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MBC in Press, published online ahead of print March 30, 2005
Mol. Biol. Cell 10.1091/mbc.E05-01-0036

A more recent version of this article appeared on June 1, 2005
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Submitted on January 18, 2005
Revised on March 15, 2005
Accepted on March 22, 2005

Neutrophil Migration across Tight Junctions Is Mediated by Adhesive Interactions between Epithelial CAR and a JAM-Like Protein on Neutrophils

Ke Zen,* Yuan Liu,{dagger} Ingrid C. McCall,* Tao Wu,* Winston Lee,* Brian A. Babbin,* Asma Nusrat,* and Charles A. Parkos*

*Epithelial Pathobiology Research Unit, Department of Pathology and Laboratory Medicine, Emory University, Atlanta, GA 30322; {dagger}Department of Biology, Georgia State University, Atlanta, GA 30034

Monitoring Editor: Keith Mostov

Neutrophil(PMN) transepithelial migration during inflammatory episodes involves a complex series of adhesive interactions and signaling events. Previous studies have shown that key adhesive interactions between leukocyte CD11b/CD18 and basally expressed proteoglycans followed by binding to desmosomal-associated JAM-C are key elements of the transmigration response. Here we provide the first evidence that PMN-expressed junctional adhesion molecule-like protein (JAML) regulates transmigration via binding interactions with epithelial coxsackie and adenovirus receptor (CAR). Experiments with a JAML fusion protein revealed specific binding of JAML to epithelial CAR expressed at tight junctions in T84 cell monolayers and normal human colonic mucosa. Furthermore, JAML-CAR binding is mediated via the membrane distal immunoglobulin (Ig) loop of CAR and the membrane proximal Ig loop of JAML. PMN bound to immobilized CAR but not JAML in a divalent cation-independent manner. Lastly, in assays of PMN transepithelial migration, JAML/CAR fusion proteins and their antibodies significantly inhibited transmigration in a specific manner. Taken together, these results indicate that JAML and CAR are a novel pair of adhesion molecules that play an important role in modulating PMN migration cross epithelial tight junctions. These findings add a new element to a multistep model of PMN transepithelial migration and may provide new targets for antiinflammatory therapies.

Address correspondence to: Ke Zen (kzen{at}emory.edu) or Charles A. Parkos (cparkos{at}emory.edu)




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