scholarly journals ADP-ribosylation Factor Functions Synergistically with a 50-kDa Cytosolic Factor in Cell-free Activation of Human Neutrophil Phospholipase D

1995 ◽  
Vol 270 (6) ◽  
pp. 2431-2434 ◽  
Author(s):  
J. David Lambeth ◽  
Jong-Young Kwak ◽  
Edward P. Bowman ◽  
David Perry ◽  
David J. Uhlinger ◽  
...  
Keyword(s):  
Phospholipase D ◽  
Human Neutrophil ◽  
Adp Ribosylation ◽  
Adp Ribosylation Factor ◽  
Cytosolic Factor

scholarly journals Didecanoyl phosphatidylcholine is a superior substrate for assaying mammalian phospholipase D

1996 ◽  
Vol 319 (3) ◽  
pp. 861-864 ◽  
Author(s):  
Anne M VINGGAARD ◽  
Torben JENSEN ◽  
Clive P. MORGAN ◽  
Shamshad COCKCROFT ◽  
Harald S. HANSEN
Keyword(s):  
Detection Limit ◽  
Phospholipase D ◽  
Cultured Cells ◽  
Human Neutrophils ◽  
Dipalmitoyl Phosphatidylcholine ◽  
Mammalian Tissues ◽  
Radioactive Concentration ◽  
Adp Ribosylation Factor ◽  
Cytosolic Factor ◽  
Assay Conditions

Phospholipase D (PLD) activity in crude or solubilized membranes from mammalian tissues is difficult to detect with the current assay techniques, unless a high radioactive concentration of substrate and/or long incubation times are employed. Generally, the enzyme has to be extracted and partially purified on one column before easy detection of activity. Furthermore, PLD activity in cultured cells can only be detected by the available assay techniques in the presence of guanosine 5´-[γ-thio]triphosphate (GTP[S]) and a cytosolic factor [usually ADP-ribosylation factor (Arf)]. In this paper we report that the use of didecanoyl phosphatidylcholine (C10-PC) in mammalian PLD assays considerably increases the detection limit. C10-PC was compared with the commonly used dipalmitoyl phosphatidylcholine (C16-PC) as a substrate for PLD activity from membranes of human neutrophils, human placenta and pig brain, and from placental cytosol. C10-PC was superior to C16-PC by a factor of 2–28 depending on assay conditions and tissue, and it allowed the detection of GTP[S]-and Arf-stimulated PLD activity without addition of phosphatidylinositol 4,5-bisphosphate.

scholarly journals ADP-ribosylation Factor Proteins Mediate Agonist-induced Activation of Phospholipase D

1998 ◽  
Vol 273 (46) ◽  
pp. 30836-30841 ◽  
Author(s):  
Kuntala Shome ◽  
Yimin Nie ◽  
Guillermo Romero
Keyword(s):  
Phospholipase D ◽  
Adp Ribosylation ◽  
Adp Ribosylation Factor

scholarly journals Nuclear ADP-ribosylation Factor (ARF)- and Oleate-dependent Phospholipase D (PLD) in Rat Liver Cells

1997 ◽  
Vol 272 (8) ◽  
pp. 5208-5213 ◽  
Author(s):  
Yoshiko Banno ◽  
Keiko Tamiya-Koizumi ◽  
Hideko Oshima ◽  
Akemi Morikawa ◽  
Shonen Yoshida ◽  
...  
Keyword(s):  
Rat Liver ◽  
Phospholipase D ◽  
Liver Cells ◽  
Adp Ribosylation ◽  
Rat Liver Cells ◽  
Adp Ribosylation Factor

scholarly journals 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

1997 ◽  
Vol 325 (3) ◽  
pp. 581-585 ◽  
Author(s):  
C. P. MORGAN ◽  
H. SENGELOV ◽  
J. WHATMORE ◽  
N. BORREGAARD ◽  
S. COCKCROFT
Keyword(s):  
Plasma Membrane ◽  
Phospholipase D ◽  
Small Gtpases ◽  
Human Neutrophils ◽  
Secretory Vesicles ◽  
Rho Proteins ◽  
Adp Ribosylation ◽  
Activated Neutrophils ◽  
Adp Ribosylation Factor ◽  
Stimulation Of

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.

ADP-Ribosylation Factor-Dependent Phospholipase D Activation by VPAC Receptors and a PAC1 Receptor Splice Variant

2001 ◽  
Vol 59 (6) ◽  
pp. 1523-1532 ◽  
Author(s):  
Derek A. McCulloch ◽  
Eve M. Lutz ◽  
Melanie S. Johnson ◽  
Derek N. Robertson ◽  
Chris J. MacKenzie ◽  
...  
Keyword(s):  
Phospholipase D ◽  
Splice Variant ◽  
Pac1 Receptor ◽  
Adp Ribosylation ◽  
Vpac Receptors ◽  
Adp Ribosylation Factor

ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity

Cell ◽  
1993 ◽  
Vol 75 (6) ◽  
pp. 1137-1144 ◽  
Author(s):  
H.Alex Brown ◽  
Stephen Gutowski ◽  
Carolyn R. Moomaw ◽  
Clive Slaughter ◽  
Paul C. Sternwels
Keyword(s):  
Phospholipase D ◽  
Regulatory Protein ◽  
Adp Ribosylation ◽  
Adp Ribosylation Factor

scholarly journals Activation of exocytosis by cross-linking of the IgE receptor is dependent on ADP-ribosylation factor 1-regulated phospholipase D in RBL-2H3 mast cells: evidence that the mechanism of activation is via regulation of phosphatidylinositol 4,5-bisphosphate synthesis

2000 ◽  
Vol 346 (1) ◽  
pp. 63-70 ◽  
Author(s):  
Gemma WAY ◽  
Niamh O'LUANAIGH ◽  
Shamshad COCKCROFT
Keyword(s):  
Mast Cells ◽  
Phospholipase D ◽  
Protein Interactions ◽  
Cross Linking ◽  
Ige Receptor ◽  
Local Synthesis ◽  
Adp Ribosylation ◽  
Phosphatidylinositol Transfer ◽  
Lipid Protein Interactions ◽  
Adp Ribosylation Factor

The physiological stimulus to exocytosis in mast cells is the cross-linking of the high-affinity IgE receptor, FcϵR1, with antigen. We demonstrate a novel function for ADP-ribosylation factor 1 (ARF1) in the regulation of antigen-stimulated secretion using cytosol-depleted RBL-2H3 mast cells for reconstitution of secretory responses. When antigen is used as the stimulus, ARF1 also reconstitutes phospholipase D activation. Using ethanol to divert the phosphatidic acid (the product of phospholipase D activity) to phosphatidylethanol causes inhibition of ARF1-reconstituted secretion. In addition. ARF1 causes an increase in phosphatidylinositol 4,5-bisphosphate (PIP2) levels at the expense of phosphatidylinositol 4-monophosphate. The requirement for PIP2 in exocytosis was confirmed by using phosphatidylinositol transfer protein (PITPα) to increase PIP2 levels. Exocytosis, restored by either ARF1 or PITPα, was inhibited when PIP2 levels were depleted by phospholipase C∆1. We conclude that the function of ARF1 and PITPα is to increase the local synthesis of PIP2, the function of which in exocytosis is likely to be linked to lipid-protein interactions, whereby recruitment of key components of the exocytotic machinery are targeted to the appropriate membrane compartment.

Sign in / Sign up

Export Citation Format

Share Document