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Activation of phospholipase D is an early event in integrin-mediated signalling leading to phagocytosis in human neutrophils

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Abstract

Integrin receptors on human neutrophils mediate adhesion and phagocytosis. These functions are linked to a signal-transduction cascade that rearranges the cytoskeleton. The intention of this study was to clarify how activation of phospholipase D (PLD) is coupled to the complement receptor three (CR3, CD18/CD11b)mediated ingestion process. Carbobenzyloxy-leucine-tyrosine-chloromethylketone (zLYCK) inhibited PLD activation induced by complement-opsonized yeast particles (COYP) by 39%. Phagocytosis of these particles was reduced by zLYCK to the same extent. Anti-CD18-antibodies bound to protein A-positiveStaphylococcus aureus bacteria induced a significant PLD activation. These particles were not ingested which implicates that CR-mediated ingestion per se is not required to induce PLD activity. Cytochalasin B-treatment, which blocks actin reorganization, partly reduced COYP-mediated PLD activity, but had no effect on activity caused by anti-CD 18-coated particles. This excludes activation of PLD to be a secondary event, but rather an early signal in the phagocytic uptake prior to actin reorganization. These data suggest an important and early role for PLD in integrin-mediated phagocytosis.

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Serrander, L., Fällman, M. & Stendahl, O. Activation of phospholipase D is an early event in integrin-mediated signalling leading to phagocytosis in human neutrophils. Inflammation 20, 439–450 (1996). https://doi.org/10.1007/BF01486745

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