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(Journal of Leukocyte Biology. 2000;68:553-560.)
© 2000 by Society for Leukocyte Biology

Engagement of ß₂ integrins induces surface expression of ß₁ integrin receptors in human neutrophils

Department of Physiology and Pharmacology, Karolinska Institutet, S-171 77 Stockholm, Sweden

Correspondence: Joachim Werr, Department of Physiology and Pharmacology, Karolinska Institutet, S-171 77 Stockholm, Sweden. E-mail: joachim.werr{at}fyfa.ki.se

Induction of ß₁ integrin (CD49/CD29) expression in polymorphonuclear leukocytes (PMN) has been shown to be associated with transendothelial migration recently. Yet, ß₁ integrin expression is relatively insensitive to cell activation with soluble agonists, such as N-formyl-methionyl-leucyl-phenylalanine (fMLP). We hypothesized that ß₂ integrins (CD11/CD18), critically involved in PMN adhesion and extravasation, may play a role in regulating ß₁ integrin expression in PMN. Antibody cross-linking of CD18, mimicking adhesion-dependent engagement of ß₂ integrins, resulted in rapid, tyrosine kinase-dependent upregulation of ß₁ integrins. This response was potentiated by simultaneous chemoattractant (fMLP) stimulation of PMN. Moreover, upregulation of ß₁ integrins evoked by CD18 cross-linking was found to support adhesion of fMLP-stimulated PMN to matrix proteins and also was critical for the ability of PMN to migrate in collagen gels in response to a gradient of fMLP. Taken together, these data demonstrate that engagement of ß₂ integrins in human PMN induces ß₁ integrin expression in these cells of significance for their migration in the extravascular tissue. Thus, ß₂ integrins may serve the function to regulate PMN locomotion in extravascular tissue via receptor crosstalk with ß₁ integrins.

Key Words: inflammation • leukocytes • adhesion • extravasation • migration

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