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4
1 Integrin/VCAM-1 Interaction Activates L2 Integrin-Mediated Adhesion to ICAM-1 in Human T Cells1
Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto General Hospital Research Institute, Toronto, Canada
Modulation of integrin affinity and/or avidity provides a
regulatory mechanism by which leukocyte adhesion to endothelium is
strengthened or weakened at different stages of emigration. In this
study, we demonstrate that binding of high-affinity
4
1 integrins to VCAM-1 strengthens
L2 integrin-mediated adhesion. The
strength of adhesion of Jurkat cells, a human leukemia T cell line, or
MnCl2-treated peripheral blood T cells to immobilized
chimeric human VCAM-1/Fc, ICAM-1/Fc, or both was quantified using
parallel plate flow chamber leukocyte detachment assays in which shear
stress was increased incrementally (0.5–30 dynes/cm2). The
strength of adhesion to VCAM-1 plus ICAM-1, or to a 40-kDa fragment of
fibronectin containing the CS-1 exon plus ICAM-1, was greater than the
sum of adhesion to each molecule alone. Treatment of Jurkat or blood T
cells with soluble cross-linked VCAM-1/Fc or HP2/1, a mAb to
4, significantly increased adhesion to ICAM-1. These
treatments induced clustering of L2
integrins, but not the high-affinity 2 integrin epitope
recognized by mAb 24. Up-regulated adhesion to ICAM-1 was abolished by
cytochalasin D, an inhibitor of cytoskeletal rearrangement. Taken
together, our data suggest that the binding of VCAM-1 or fibronectin to
41 integrins initiates a signaling
pathway that increases 2 integrin avidity but not
affinity. A role for the cytoskeleton is implicated in this
process.
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