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Inflammation. 1996 Aug;20(4):439-50.

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

Author information

1
Department of Medical Microbiology University of Linköping, Sweden.

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-choloromethylketone (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-positive Staphylococcus 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-CD18-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.

PMID:
8872506
DOI:
10.1007/bf01486745
[Indexed for MEDLINE]

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