ADP-ribosylation-factor-regulated phospholipase D activity localizes to secretory vesicles and mobilizes to the plasma membrane following N-formylmethionyl-leucyl-phenylalanine stimulation of human neutrophils.
Phospholipase D (PLD) is responsible for the hydrolysis of phosphatidylcholine to produce phosphatidic acid and choline. Human neutrophils contain PLD activity which is regulated by the small GTPases, ADP-ribosylation factor (ARF) and Rho proteins. In this study we have examined the subcellular localization of the ARF-regulated PLD activity in non-activated neutrophils and cells 'primed' with N-formylmethionyl-leucyl-phenylalanine (fMetLeuPhe). We report that PLD activity is localized at the secretory vesicles in control cells and is mobilized to the plasma membrane upon stimulation with fMetLeuPhe. We conclude that the ARF-regulated PLD activity is translocated to the plasma membrane by secretory vesicles upon stimulation of neutrophils with fMetLeuPhe in inflammatory/priming doses. We propose that this relocalization of PLD is important for the subsequent events occurring during neutrophil activation.
Morgan
C P
CP
Department of Physiology, University College London, London WC1E 6JJ, U.K.
Sengelov
H
H
Whatmore
J
J
Borregaard
N
N
Cockcroft
S
S
D020727:ADP-Ribosylation Factors; D002458:Cell Fractionation; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D004586:Electrophoresis / Q000379:methods; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006801:Humans; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology*; D018375:Neutrophil Activation; D009504:Neutrophils / Q000187:drug effects* / Q000276:immunology / Q000378:metabolism; D010739:Phospholipase D / Q000378:metabolism*
D009240:N-Formylmethionine Leucyl-Phenylalanine; D010739:Phospholipase D; D019204:GTP-Binding Proteins; D020727:ADP-Ribosylation Factors