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Speros Martel Section of Leukocyte Biology, Baylor College of Medicine, Houston, TX 77030; and
Institute of Cell Biology, Zentrum für Molekular Biologie der Entzündung, University of Münster, Münster, Germany
On inflamed endothelium selectins support neutrophil capture and
rolling that leads to firm adhesion through the activation and binding
of ß2 integrin. The primary mechanism of cell activation
involves ligation of chemotactic agonists presented on the endothelium.
We have pursued a second mechanism involving signal transduction
through binding of selectins while neutrophils tether in shear flow. We
assessed whether neutrophil rolling on E-selectin led to cell
activation and arrest via ß2 integrins. Neutrophils were
introduced into a parallel plate flow chamber having as a substrate an
L cell monolayer coexpressing E-selectin and ICAM-1 (E/I). At shears
0.1 dyne/cm2, neutrophils rolled on the E/I. A step
increase to 4.0 dynes/cm2 revealed that 
60% of the
interacting cells remained firmly adherent, as compared with 10% on
L cells expressing E-selectin or ICAM-1 alone. Cell arrest was
dependent on application of shear and activation of Mac-1 and LFA-1 to
bind ICAM-1. Firm adhesion was inhibited by blocking E-selectin,
L-selectin, or PSGL-1 with Abs and by inhibitors to the
mitogen-activated protein kinases. A chimeric soluble E-selectin-IgG
molecule specifically bound sialylated ligands on neutrophils and
activated adhesion that was also inhibited by blocking the
mitogen-activated protein kinases. We conclude that neutrophils rolling
on E-selectin undergo signal transduction leading to activation of cell
arrest through ß2 integrins binding to
ICAM-1.
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