Granulocyte-macrophage colony-stimulating factor primes phospholipase D activity in human nerutrophils in vitro: Role of calcium, G-proteins and tyrosine kinases

Bourgoin, Sylvain G.; Pe, Poubelle; Liao, NW; Umezawa, Kazuo; Borgeat, Pierre; Naccache, Paul H.

doi:10.1016/0898-6568(92)90018-4

Cited by 42 publications

(20 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, the receptor for the lipid chemoattractant PAF is expressed exclusively in the plasma membrane (33), and despite this, TNF-␣ also primes the PAF-induced neutrophil response (33). Priming may thus be achieved without receptor mobilization; additional suggested mechanisms include increased membrane expression or translocation of NADPH oxidase components (49), alterations of intracellular signaling pathways, increased protein phosphorylation (50), phospholipase activity (51), intracellular Ca 2ϩ changes (52), cross talk between Ca 2ϩ increase and tyrosine phosphorylation (53), altered assembly of the oxidase (54), and proteolytic processing of cell surface proteins (55). Multiple mechanisms may be involved in TNF-␣-induced priming, and since no antibody is available that recognizes surface-expressed FFA2Rs, it is not possible to conclusively determine the degree of mobilization of the FFA2R during priming.…”

Section: Discussionmentioning

confidence: 99%

The Neutrophil Response Induced by an Agonist for Free Fatty Acid Receptor 2 (GPR43) Is Primed by Tumor Necrosis Factor Alpha and by Receptor Uncoupling from the Cytoskeleton but Attenuated by Tissue Recruitment

Björkman

Mårtensson

Winther

et al. 2016

Molecular and Cellular Biology

View full text Add to dashboard Cite

c Ligands with improved potency and selectivity for free fatty acid receptor 2 (FFA2R) have become available, and we here characterize the neutrophil responses induced by one such agonist (Cmp1) and one antagonist (CATPB). Cmp1 triggered an increase in the cytosolic concentration of Ca 2؉ , and the neutrophils were then desensitized to Cmp1 and to acetate, a naturally occurring FFA2R agonist. The antagonist CATPB selectively inhibited responses induced by Cmp1 or acetate. The activated FFA2R induced superoxide anion secretion at a low level in naive blood neutrophils. This response was largely increased by tumor necrosis factor alpha (TNF-␣) in a process associated with a recruitment of easily mobilizable granules, but neutrophils recruited to an aseptic inflammation in vivo were nonresponding. Superoxide production induced by Cmp1 was increased in latrunculin Atreated neutrophils, but no reactivation of desensitized FFA2R was induced by this drug, suggesting that the cytoskeleton is not directly involved in terminating the response. The functional and regulatory differences between the receptors that recognize short-chain fatty acids and formylated peptides, respectively, imply different roles of these receptors in the orchestration of inflammation and confirm the usefulness of a selective FFA2R agonist and antagonist as tools for the exploration of the precise role of the FFA2R.

show abstract

Section: Discussionmentioning

confidence: 99%

The Neutrophil Response Induced by an Agonist for Free Fatty Acid Receptor 2 (GPR43) Is Primed by Tumor Necrosis Factor Alpha and by Receptor Uncoupling from the Cytoskeleton but Attenuated by Tissue Recruitment

Björkman

Mårtensson

Winther

et al. 2016

Molecular and Cellular Biology

View full text Add to dashboard Cite

show abstract

“…PLD is known to be activated by at least two distinct pathways: a tyrosine kinasemediated pathway and a protein kinase C-mediated pathway (10 -13). Stimulation of PLD by agonists such as fMLP is pertussis toxin-sensitive, but activation of protein kinase C by phorbol esters induces a PLD response that is pertussis toxininsensitive (14,15). Increasing tyrosine phosphorylation by use of inhibitors of tyrosine phosphatases also causes a pertussis toxin-insensitive activation of PLD.…”

mentioning

confidence: 95%

“…The biological effects of the chemotactic peptide fMLP include the activation of PLD (7,15). Therefore, the effects of fMLP on the activity of the membrane-associated PLD were examined next.…”

Section: Potentiation Of Pld Activity In Membrane Fractions Of Hl-60 mentioning

confidence: 99%

ADP-ribosylation Factor Translocation Correlates with Potentiation of GTPγS-stimulated Phospholipase D Activity in Membrane Fractions of HL-60 Cells

Houle

Kahn

Naccache

et al. 1995

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Phospholipase D (PLD) activation by guanine nucleotides requires protein cofactors from both the membrane and the cytosol. The small GTP-binding protein ADP-ribosylation factor (ARF) has been established as one important component of PLD activation. By stimulating HL-60 cells with various agonists and then isolating the membrane fraction and assaying PLD activity in the presence and absence of GTP␥S, we observed that fMet-Leu-Phe (fMLP) and phorbol esters induced a potentiation of GTP␥S-stimulated PLD activity in the membrane fractions of these cells. Inactive phorbol esters induced no such potentiation. Both fMLP and active phorbol esters induced a 2-3-fold increase in GTP␥S-stimulated PLD in HL-60 membranes. Membranes derived from stimulated HL-60 cells contained 60 -70% more ARF as compared with membranes derived from control cells. Membrane contents of ARF were assessed by Western blotting with the anti-ARF monoclonal antibody 1D9 followed by densitometric evaluation. Therefore, ARF translocation correlates with the potentiation of the GTP␥S-stimulated PLD activity. The effect on PLD activity and ARF membrane content achieved through fMLP stimulation was greatly enhanced by prior treatment of the cells with cytochalasin B. Membranes derived from control and fMLP-stimulated cells were assayed for PLD activity in the presence of exogenous ARF and a 50-kDa fraction known to contain elements implicated in PLD activation. The ability of ARF and the 50-kDa fraction to enhance GTP␥S-sensitive PLD activity was significantly reduced when the membranes were derived from fMLP-stimulated cells. The data indicate that, in addition to ARF, elements of the 50-kDa PLD-inducing factors were likely already translocated to the membranes upon stimulation. We propose that ARF, upon stimulation with agonists such as fMLP or phorbol esters, is translocated to the membrane and in concert with other protein components of the 50-kDa fraction enhances PLD activity.Neutrophils exercise their functions in primary host defense against pathogens through different effector systems including superoxide generation and granular secretion. It is now generally accepted that phospholipases are implicated in the generation of second messengers essential to these effector systems (1). Phospholipase C catalyzes the hydrolysis of phosphatidylinositol 4,5-biphosphate into inositol 1,4,5-triphosphate and diradylglycerol; two important second messengers. PLD 1 hydrolyzes phosphatidylcholine into choline and phosphatidic acid. Phosphatidic acid is possibly involved in superoxide anion production by inducing the dissociation of the Rac-GDP/GTP dissociation inhibitor complex (2), thereby releasing Rac, which can then assemble the NADPH oxidase complex (e.g. for review see Ref.3). Phosphatidic acid can also be converted to diradylglycerol by the enzyme phosphatidic acid phosphatase. Diradylglycerol derived from the PLD and phospholipase C pathways has been shown to cause different patterns of protein kinase C isoform translocation and to have distinct cell...

show abstract

“…3A and 4A). Erbstatin, a tyrosine kinase inhibitor related to MDHC, has previously been shown to reduce fMLP-induced PLD activation and tyrosine phosphorylation in human granulocytes [12]. ST-638 inhibited the GTP␥S-sensitive membraneassociated PLD activation induced by V 4ϩ -OOH (Fig.…”

Section: Anti-arf Anti-rhoa and Anti-pkc Immunoblottingmentioning

confidence: 99%

“…Receptormediated PLD activation is sensitive to tyrosine kinase inhibitors, suggesting a role for tyrosine phosphorylation in PLD regulation [11][12][13]. Furthermore, peroxides of vanadate, which induce hyperphosphorylation of tyrosine residues, significantly increased PLD activity in granulocytes [14].…”

Section: Introductionmentioning

confidence: 99%

Tyrosine kinase-regulated small GTPase translocation and the activation of phospholipase D in HL60 granulocytes

Houle

Naccache

Bourgoin

1999

Journal of Leukocyte Biology

Self Cite

View full text Add to dashboard Cite

We focus on the mechanisms of regulation of phospholipase D (PLD) activity. Three agonists known to stimulate PLD activity, fMet-LeuPhe (fMLP), phorbol 12-myristate 13-acetate (PMA) and V 4؉ -OOH, induced a differential translocation of ADP-ribosylation factor (ARF), RhoA, and protein kinase C␣ (PKC␣), all cofactors for PLD activation. Whereas fMLP recruited all three proteins to membranes, V 4؉ -OOH only elicited RhoA translocation and PMA induced ARF and PKC␣ translocation. Three tyrosine kinases inhibitors, ST-638, methyl 2,5-dihydroxycinnamate, and genistein reduced fMLP-stimulated PLD activity by up to 80%. Furthermore, tyrosine kinase inhibitors reduced the fMLP-induced increase of GTP␥S-stimulated PLD activity in membranes and recruitment of ARF, RhoA, and PKC␣ to the membrane fraction. The data suggest that a tyrosine phosphorylation event is located upstream of the translocation of ARF, RhoA, and PKC␣ in the signaling pathway leading to PLD activation by fMLP. RO 31-8220, a specific inhibitor of PKC, reduced PMA-induced PLD activity by 80% in intact HL60 granulocytes but enhanced fMLP-stimulated PLD activity by 60%. Although PMA alone had no effect on RhoA recruitment to the membrane fraction, in the presence of RO 31-8220 the levels of membrane-bound RhoA were increased. The levels of membrane-bound ARF and PKC␣ were unaffected by RO 31-8220 during PMA stimulation. In contrast, fMLP-induced recruitment of ARF and RhoA was insensitive to RO 31-8220 but PKC␣ translocation was increased. We propose that RhoA translocation may be regulated by PKC in an ATPindependent manner. Furthermore, increased fMLP-induced PKC␣ translocation in the presence of RO 31-8220 may partially account for the synergistic activation of PLD observed when both fMLP and RO 31-8220 are used together in intact HL60 cells.

show abstract

Granulocyte-macrophage colony-stimulating factor primes phospholipase D activity in human nerutrophils in vitro: Role of calcium, G-proteins and tyrosine kinases

Cited by 42 publications

References 50 publications

The Neutrophil Response Induced by an Agonist for Free Fatty Acid Receptor 2 (GPR43) Is Primed by Tumor Necrosis Factor Alpha and by Receptor Uncoupling from the Cytoskeleton but Attenuated by Tissue Recruitment

The Neutrophil Response Induced by an Agonist for Free Fatty Acid Receptor 2 (GPR43) Is Primed by Tumor Necrosis Factor Alpha and by Receptor Uncoupling from the Cytoskeleton but Attenuated by Tissue Recruitment

ADP-ribosylation Factor Translocation Correlates with Potentiation of GTPγS-stimulated Phospholipase D Activity in Membrane Fractions of HL-60 Cells

Tyrosine kinase-regulated small GTPase translocation and the activation of phospholipase D in HL60 granulocytes

Contact Info

Product

Resources

About