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Quantitative In vitro Assay to Measure Neutrophil Adhesion to Activated Primary Human Microvascular Endothelial Cells under Static Conditions
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Published on: August 23, 2013

The adhesion receptor CD-31 can be primed to rapidly adjust the neutrophil cytoskeleton

Ivan Dimitrijevic1, Lena Axelsson, Tommy Andersson

  • 1Experimental Pathology, Department of Laboratory Medicine, Lund University, U-MAS, Malmö, SE-205 02, Sweden.

Biochemical and Biophysical Research Communications
|April 12, 2002
PubMed

The adhesion receptor CD-31 is expressed on neutrophils and endothelial cells and participates in transendothelial migration of neutrophils. Although necessary, information on CD-31-induced signaling and its influence on the shape-forming actin network is scarce. Here, we found that antibody engagement of CD-31 on suspended neutrophils triggered a prompt intracellular Ca(2+) signal, providing the cells had been primed with a chemotactic factor. Inhibition of Src-tyrosine kinases blocked this Ca(2+) signal, but not a fMet-Leu-Phe-induced Ca(2+) signal. Despite the ability of fMet-Leu-Phe to activate Src-tyrosine kinases, it did not per se induce tyrosine phosphorylation of CD-31. However, fMet-Leu-Phe did enable such a phosphorylation following an antibody-induced engagement of CD-31. This clustering also triggered a Ca(2+)-dependent depolymerization of actin and, surprisingly enough, a simultaneous polymerization. The ability of CD-31 to signal dynamic alterations in the cytoskeleton, particularly the Ca(2+)-induced actin depolymerization, further explains how neutrophils can squeeze themselves out between adjacent endothelial cells.

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