Activation of phospholipase D by chemotactic peptide in HL-60 granulocytes

Pai, Jin-Keon; Siegel, Marvín I.; Egan, Robert W.; Billah, M. Motasim

doi:10.1016/0006-291x(88)90528-1

Cited by 160 publications

(60 citation statements)

References 32 publications

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“…Activation of monomeric and heterotrimeric G-proteins results in receptor-mediated stimulation of PLD in several neuronal cell lines (see Klein et al, 1995), canine cortical synaptosomes (Qian & Drewes, 1989), and rat hippocampal slices (Holler et al, 1994). In granulocytes, pre-incubation with pertussis toxin inhibits PLD activity induced by agonists (Pai et al, 1988;Kanaho et al, 1991) but not that induced by phorbol esters (Billah et al, 1989). Similarly, PKC-independent activation of PLD by al-adrenoceptors in neocortex (Llahi & Fain, 1992) or by mGluRs in hippocampus (this study) could be, in part, a G-protein-mediated process.…”

Section: Discussionmentioning

confidence: 99%

“…Thus, in the presence of exogenously added ethanol, PLD preferentially transfers the alcohol rather than water to the phosphatidyl moiety of phosphatidylcholine, producing phosphatidylethanol (PEt) in place of phosphatidic acid. The formation of agonist-induced PEt is generally accepted as a useful marker for PLD activity in intact cells (Pai et al, 1988;Llahi & Fain, 1992 …”

Section: Determination Of Pld Activitymentioning

confidence: 99%

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Pharmacological characterization of metabotropic glutamate receptors coupled to phospholipase D in the rat hippocampus

Pellegrini‐Giampietro

Torregrossa

Moroni

1996

British J Pharmacology

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1 Phospholipase D (PLD) is the key enzyme in a signal transduction pathway leading to the formation of the second messengers phosphatidic acid and diacylglycerol. In order to define the pharmacological profile of PLD-coupled metabotropic glutamate receptors (mGluRs), PLD activity was measured in slices of adult rat brain in the presence of mGluR agonists or antagonists. Activation of the phospholipase C (PLC) pathway by the same agents was also examined. 2 The mGluR-selective agonist (1S,3R)-l-aminocyclopentane-1,3-dicarboxylic acid [(1S,3R)-ACPD] induced a concentration-dependent (10-300 gM) activation of PLD in the hippocampus, neocortex, and striatum, but not in the cerebellum. The effect was particularly evident in hippocampal slices, which were thus used for all subsequent experiments. 3 The rank order of potencies for agonists stimulating the PLD response was: quisqualate>ibotena- reduced PLD activation induced by 1 gM PDBu but not by 100 gM (lS,3R)-ACPD. 6 Our results suggest that PLD-linked mGluRs in rat hippocampus may be distinct from any known mGluR subtype coupled to PLC or adenylyl cyclase. Moreover, they indicate that independent mGluRs coupled to the PLC and PLD pathways exist and that mGluR agonists can stimulate PLD through a PKC-independent mechanism.

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Section: Discussionmentioning

confidence: 99%

Section: Determination Of Pld Activitymentioning

confidence: 99%

Pharmacological characterization of metabotropic glutamate receptors coupled to phospholipase D in the rat hippocampus

Pellegrini‐Giampietro

Torregrossa

Moroni

1996

British J Pharmacology

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“…Addition of short chain, primary alcohols into the media results in their uptake by the cultured cells and subsequent participation in the PLD-mediated transesterification of phospholipids, resulting in the production of the respective phosphatidylalcohols, which are not PAP-1 substrates (29). By competing with water, which is the normal PLD-mediated reaction nucleophile, the primary alcohol inhibits PAP-1 cellular activity by reducing the availability of the substrate phosphatidic acid.…”

Section: Inhibition Of Lps-induced Pge 2 Production and Cox-2 Expressmentioning

confidence: 99%

Lipopolysaccharide-induced Cyclooxygenase-2 Expression in Human U937 Macrophages Is Phosphatidic Acid Phosphohydrolase-1-dependent

Grkovich¹,

Johnson²,

Buczynski

et al. 2006

Journal of Biological Chemistry

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Cyclooxygenase (COX) has two isoforms, COX-1 and -2, which catalyze the key step in the conversion of cellular arachidonic acid into prostaglandins. In recent years, interest in COX-2 has significantly increased since it has been a target for the development of specific non-steroidal anti-inflammatory drugs. We report that COX-2 expression is up-regulated in phorbol ester (phorbol myristate acetate, PMA)-differentiated human U937 macrophage-like cells stimulated with lipopolysaccharide (LPS), whereas COX-1 is not up-regulated. We show that the LPS-induced up-regulation of COX-2 depends on the activity of the Mg ؉2 -dependent phosphatidic acid phosphohydrolase 1 (PAP-1). Inhibition of PAP-1 by bromoenol lactone, propranolol, or ethanol resulted in a decrease in LPS-induced COX-2 mRNA transcript production, COX-2 protein expression, and prostaglandin E 2 release from U937 macrophages. To ensure that these results did not arise because of PMA treatment of the U937 cells, similar experiments were conducted with the P388D 1 cell line, which does not require PMA differentiation. LPS increased the levels of endogenous cellular diacylglycerol (DAG) within 2 min of stimulation. This increase was observed to be sensitive to the PAP-1 inhibitors. Furthermore, phosphatidic acid phosphohydrolase activity assays showed that the bromoenol lactone-sensitive PAP-1 activity was translocated from the cytosolic fraction to the membrane fraction within 2 min of LPS exposure. Finally, DAG add-back experiments demonstrate that LPS-induced COX-2 expression is enhanced by the addition of exogenous DAG.

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“…phosphatidylethanol or phosphatidylpropanol) [1,2]. The production of phosphatidylalcohol in intact cells (in the presence of a primary alcohol) appears to be exclusively mediated by phospholipase D [3,4]. In contrast, the natural phospholipase D product phosphatidic acid can also be produced by alternative pathways (such as de novo synthesis and by diacylglycerol kinase); moreover, once produced, phosphatidic acid is likely to be quickly metabolized.…”

Section: Introductionmentioning

confidence: 99%

“…We have recently utilized phosphatidylethanol production to demonstrate the activation of phospholipase D by the phorbol ester TPA in NGlO%15 cells [5], and by gonadotropin-releasing hormone in ovarian granulosa cells [6]. Agonist-activated production of phosphatidylethanol by phospholipase D was similarly shown in HL-60 cells [3,4,7], hepatocytes [8,9], and platelets [lo]. In addition, evidence that cell surface receptors may couple with phospholipase D via a guanine [8,9,1 l] suggests that the activation of phospholipase D represents a novel signal transduction pathway.…”

Section: Introductionmentioning

confidence: 99%

Phospholipase D activation by the mitogens platelet‐derived growth factor and 12‐O‐tetradecanoylphorbol 13‐acetate in NIH‐3T3 cells

Ben‐Av

Liscovitch

1989

FEBS Letters

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The effect of mitogens on phospholipase D activity was investigated in NIH-3T3 fibroblasts by measuring the accumulation of phosphatidylpropan-01, produced by phospholipase D phosphatidyl transferase activity when I-propanol acts as the phosphatidyl group acceptor. Platelet-derived growth factor (PDGF) and 120tetradecanoylphorbol13-acetate (TPA) stimulated phosphatidylpropanol production by the cells. The dose-response relationships for activation of phospholipase D and stimulation of thymidine incorporation by PDGF and TPA were comparable. The possibility that activation of phospholipase D is utilized by mitogens as a trans-membrane pathway for signalling cell growth is discussed.

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Activation of phospholipase D by chemotactic peptide in HL-60 granulocytes

Cited by 160 publications

References 32 publications

Pharmacological characterization of metabotropic glutamate receptors coupled to phospholipase D in the rat hippocampus

Pharmacological characterization of metabotropic glutamate receptors coupled to phospholipase D in the rat hippocampus

Lipopolysaccharide-induced Cyclooxygenase-2 Expression in Human U937 Macrophages Is Phosphatidic Acid Phosphohydrolase-1-dependent

Phospholipase D activation by the mitogens platelet‐derived growth factor and 12‐O‐tetradecanoylphorbol 13‐acetate in NIH‐3T3 cells

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