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Published online before print May 22, 2003

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(Journal of Leukocyte Biology. 2003;74:260-269.)
© 2003 by Society for Leukocyte Biology

A role for Syk-kinase in the control of the binding cycle of the ß₂ integrins (CD11/CD18) in human polymorphonuclear neutrophils

Thomas Willeke^*, Jürgen Schymeinsky^*, Peggy Prange, Stefan Zahler^* and Barbara Walzog^*

^* Department of Physiology, Ludwig-Maximilians-Universität München, Germany; and
Department of Physiology, Freie Universität Berlin, Germany

Correspondence: Professor Dr. Barbara Walzog, Ludwig-Maximilians-Universität München, Department of Physiology, Schillerstr. 44, D-80336 München, Germany. E-mail: walzog{at}lrz.uni-muenchen.de

A fine control of ß₂ integrin (CD11/CD18)-mediated firm adhesion of human neutrophils to the endothelial cell monolayer is required to allow ordered emigration. To elucidate the molecular mechanisms that control this process, intracellular protein tyrosine signaling subsequent to ß₂ integrin-mediated ligand binding was studied by immunoprecipitation and Western blotting techniques. The 72-kDa Syk-kinase, which was tyrosine-phosphorylated upon adhesion, was found to coprecipitate with CD18, the ß-subunit of the ß₂ integrins. Moreover, inhibition of Syk-kinase by piceatannol enhanced adhesion and spreading but diminished N-formyl-Met-Leu-Phe-induced chemotactic migration. The enhancement of adhesiveness was associated with integrin clustering, which results in increased integrin avidity. In contrast, piceatannol had no effect on the surface expression or on the affinity of ß₂ integrins. Altogether, this suggests that Syk-kinase controls alternation of ß₂ integrin-mediated ligand binding with integrin detachment.

Key Words: MAC-1 • adhesion • migration

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