An essential role for phospholipase D in the recruitment of vesicle amine transport protein-1 to membranes in human neutrophils

2011 ◽  
Vol 81 (1) ◽  
pp. 144-156 ◽  
Author(s):  
Delphine Faugaret ◽  
François C. Chouinard ◽  
Danielle Harbour ◽  
Mohammed-Amine El azreq ◽  
Sylvain G. Bourgoin
Keyword(s):  
Phospholipase D ◽  
Essential Role ◽  
Transport Protein ◽  
Human Neutrophils

scholarly journals Arachidonic acid activates phospholipase D in human neutrophils; essential role of endogenous leukotriene B4and inhibition by adenosine A2Areceptor engagement

2003 ◽  
Vol 73 (4) ◽  
pp. 530-539 ◽  
Author(s):  
Sonya Grenier ◽  
Nicolas Flamand ◽  
Julie Pelletier ◽  
Paul H. Naccache ◽  
Pierre Borgeat ◽  
...  
Keyword(s):  
Arachidonic Acid ◽  
Phospholipase D ◽  
Essential Role ◽  
Human Neutrophils

scholarly journals The Antibacterial Activity of Human Neutrophils and Eosinophils Requires Proton Channels but Not BK Channels

2006 ◽  
Vol 127 (6) ◽  
pp. 659-672 ◽  
Author(s):  
Jon K. Femling ◽  
Vladimir V. Cherny ◽  
Deri Morgan ◽  
Balázs Rada ◽  
A. Paige Davis ◽  
...  
Keyword(s):  
Nadph Oxidase ◽  
Respiratory Burst ◽  
Essential Role ◽  
Outward Current ◽  
Bk Channels ◽  
Bk Channel ◽  
Human Neutrophils ◽  
H2o2 Production ◽  
Proton Channels ◽  
Voltage Gated

Electrophysiological events are of central importance during the phagocyte respiratory burst, because NADPH oxidase is electrogenic and voltage sensitive. We investigated the recent suggestion that large-conductance, calcium-activated K+ (BK) channels, rather than proton channels, play an essential role in innate immunity (Ahluwalia, J., A. Tinker, L.H. Clapp, M.R. Duchen, A.Y. Abramov, S. Page, M. Nobles, and A.W. Segal. 2004. Nature. 427:853–858). In PMA-stimulated human neutrophils or eosinophils, we did not detect BK currents, and neither of the BK channel inhibitors iberiotoxin or paxilline nor DPI inhibited any component of outward current. BK inhibitors did not inhibit the killing of bacteria, nor did they affect NADPH oxidase-dependent degradation of bacterial phospholipids by extracellular gIIA-PLA2 or the production of superoxide anion (\batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(\mathrm{O}_{2^{.}}^{{-}}\) \end{document}). Moreover, an antibody against the BK channel did not detect immunoreactive protein in human neutrophils. A required role for voltage-gated proton channels is demonstrated by Zn2+ inhibition of NADPH oxidase activity assessed by H2O2 production, thus validating previous studies showing that Zn2+ inhibited \batchmode \documentclass[fleqn,10pt,legalpaper]{article} \usepackage{amssymb} \usepackage{amsfonts} \usepackage{amsmath} \pagestyle{empty} \begin{document} \(\mathrm{O}_{2^{.}}^{{-}}\) \end{document} production when assessed by cytochrome c reduction. In conclusion, BK channels were not detected in human neutrophils or eosinophils, and BK inhibitors did not impair antimicrobial activity. In contrast, we present additional evidence that voltage-gated proton channels serve the essential role of charge compensation during the respiratory burst.

scholarly journals Monosodium urate-crystal-stimulated phospholipase D in human neutrophils

1999 ◽  
Vol 337 (2) ◽  
pp. 185 ◽  
Author(s):  
Josée MARCIL ◽  
Danielle HARBOUR ◽  
Martin G. HOULE ◽  
Paul H. NACCACHE ◽  
Sylvain BOURGOIN
Keyword(s):  
Phospholipase D ◽  
Human Neutrophils ◽  
Monosodium Urate ◽  
Urate Crystal

Association between leukotriene B4-induced phospholipase D activation and degranulation of human neutrophils

1993 ◽  
Vol 46 (1) ◽  
pp. 139-148 ◽  
Author(s):  
Zhou Han-Liang ◽  
Marie Chabot-Fletcher ◽  
James J. Foley ◽  
Henry M. Sarau ◽  
Maritsa N. Tzimas ◽  
...  
Keyword(s):  
Phospholipase D ◽  
Leukotriene B4 ◽  
Human Neutrophils

Biochemical characterization of phospholipase D activity from human neutrophils

1989 ◽  
Vol 186 (3) ◽  
pp. 717-724 ◽  
Author(s):  
Jesus BALSINDE ◽  
Emilio DIEZ ◽  
Belen FERNANDEZ ◽  
Faustino MOLLINEDO
Keyword(s):  
Phospholipase D ◽  
Biochemical Characterization ◽  
Human Neutrophils

scholarly journals The temporal relationship between phospholipase activation, diradylglycerol formation and superoxide production in the human neutrophil

1990 ◽  
Vol 271 (1) ◽  
pp. 209-213 ◽  
Author(s):  
N T Thompson ◽  
J E Tateson ◽  
R W Randall ◽  
G D Spacey ◽  
R W Bonser ◽  
...  
Keyword(s):  
Phospholipase D ◽  
Human Neutrophil ◽  
Second Messengers ◽  
Superoxide Production ◽  
Human Neutrophils ◽  
Inositol 1,4,5 Trisphosphate ◽  
Phosphatidate Phosphohydrolase ◽  
Time Courses ◽  
Rapid Activation ◽  
Stimulation Of

Fluctuations in the amounts of choline, inositol 1,4,5-trisphosphate (IP3) and diradylglycerol have been used to monitor phospholipase activation in the human neutrophil. Stimulation of human neutrophils by formylmethionyl-leucylphenylalanine (fMet-Leu-Phe) resulted in a rapid activation of both phosphatidylinositol 4,5-bisphosphate breakdown by phospholipase C and phosphatidylcholine breakdown by phospholipase D. Diradylglycerol accumulation occurred more slowly than that of either choline or IP3 and was inhibited by 30 mM-butanol, suggesting that the bulk was derived from the phospholipase D pathway via phosphatidate phosphohydrolase. Consistent with this is the observation that choline and diradylglycerol are produced in similar amounts. 1,2-Diacylglycerol (DAG) and 1-O-alkyl-2-acyl-sn-glycerol species accumulated with different time courses, indicating that one or more steps in the phospholipase D pathway was selective for the diacyl species. Superoxide production by fMet-Leu-Phe-stimulated neutrophils paralleled DAG accumulation over the first 5 min, but thereafter this production stopped, despite the fact that DAG remained elevated. We conclude that DAG derived from the phospholipase D pathway is only one of the second messengers important in controlling this functional response.

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 Protein kinase C activity is not involved in N-formylmethionyl-leucyl-phenylalanine-induced phospholipase D activation in human neutrophils, but is essential for concomitant NADPH oxidase activation: studies with a staurosporine analogue with improved selectivity for protein kinase C

1993 ◽  
Vol 292 (3) ◽  
pp. 781-785 ◽  
Author(s):  
G C Kessels ◽  
K H Krause ◽  
A J Verhoeven
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Nadph Oxidase ◽  
Phospholipase D ◽  
Respiratory Burst ◽  
Feedback Inhibition ◽  
Human Neutrophils ◽  
Kinase C ◽  
Pkc Activation

Stimulation of human neutrophils by the receptor agonist N-formylmethionyl-leucyl-phenylalanine (fMLP) results in a respiratory burst, catalysed by an NADPH oxidase. Concomitantly, phospholipase D (PLD) is activated. To investigate the role of protein kinase C (PKC) in these neutrophil responses, we have compared the effects of staurosporine and a structural analogue of staurosporine (cgp41251), that reflects a higher selectivity towards PKC [Meyer, Regenass, Fabbro, Alteri, Rösel, Müller, Caravatti and Matter (1989) Int. J. Cancer 43, 851-856]. Both staurosporine and cgp41251 dose-dependently inhibited the production of superoxide induced by phorbol 12-myristate 13-acetate (PMA). Both compounds also caused inhibition of the fMLP-induced respiratory burst, but with a lower efficacy during the initiation phase of this response. This latter observation cannot be taken as evidence against PKC involvement in the activation of the respiratory burst, because pretreatment of neutrophils with ionomycin before PMA stimulation also results in a lower efficacy of inhibition. Activation of PLD by fMLP was enhanced in the presence of staurosporine, but not in the presence of cgp41251. Enhancement of PLD activation was also observed in the presence of H-89, an inhibitor of cyclic-AMP-dependent protein kinase (PKA). Both staurosporine and H-89 reversed the dibutyryl-cyclic-AMP-induced inhibition of PLD activation, whereas cgp41251 was without effect. These results indicate that the potentiating effect of staurosporine on PLD activation induced by fMLP does not reflect a feedback inhibition by PKC activation, but instead a feedback inhibition by PKC activation. Taken together, our results indicate that in human neutrophils: (i) PKC activity is not essential for fMLP-induced activation of PLD; (ii) PKC activity does play an essential role in the activation of the respiratory burst by fMLP, other than mediating or modulating PLD activation; (iii) there exists a negative-feedback mechanism on fMLP-induced PLD activation by concomitant activation of PKA.

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