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

C P Morgan; H Sengelov; J Whatmore; N Borregaard; S Cockcroft

doi:10.1042/bj3250581

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

C P Morgan, H Sengelov, J Whatmore, N Borregaard, S Cockcroft

81 Citations (Scopus)

Abstract

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.

Original language	English
Journal	Biochemical Journal
Volume	325 ( Pt 3)
Issue number	Pt 3
Pages (from-to)	581-5
Number of pages	5
ISSN	0264-6021
DOIs	https://doi.org/10.1042/bj3250581
Publication status	Published - 1 Aug 1997
Externally published	Yes

Keywords

ADP-Ribosylation Factors
Cell Fractionation
Cell Membrane/drug effects
Electrophoresis/methods
GTP-Binding Proteins/metabolism
Humans
N-Formylmethionine Leucyl-Phenylalanine/pharmacology
Neutrophil Activation
Neutrophils/drug effects
Phospholipase D/metabolism

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10.1042/bj3250581

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Morgan, C. P., Sengelov, H., Whatmore, J., Borregaard, N., & Cockcroft, S. (1997). 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. Biochemical Journal, 325 ( Pt 3)(Pt 3), 581-5. https://doi.org/10.1042/bj3250581

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. / Morgan, C P; Sengelov, H; Whatmore, J et al.
In: Biochemical Journal, Vol. 325 ( Pt 3), No. Pt 3, 01.08.1997, p. 581-5.

Research output: Contribution to journal › Journal article › Research › peer-review

Morgan, CP, Sengelov, H, Whatmore, J, Borregaard, N & Cockcroft, S 1997, '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', Biochemical Journal, vol. 325 ( Pt 3), no. Pt 3, pp. 581-5. https://doi.org/10.1042/bj3250581

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title = "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",

abstract = "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.",

keywords = "ADP-Ribosylation Factors, Cell Fractionation, Cell Membrane/drug effects, Electrophoresis/methods, GTP-Binding Proteins/metabolism, Humans, N-Formylmethionine Leucyl-Phenylalanine/pharmacology, Neutrophil Activation, Neutrophils/drug effects, Phospholipase D/metabolism",

author = "Morgan, {C P} and H Sengelov and J Whatmore and N Borregaard and S Cockcroft",

year = "1997",

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T1 - 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

AU - Morgan, C P

AU - Sengelov, H

AU - Whatmore, J

AU - Borregaard, N

AU - Cockcroft, S

PY - 1997/8/1

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N2 - 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.

AB - 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.

KW - ADP-Ribosylation Factors

KW - Cell Fractionation

KW - Cell Membrane/drug effects

KW - Electrophoresis/methods

KW - GTP-Binding Proteins/metabolism

KW - Humans

KW - N-Formylmethionine Leucyl-Phenylalanine/pharmacology

KW - Neutrophil Activation

KW - Neutrophils/drug effects

KW - Phospholipase D/metabolism

U2 - 10.1042/bj3250581

DO - 10.1042/bj3250581

M3 - Journal article

C2 - 9271075

SN - 0264-6021

VL - 325 ( Pt 3)

SP - 581

EP - 585

JO - Biochemical Journal

JF - Biochemical Journal

IS - Pt 3

ER -