Effect of membrane phosphatidylethanolamine‐deficiency/phosphatidylcholine‐excess on the metabolism of phosphatidylcholine and phosphatidylethanolamine

Fisk, Harold A.; Kano-Sueoka, Tamiko

doi:10.1002/jcp.1041530321

Cited by 17 publications

(12 citation statements)

References 33 publications

(19 reference statements)

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“…Based on the measured rate of PtdCho and PtdEtn hydrolysis, a number of cell types examined appear to possess only the PtdCho-specific PLD activity (reviewed in [17,18]). On the other hand, NIH 3T3 fibroblasts [33][34][35][36][37][38], endothelial cells [46], rat mesangial cells [41][42][43][44], human amnion cells [45], rat mammary cells [40], HeLa cells [39], baby-hamster kidney cells [33] and HL60 human leukaemic cells [33] clearly express both PtdCho-and PtdEtn-hydrolysing PLD activities.…”

Section: Formation Of Glycerophospho Giycerophosphoethanolamine Cholimentioning

confidence: 99%

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Phorbol ester selectively stimulates the phospholipase D-mediated hydrolysis of phosphatidylethanolamine in multidrug-resistant MCF-7 human breast carcinoma cells

Kiss

Tomono

Anderson

1994

Biochemical Journal

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The phospholipase D (PLD)-mediated synthesis of phosphatidylethanol (PtdEtOH) and the hydrolysis of phosphatidylethanolamine (PtdEtn) and phosphatidylcholine (PtdCho) were examined in drug-sensitive and multidrug-resistant lines of MCF-7 human breast carcinoma cells. In drug-sensitive (MCF-7/WT) cells, the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA) failed to enhance either the synthesis of PtdEtOH or the hydrolysis of either phospholipid. In the drug-resistant (MCF-7/MDR) cells, 100 nM PMA greatly enhanced both the synthesis of PtdEtOH (approximately 21-fold) and the hydrolysis of PtdEtn (approximately 29-fold), but had no effect on the hydrolysis of PtdCho. The PLD activators sphingosine and H2O2 were found to elicit only a slight (1.28-1.4-fold) stimulatory effect on PtdCho hydrolysis in both the MCF-7/WT and MCF-7/MDR cell types, and had only a small effect on PtdEtn hydrolysis in the MCF-7/WT cells as well. However, these agents significantly (approximately 2.6-3.5-fold) stimulated PtdEtn hydrolysis in the MCF-7/MDR cells. These data indicate that MCF-7/MDR cells contain a PtdEtn-specific PLD activity which can be selectively stimulated by PMA, sphingosine and H2O2.

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Section: Formation Of Glycerophospho Giycerophosphoethanolamine Cholimentioning

confidence: 99%

“…Recently, stimulation of PtdEtn hydrolysis in response to activators of PLD also has been reported in several other cell types [39][40][41][42][43][44][45][46] 12 mg/ml L-proline, 50 ,ug/ml gentamicin and 10 % fetal bovine serum. Cells were passaged twice weekly and monitored routinely for their resistance to adriamycin.…”

Section: Introductionmentioning

confidence: 99%

Phorbol ester selectively stimulates the phospholipase D-mediated hydrolysis of phosphatidylethanolamine in multidrug-resistant MCF-7 human breast carcinoma cells

Kiss

Tomono

Anderson

1994

Biochemical Journal

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“…When these cells are cultured without Etn, cellular functions, particularly those associated with cellular membranes, become abnormal, resulting in growth arrest (Kano-Sueoka and King, 1988;Kano-Sueoka et al, 1990;Fisk and Kano-Sueoka, 1992;Kano-Sueoka and Nicks, 1993). In addition, when deprived of Etn, membrane compositions are affected, witb the amouut of phosphatidylethanolamine (PE) decreasing by 50% and that of phosphatidylcholine (PC) increasing by 30%.…”

Section: Introductionmentioning

confidence: 99%

Ethanolamine modulates DNA synthesis through epidermal growth factor receptor in rat primary hepatocytes

Kume

Sasaki

2006

In Vitro Cell.Dev.Biol.-Animal

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Ethanolamine (Etn) stimulates hepatocyte proliferation in vivo and in vitro; however, the physiological function of Etn in hepatocytes has yet to be elucidated. In the present study, we examined the effect of Etn using a primary culture of rat hepatocytes. The level of membrane phosphatidylethanolamine (PE) significantly decreased when the hepatocytes were cultured without Etn but increased to the level found in the liver when the culture medium was supplemented with 20- 50 microM Etn. Moreover, Etn stimulated DNA synthesis in a dose-dependent manner and had a synergistic effect with epidermal growth factor (EGF). A binding assay and Western blotting showed that the number of EGF receptors was 22- 30% lower in cells grown in the absence of Etn compared to those grown in its presence, but the respective Kd values were almost the same. Furthermore, tyrosine phosphorylation of the EGF receptor was significantly lower in cells grown without Etn. Phosphatidylcholine (PC) synthesis in the liver is unique in that it occurs via stepwise methylation of PE. We found that without Etn supplementation, bezafibrate-induced inhibition of PE methylation increased the level of PE by decreasing its conversion to PC and stimulated DNA synthesis. Moreover, the function of EGF in stimulating DNA synthesis was significantly enhanced under Etn-sufficient conditions. These data suggest that Etn is a nutritional factor required for synthesis of adequate PE, levels of which are important for hepatocyte proliferation.

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“…PMA also potentiates the mitogenic effect of insulin by a wortmannin-sensitive mechanism (9). Moreover, in NIH 3T3 fibroblasts (13,14) and in several other cell types (15)(16)(17)(18) PMA can stimulate the formation of ethanolamine from phosphatidylethanolamine (PtdEtn) by a mechanism involving a specific PLD activity. These observations raise the possibility that ethanolamine may contribute to the growth regulating and/or tumor promoting effects of PMA.…”

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confidence: 99%

Protein Kinase Cα Is a Major Mediator of the Stimulatory Effect of Phorbol Ester on Phospholipase D-mediated Hydrolysis of Phosphatidylethanolamine

Mukherjee

Chung

Ways

et al. 1996

Journal of Biological Chemistry

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Stimulation of phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine (PtdCho) by phorbol 12-myristate 13-acetate (PMA) has been shown to be mediated by the ␣-and ␤I-isoforms of protein kinase C (PKC). To determine the role of various PKC isozymes in the regulation of PLD-mediated phosphatidylethanolamine (PtdEtn) hydrolysis, MCF-7 human breast carcinoma cells overexpressing the ␣-and -isoforms, and R6 rat fibroblasts overexpressing the ␣-, ␤I-, and ⑀-isoforms were used. In the vector control MCF-7 cells, which contain low levels of PKC-␣, PMA (100 nM) had only small effects on the hydrolysis of PtdEtn (1.1-1.35-fold) and PtdCho (1.15-1.6-fold). Stable expression of PKC-␣ in MCF-7 cells, which was accompanied by increased levels of the ␤I-and -isoforms as well, greatly enhanced both PMA-induced PLD-mediated formation of phosphatidylethanol (ϳ5-fold) and the hydrolysis of PtdEtn (2.5-2.9-fold) and PtdCho (5.5-7.2-fold). The effects of PMA on the hydrolysis of PtdEtn (and PtdCho) in MCF-7/PKC-␣ cells were significantly inhibited by 0.5-3 M concentrations of Gö 6976, a selective inhibitor of the conventional PKC subfamily. Stable expression of PKC-␣ in R6 fibroblasts enhanced, at a shorter (10 min) incubation time, the effects of PMA on the hydrolysis of both PtdEtn and, to a lesser extent, PtdCho. In contrast, stable expression of PKC-␤I in R6 fibroblasts, which originally did not contain this enzyme, enhanced the effects of PMA only on PtdCho, but not PtdEtn, hydrolysis. Overexpression of either PKC-in MCF-7 cells or PKC-⑀ in R6 and NIH 3T3 fibroblasts had no detectable effects on PMA-induced hydrolysis of PtdEtn. Collectively, the results suggest that PKC-␣ has a major role in the mediation of phorbol ester action on PtdEtn hydrolysis, while PtdCho hydrolysis may be regulated by both the ␣ and ␤I isoforms.In many cell lines activators of phospholipase D (PLD), 1 including the protein kinase C (PKC) activator phorbol 12-myristate 13-acetate (PMA), appear to stimulate only the hydrolysis of phosphatidylcholine (PtdCho) (1, 2). In MadinDarby canine kidney cells (3) and in Swiss/3T3 cells (4) PKC-␣ was shown to be a major regulator of PtdCho hydrolysis. However, expression of PKC-␤I (5) or addition of PKC-␤I to isolated membranes (6, 7) also enhanced the effect of PMA on PtdCho hydrolysis. Interestingly, while PKC-␣ was a more effective mediator of PMA effect in lung fibroblast membranes than PKC-␤I (6), a reversed order of potency was observed in neutrophil membranes (7). Collectively, these data suggest that if expressed, both PKC-␣ and PKC-␤I may be able to regulate PtdCho hydrolysis.The role of increased PtdCho hydrolysis in the mediation of cellular actions of PKC activators is unknown. Recently, we presented evidence showing that in NIH 3T3 fibroblasts PtdCho hydrolysis is unlikely to play a major role in the mediation of mitogenic effects of PMA (8). In fact, choline phosphate, which in agonist-treated cells can be formed by the sequential actions of PLD and choline kinase, and PMA were found to sti...

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Effect of membrane phosphatidylethanolamine‐deficiency/phosphatidylcholine‐excess on the metabolism of phosphatidylcholine and phosphatidylethanolamine

Cited by 17 publications

References 33 publications

Phorbol ester selectively stimulates the phospholipase D-mediated hydrolysis of phosphatidylethanolamine in multidrug-resistant MCF-7 human breast carcinoma cells

Phorbol ester selectively stimulates the phospholipase D-mediated hydrolysis of phosphatidylethanolamine in multidrug-resistant MCF-7 human breast carcinoma cells

Ethanolamine modulates DNA synthesis through epidermal growth factor receptor in rat primary hepatocytes

Protein Kinase Cα Is a Major Mediator of the Stimulatory Effect of Phorbol Ester on Phospholipase D-mediated Hydrolysis of Phosphatidylethanolamine

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