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*
Department of Biomedical Engineering, University of Virginia, Charlottesville, VA 22903;
Department of Internal Medicine, University of Michigan and Veterans Affairs Medical Center, Ann Arbor, MI 48105; and
Department of Pathology and Cytometry, Cancer Research and Treatment Center, University of New Mexico Health Sciences Center, Albuquerque, NM 87131
The chemokine IL-8 is found on the luminal side of vascular
endothelial cells, where it is postulated to be immobilized during
inflammation. In this study, we observed that immobilized IL-8 can
stimulate neutrophils to firmly adhere to a substrate containing ICAM-1
in a static adhesion assay. Soluble IL-8 was then perfused over
neutrophils rolling on P-selectin (P-sel) and ICAM-1, confirming that
IL-8 in solution can quickly cause rolling neutrophils to arrest. To
mimic a blood vessel wall with IL-8 expressed on the luminal surface of
endothelial cells, IL-8 was immobilized along with P-sel and ICAM-1 at
defined site densities to a surface. Neutrophils rolled an average of
200 µm on surfaces of P-sel, ICAM-1, and IL-8 before firmly adhering
through ICAM-1-
2 integrin interactions at 2
dynes/cm2 wall shear stress. Increasing the density of IL-8
from 60 to 350 sites/µm2 on the surface decreased by 50%
the average distance and time the neutrophils rolled before becoming
firmly adherent. Temporal dynamics of ICAM-1-2 integrin
interactions of rolling neutrophils following IL-8 exposure suggest the
existence of two classes of 2 integrin-ICAM-1
interactions, a low avidity interaction with a 65% increase in pause
times as compared with P-sel-P-sel glycoprotein ligand-1 interactions,
and a high avidity interaction with pause times 400% greater than the
selectin interactions. Based on the proportionality between IL-8 site
density and time to arrest, it appears that neutrophils may need to
sample a critical number of IL-8 molecules presented by the vessel wall
before forming a sufficient number of high avidity 2
integrin bonds for firm adhesion.
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