Affinity and topography provide for dynamic regulation of b2-integrin-dependent leukocyte adhesion during inflammation

COLL 428

Scott I. Simon, Biomedical Engineering, Biomedical Engineering, University of Cal, Davis, One Shields Ave, 1228 Bainer Hall, Davis, CA 95616
Adhesion of leukocytes is in general maintained at a low level until cell recruitment is triggered during acute inflammation. Leukocytes detect low levels of tissue activation by signaling via G-protein linked chemotactic receptors that in turn activate b2-integrin adhesion receptors (CD18) and capture to ICAM-1, its counter-receptor upregulated on inflamed endothelium. This is deemed a critical step in facilitating cell arrest under the shear force of blood flow. Where and when leukocyte recruitment takes place in the vasculature appears to be a highly controlled process and a prime target for development of anti-inflammatory therapeutics. An allosteric shift in CD18 conformation regulates the affinity of CD18 for ICAM-1. We examined the efficiency of cell capture as a function of the dynamics of chemotactic receptor stimulation, the accompanying increase in CD18 affinity, and correlated this with the membrane distribution of the active conformation of CD18. A fluorescence flow cytometric based assay was developed to detect binding of beads derivitized with recombinant ICAM-1 while fluorescence microscopy was applied to detect receptor topography. We provide evidence that the efficiency of neutrophil capture on ICAM-1 is tightly regulated by the level of chemotactic receptor binding and the topography and lifetime of high affinity CD18
 

Adamson Award Symposium Honoring Dave Allara and Ralph Nuzzo

Division of Colloid and Surface Chemistry
The 225th ACS National Meeting, New Orleans, LA, March 23-27, 2003