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Articles in PresS, published online ahead of print November 13, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00331.2002
Submitted on July 16, 2002
Accepted on November 8, 2002
1 Biomedical Engineering, University of California, Davis, Davis, CA, USA
* To whom correspondence should be addressed. E-mail: sisimon{at}ucdavis.edu.
Cross-linking of L-selectin on leukocytes signals phosphorylation of mitogen activated protein kinases (MAPK) leading to activation of CD18 function and enhanced transmigration on inflamed endothelium. Here we examine how alterations in the topography of L-selectin correlate with the dynamics of CD18 activation and phosphorylation of MAPK. Simultaneous ligation of humanized antibodies DREG55 and DREG200 provided a strategy to regulate the extent of cross-linking. Triggering of CD11b/CD18 upregulation and adhesion required clustering of L-selectin to microvillus sized patches of ~.2 µm2. Immunofluorescence revealed that L-selectin was colocalized with high affinity CD18. Anti-L-selectin coated protein-A microspheres revealed that a single site of contact to a 5.5 µm bead, or multiple contacts to 0.94 or 0.3 µm beads, elicited maximum neutrophil activation. Adhesion signaled via L-selectin coincided with the kinetics of MAPK phosphorylation and was inhibited by blocking p38 or p42/44 activity. These data demonstrate the capacity of L-selectin to transduce signals effecting rapid (~1 sec) neutrophil adhesion that is regulated by the size and frequency of clustering.
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