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The Journal of Immunology, Vol 159, Issue 8 3968-3975, Copyright © 1997 by American Association of Immunologists

ARTICLES

Role of alpha L beta 2 integrin avidity in transendothelial chemotaxis of mononuclear cells

C Weber, CF Lu, JM Casasnovas and TA Springer
Center for Blood Research, Harvard Medical School, Boston, MA 02115, USA.

The leukocyte integrin alpha L beta 2 (LFA-1) is important in transendothelial migration. Since it is not fully understood how LFA-1 mediates transmigration, we studied the effects of alpha L and beta 2 cytoplasmic domain mutants that alter LFA-1 adhesiveness for intercellular adhesion molecule-1. Monocyte chemotactic protein-1 (MCP- 1) induced LFA-1-dependent transendothelial migration of Jurkat and J- beta 2.7 transfectants coexpressing the MCP-1 receptor CCR2B and wild- type alpha L. No transendothelial chemotaxis was observed with truncation mutants of the alpha L cytoplasmic tail, which rendered LFA- 1 constitutively active or locked LFA-1 in a low avidity state unresponsive to cellular activation. Moreover, transendothelial chemotaxis of lymphoblastoid SLA transfectants was abolished by truncation of the beta 2 cytoplasmic domain, but not by mutation of its TTT motif, which is important in phorbol ester-induced adhesion. These data indicate that transmigration may require both alpha L and beta 2 cytoplasmic domains. We further show that MCP-1-induced transendothelial chemotaxis of PBMC was inhibited by sustained activation of LFA-1 with Mn2+ or a stimulatory mAb to beta 2. Dimeric soluble intercellular adhesion molecule-1 also reduced transendothelial chemotaxis of PBMC. Taken together, our data suggest that transendothelial chemotaxis of mononuclear cells may involve dynamic changes in LFA-1 avidity.


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