific binding of JAM-C to CD11b/CD18 and provided evidence of other epithelial ligands for CD11b/CD18. These findings represent the first demonstration of direct adhesive interactions between PMN and epithelial intercellular junctions (desmosomes) that regulate PMN transepitheial migration and also suggest that JAM-C may play a role in desmosomal structure/function.
Corresponding author. E-mail: kzen{at}emory.edu
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