Activation of protein kinase C by fatty acids and its dependency on Ca2+ and phospholipid.

Morimoto, Yosuke; Nobori, Koichi; Edashige, Keisuke; Yamamoto, Masazumi; Kobayashi, Sumio; Utsumi, Kozo

doi:10.1247/csf.13.45

Cited by 19 publications

(4 citation statements)

References 11 publications

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“…An interesting precedent for these findings is the regulation of protein kinase C (PKC) activity (McPhail, Clayton, and Snyderman, 1984;Sekiguchi, Tsukuda, Ogita, Kikkawa, and Nishizuka, 1987;Seifert, Sch~ictele, Rosenthal, and Schultz, 1988;Morimoto, Nobori, Edashige, Yamamoto, Kobayashi, and Utsumi, 1988;Merrill et al, 1989;Bottega and Epand, 1992) and Na+-Ca 2+ exchange (Philipson, 1984;Philipson and Ward, 1985) by negatively and positively charged lipids. While PKC activity was increased by fatty acids (McPhail et al, 1984;Sekiguchi et al, 1987;Seifert et al, 1988;Morimoto et al, 1988;Touny et al, 1990), it was inhibited by a range of positively charged compounds with structural requirements for action similar to those found in the present study for the inhibition of K ÷ channel activity (Merrill et al, 1989). (By this we do not mean to suggest that PKC-mediated phosphorylation is responsible for alterations in channel activity in the present study.…”

Section: Mechanisms Of Amphiphile Actionmentioning

confidence: 99%

Structural requirements for charged lipid molecules to directly increase or suppress K+ channel activity in smooth muscle cells. Effects of fatty acids, lysophosphatidate, acyl coenzyme A and sphingosine.

Petrou

Ordway

Hamilton

et al. 1994

The Journal of General Physiology

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We determined the structural features necessary for fatty acids to exert their action on K ÷ channels of gastric smooth muscle cells. Examination of the effects of a variety of synthetic and naturally occurring lipid compounds on K + channel activity in cell-attached and excised membrane patches revealed that negatively charged analogs of medium to long chain fatty acids (but not short chain analogs) as well as certain other negatively charged lipids activate the channels. In contrast, positively charged, medium to long chain analogs suppress activity, and neutral analogs are without effect. The key requirements for effective compounds seem to be a sufficiently hydrophobic domain and the presence of a charged group. Furthermore, those negatively charged compot,nds unable to "flip" across the bilayer are effective only when applied at the cytosolic surface of the membrane, suggesting that the site of fatty acid action is also located there. Finally, because some of the effective compounds, for example, the fatty acids themselves, lysophosphatidate, acyl Coenzyme A, and sphingosine, are naturally occurring substances and can be liberated by agonist-activated or metabolic enzymes, they may act as second messengers targeting ion channels.

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Section: Mechanisms Of Amphiphile Actionmentioning

confidence: 99%

Structural requirements for charged lipid molecules to directly increase or suppress K+ channel activity in smooth muscle cells. Effects of fatty acids, lysophosphatidate, acyl coenzyme A and sphingosine.

Petrou

Ordway

Hamilton

et al. 1994

The Journal of General Physiology

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“…The addition of the fatty acid stimulates several of the characteristic functions of the cells including: the mobilization of calcium Sha'afi et al, 1980;Naccache et al, 1983), the polymerization of actin (Yassin et al, 1985), degranulation (Naccache et al, 1979), aggregation O'Flaherty et al, 1979), and the stimulation of superoxide production (Badwey et al, 1981;1987). Furthermore, arachidonic acid has 1 Author for correspondence. been found to augment the activity of purified protein kinase C (McPhail et al, 1984;Murakami et al, 1986;Morimoto et al, 1988), an enzyme potentially involved in the initiation and/or regulation of neutrophil responsiveness (White et al, 1984;Naccache et al, 1985;Rossi, 1986;Tauber, 1987), as well as that of partially purified NADPH-oxidase preparations from these cells (Rossi, 1986;Tauber, 1987;Curnutte et al, 1987;Clark et al, 1987). These various biological activities of arachidonic acid are generally assumed to support the concept that the fatty acid is an important modulator of the pathophysiological functions of the neutrophils.…”

Section: Introductionmentioning

confidence: 99%

Arachidonic acid‐induced mobilization of calcium in human neutrophils: evidence for a multicomponent mechanism of action

Naccache

McColl

Caon

et al. 1989

British J Pharmacology

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1 The mechanism(s) involved in the mobilization of calcium induced by arachidonic acid in human neutrophils was investigated. 2 The addition of arachidonic acid to a suspension of human neutrophils led to a time-and concentration-dependent mobilization of calcium which was the result of two separate and experimentally differentiable processes. The latter consisted of a rapid and transient phase followed by a slower and more sustained response. 3 The initial phase of calcium mobilization elicited by arachidonic acid was decreased in the presence of EGTA, inhibited by pertussis toxin as well as by nordihydroguaiaretic acid (NDGA), and diminished following a pre-incubation with leukotriene B4, but not platelet-activating factor. 4 The characteristics of the first phase of the mobilization of calcium were consistent with an interaction of the fatty acid with the leukotriene B4 receptors, either directly or indirectly following the synthesis of leukotriene B4, as well as with a release of internal calcium. 5 The second, slower and more sustained phase of calcium mobilization was more apparent at high concentrations (> 8-16 gM) of arachidonic acid, and was relatively insensitive to pertussis toxin, EGTA or NDGA. 6 The characteristics of the 'slow' phase of calcium mobilization by arachidonic acid are consistent with its being associated primarily with a release of calcium from internal storage pools. 7 The data presented indicate that the mechanism of mobilization of calcium by arachidonic acid in human neutrophils is complex and involves specific activation pathways employed, in part at least, by other neutrophil agonists. These findings may have relevance to various inflammatory situations in which the elevated levels of extracellular arachidonic acid known to be present could modulate the functional responsiveness of the neutrophils to other stimuli.

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“…The activity of PKC was routinely assayed by measuring the incorporation of 32p from [-r-32p]ATP into calf thymus H1 histone (type IIIs) or cytoplasmic proteins of neutrophils at 30°C for 3 to 10 rain by the method of Boni and Rondo [14] as described [15]. For the phosphorylation of cytoplasmic proteins by PKC, cytoplasmic supernatant was treated at 55°C for 3 rain to inactivate endogenous protein kinases [11].…”

Section: Assay Of Pkcmentioning

confidence: 99%

“…SDS-PAGE [17] of the reaction mixture was employed. The gels were stained with Coomassie brilliant blue R250 then autoradiograms of the 32p-labelled proteins were made as reported [11,15].…”

Section: Assay Of Pkcmentioning

confidence: 99%

Halothane, an inhalation anesthetic, activates protein kinase C and superoxide generation by neutrophils

Tsuchiya¹,

Okimasu²,

Ueda³

et al. 1988

FEBS Letters

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The rate of superoxide generation of guinea pig intraperitoneal neutrophils by a chemotactic peptide or 12-O-tetradecanoylphorbol-13-acetate (TPA) was increased by 2-bromo-2-chloro-l,l,l,-trifluoroethane (halothane), an inhalation anesthetic. This increase was inhibited by l-(5-isoquinolinesulfonyl)methylpiperazine dihydrochloride (H-7), a specific inhibitor of Ca 2+-and phospholipid-dependent protein ldnase C (PKC). Halothane was found to significantly activate partially purified PKC. The activation required phosphatidylserine (IS) and Ca 2+. Dioleoylglycerol-or TPA-activated PKC activity was further increased by halothane. The cytoplasmic proteins of guinea pig neutrophils phosphorylated by halothaneactivated PKC were similar to those phosphorylated by PMA-activated PKC. The phosphorylation of a 48 kDa protein, a phosphorylated protein required for NADPH oxidase activation, was also increased by halothane. These data suggest that the increase of superoxide production by halothane is correlated with its activation of PKC.

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Activation of protein kinase C by fatty acids and its dependency on Ca2+ and phospholipid.

Cited by 19 publications

References 11 publications

Structural requirements for charged lipid molecules to directly increase or suppress K+ channel activity in smooth muscle cells. Effects of fatty acids, lysophosphatidate, acyl coenzyme A and sphingosine.

Structural requirements for charged lipid molecules to directly increase or suppress K+ channel activity in smooth muscle cells. Effects of fatty acids, lysophosphatidate, acyl coenzyme A and sphingosine.

Arachidonic acid‐induced mobilization of calcium in human neutrophils: evidence for a multicomponent mechanism of action

Halothane, an inhalation anesthetic, activates protein kinase C and superoxide generation by neutrophils

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