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Volume 271, Number 24, Issue of June 14, 1996 pp. 14623-14630
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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FcRII-mediated Adhesion and Phagocytosis Induce L-Plastin Phosphorylation in Human Neutrophils

(Received for publication, December 8, 1995, and in revised form, April 1, 1996)

From the Division of Infectious Diseases, Washington University School of Medicine, St. Louis, Missouri 63110

L-Plastin is a calcium-regulated actin bundling protein expressed in leukocytes and some transformed cells, which is phosphorylated on serine in response to several different leukocyte-activating stimuli. Adhesion to immune complexes induced L-plastin phosphorylation in neutrophils, as did phagocytosis of IgG-opsonized particles, but insoluble immune complexes in suspension were very inefficient activators of L-plastin phosphorylation. Neutrophils express two IgG Fc receptors, the transmembrane FcRII and the glycan phosphoinositol-linked FcRIIIB. Use of monoclonal antibodies that distinguished the two Fc receptors demonstrated that FcRII ligation was 100-fold more potent at signaling L-plastin phosphorylation than occupancy of FcRIIIB. Depletion of intracellular calcium did not affect FcRII-activated L-plastin phosphorylation, demonstrating that any potential regulation of plastin function by calcium did not affect its phosphorylation. Adhesion to immune complexes caused L-plastin to localize to podosomes, since it colocalized with actin to discrete, punctate Triton X-100-insoluble sites on the adherent neutrophil surface in a pattern indistinguishable from vinculin and -actinin. Nonetheless, localization to podosomes was not required for L-plastin phosphorylation, since both neutrophils from a patient with leukocyte adhesion deficiency (CD18 deficiency) and neutrophils treated with anti-CD18 F(ab)2, which do not form podosomes upon adhesion to immune complexes, phosphorylated L-plastin normally. Indeed, L-plastin was normally phosphorylated in response to adhesion to immune complexes even when the actin cytoskeleton was disrupted with cytochalasin D. We conclude that efficient FcRII-mediated phosphorylation of L-plastin requires cell adhesion but does not require IgG-induced rearrangements of the actin cytoskeleton. These data suggest a model in which plastin phosphorylation and localization to the actin cytoskeleton can act as two distinct mechanisms regulating L-plastin functions in neutrophils adherent to immune complexes.

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