Synergism between phorbol ester and A23187 in Superoxide production by neutrophils

Dale, M. Maureen; Penfield, Adrienne

doi:10.1016/0014-5793(84)80592-x

Cited by 46 publications

(8 citation statements)

References 17 publications

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“…This inhibitory effect of PMA on chemokinesis is in sharp contrast to its previously recognised ability to enhance the effects of neutrophil stimulants on other neutrophil functions such as superoxide generation and enzyme secretion occurring at higher stimulant doses (e.g., Gallin et al, 1978;Kajikawa et al, 1983;O'Flaherty et al, 1984;Dale & Penfield, 1984;Blackwell et al, 1985) and shown in Figure lb and (Nishizuka, 1984). Furthermore, there is a recent report which contradicts the general conclusion from the studies cited above, in that PMA at concentrations of 16 nM or more preincubated with rabbit neutrophils for 1 to 5 min inhibited their subsequent ability to release lysozomal and azurophil enzymes in response to FMLP, C5a and leukotriene B4 (Naccache et al, 1985).…”

Section: Discussioncontrasting

confidence: 46%

Phorbol myristate acetate enhances human polymorphonuclear neutrophil release of granular enzymes but inhibits chemokinesis

Hoult

Nourshargh

1985

British J Pharmacology

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1 The effects of the co-carcinogenic phorbol ester, phorbol myristate acetate (PMA), on N-formylMet-Leu-Phe (FMLP)-induced human polymorphonuclear leukocyte chemokinesis and release of granular lysozyme and ,-glucuronidase were compared with those of the inactive phorbol didecanoate (PDD). 2 Release of the enzymes was enhanced by PMA but was unaffected by PDD which also had no effect on chemokinesis. 3 In contrast, FMLP-induced chemokinesis was completely suppressed by PMA in a dose-dependent fashion (ID50 = 3.5 nM). 4 PMA also inhibited the FMLP-induced increase in cytoplasmic calcium level, measured by the fluorescent indicator quin-2. 5 These and other results suggest that although the diacylglycerol/protein kinase C system is involved in the positive regulation of certain neutrophil functions (degranulation and superoxide generation), if it is very powerfully stimulated, as with PMA, it has inhibitory actions on other neutrophil properties such as motility.

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Section: Discussioncontrasting

confidence: 46%

Phorbol myristate acetate enhances human polymorphonuclear neutrophil release of granular enzymes but inhibits chemokinesis

Hoult

Nourshargh

1985

British J Pharmacology

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“…Role in other cellular functions. In addition to exocytosis and cell division, protein kinase C has been suggested to regulate other cellular functions such as glycogenolysis in hepatocytes [74], superoxide generation in neutrophils [75,76], and contraction of smooth muscle [77]. Presumably, protein kinase C may be related to the regulation of a wide variety of cellular functions that are elicited by extracellular signals listed in Table I, and the role of protein kinase C in transmembrane signaling will be more definitely clarified in the near future.…”

Section: Role Of Protein Kinase C In Transmembrane Signalingmentioning

confidence: 96%

Role of protein kinase C in transmembrane signaling

Takai

Kaibuchi

Tsuda

et al. 1985

J of Cellular Biochemistry

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Many extracellular signals elicit Ca2+ mobilization and diacylglycerol formation in their target cells. Diacylglycerol is derived from the receptor-linked phosphoinositide turnover and serves as a second messenger for the activation of protein kinase C in the presence of Ca2+ and phosphatidylserine. Unique diacylglycerols such as 1-oleoyl-2-acetyl-glycerol, which activate intracellular protein kinase C when added to intact cells, have been synthesized. Tumor-promoting phorbol esters substitute for such diacylglycerols and directly activate protein kinase C in both intact cell and cell-free systems. Under appropriate conditions, the synthetic diacylglycerols and phorbol esters induce protein kinase C activation without Ca2+ mobilization, whereas Ca2+ ionophore A23187 induces Ca2+ mobilization without protein kinase C activation. Using these substances, we have obtained evidence that both protein C and Ca2+ are involved in and play a synergistic role in exocytosis, cell division, and other cellular functions. In this article, the role of protein kinase C in transmembrane signaling is discussed.

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“…We report that PGEz had different effects in each case and the results might provide a clue as to its site of action in stimulus-activation coupling. at 37"C, the reaction was stopped and the amount of 0: generated measured as in [15]. All reagents were obtained from Sigma, except OAG which was synthesized by Dr A. Watts, Biochemistry Department, University of Oxford, England.…”

Section: Abbreviationsmentioning

confidence: 99%

Prostaglandins E₁ and E₂ enhance the stimulation of superoxide release by 1‐oleoyl‐2‐acetylglycerol from human neutrophils

Penfield

Dale

1985

FEBS Letters

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Superoxide release from human neutrophils was stimulated either by receptor activation (using fMet-LeuPhe) or by activating, independently, each of the two pathways considered to be involved in signal transduction -calcium mobilization (using the ionophore, A23 187) and protein kinase C activation (using phorbol myristate acetate or I-oleoyl-2-acetylglycerol).Prostaglandin E, (3 x 10ms M) decreased &let-Leu-Phe-stimmated superoxide release, had no effect on superoxide release stimulated by A23 187, or by phorbol myristate acetate, and markedly enhanced the superoxide release stimulated by I-oleoyl-2-acetylglycerol. Similar enhancement was obtained with prostaglandin E,. Neutrophil Phorbol ester Protein kinase C Prostaglandin E fMet-Leu-Phe Phosphatidylinositol

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Synergism between phorbol ester and A23187 in Superoxide production by neutrophils

Cited by 46 publications

References 17 publications

Phorbol myristate acetate enhances human polymorphonuclear neutrophil release of granular enzymes but inhibits chemokinesis

Phorbol myristate acetate enhances human polymorphonuclear neutrophil release of granular enzymes but inhibits chemokinesis

Role of protein kinase C in transmembrane signaling

Prostaglandins E₁ and E₂ enhance the stimulation of superoxide release by 1‐oleoyl‐2‐acetylglycerol from human neutrophils

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Synergism between phorbol ester and A23187 in Superoxide production by neutrophils

Cited by 46 publications

References 17 publications

Phorbol myristate acetate enhances human polymorphonuclear neutrophil release of granular enzymes but inhibits chemokinesis

Phorbol myristate acetate enhances human polymorphonuclear neutrophil release of granular enzymes but inhibits chemokinesis

Role of protein kinase C in transmembrane signaling

Prostaglandins E1 and E2 enhance the stimulation of superoxide release by 1‐oleoyl‐2‐acetylglycerol from human neutrophils

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Prostaglandins E₁ and E₂ enhance the stimulation of superoxide release by 1‐oleoyl‐2‐acetylglycerol from human neutrophils