Vasopressin, phorbol diesters and serum elicit choline glycerophospholipid hydrolysis and diacylglycerol formation in nontransformed cells: transformed derivatives do not respond

Cabot, Myles C.; Welsh, Clement J.; Zhang, Zu-chuan; Cao, Hui-ting; Chabbott, Holly; Lebowitz, Michael

doi:10.1016/0005-2760(88)90148-8

Cited by 68 publications

(23 citation statements)

References 40 publications

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“…In a previous study we have shown that serum, VP and TPA induce PC degradation and the collateral formation of DG in cultured REF52 cells [9]. Cell treatment was accompanied by the release of [3Hlcholine to the culture medium [9], suggesting that phospholipase D was the initial enzyme involved in the evolution of DGs.…”

Section: Introductionmentioning

confidence: 89%

“…McClure (Division of Molecular and Cellular Biology, Eli Lilly and Company, Indianapolis, IN), was cultured as previously described [9][10][11]. Cells were used at passages 5 through to 15.…”

Section: Cell Culture Radiolabeling and Treatmentmentioning

confidence: 99%

“…After removal of isotope, monolayers were rinsed twice in serum-free medium containing 1.0 mg BSA/ml (medium B), and incubated in the same for 60 min. Following one rinse with medium B, TPA and VP were added in medium B. TPA (8 x 10 -8 M) was added as previously described [9]; VP (100 ng/ml) was added in 0.05 N acetic acid. Cells were prelabeled with [3H]choline (1.0/zCi/ml medium) for 48 h and then prepared for experiments as described above.…”

Section: Cell Culture Radiolabeling and Treatmentmentioning

confidence: 99%

“…The classical scheme involving PIPE as the sole source of DG second messengers has recently been challenged. New research has revealed a cellular pathway for the agonist-induced generation of DG from PC [6][7][8][9]; however, the enzymatic avenue of DG formation has not been clarified.…”

Section: Introductionmentioning

confidence: 99%

“…Cell treatment was accompanied by the release of [3Hlcholine to the culture medium [9], suggesting that phospholipase D was the initial enzyme involved in the evolution of DGs. The study of PC degradation in cultured cells has been hindered due to a lack of precursors that are specific for labeling the aliphatic portion of the molecule.…”

Section: Introductionmentioning

confidence: 99%

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The phosphatidylcholine pathway of diacylglycerol formation stimulated by phorbol diesters occurs via phospholipase D activation

et al. 1988

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Agonist-induced degradation of phosphatidylcholine (PC) is of interest as this pathway of diacylglycerol (DG) generation may provide added opportunities for the regulation of protein kinase C (PKC). In REF52 cells pH]myristic acid is preferentially incorporated into PC; this, coupled with the use of pH]eholine, allows for quantitation of both the water-soluble and the lipid products generated when PC is degraded. In cells prelabeled with pH]choline, TPA stimulated a time-dependent release, into the medium, of choline and not phosphocholine or glycerophosphocholine. Treatment of pH]myristic acid-labeled cells with either phorbol diesters, sn-1,2-dioetanoyiglycerol, or vasopressin elicited the formation of labeled phosphatidate (PA) and DG. The temporal pattern of PC hydrolysis in cells treated with TPA is indicative of a precursor (PA)-product (DG) relationship for an enzymatic sequence initiated by phospholipase D. Adding propranolol, a phosphatidate phosphohydrolase inhibitor, eliminated TPA-induced DG formation, whereas PA generation was unaffected. From these data we conclude that TPA elicits DG formation from PC by the sequential actions of phospholipase D and phosphatidate phosphohydrolase.

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Section: Introductionmentioning

confidence: 89%

Section: Cell Culture Radiolabeling and Treatmentmentioning

confidence: 99%

Section: Cell Culture Radiolabeling and Treatmentmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The phosphatidylcholine pathway of diacylglycerol formation stimulated by phorbol diesters occurs via phospholipase D activation

et al. 1988

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Adenine nucleotides modulate phosphatidylcholine metabolism in aortic endothelial cells

Pirotton¹,

Robaye²,

Lagneau³

et al. 1990

Journal Cellular Physiology

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ATP and ADP, in concentrations ranging from 1-100 microM, increased the release of [3H]choline and [3H]phosphorylcholine (P-choline) from bovine aortic endothelial cells (BAEC) prelabelled with [3H]choline. This action was detectable within 5 minutes and was maintained for at least 40 minutes. ATP and ADP were equiactive, and their action was mimicked by their phosphorothioate analogs (ATP gamma S and ADP beta S) and adenosine 5'-(beta, gamma imido) triphosphate (APPNP), but not by AMP, adenosine, and adenosine 5'-(alpha, beta methylene)triphosphate (APCPP): these results are consistent with the involvement of P2Y receptors. ATP also induced an intracellular accumulation of [3H]choline: the intracellular level of [3H]choline was increased 30 seconds after ATP addition and remained elevated for a least 20 minutes. The action of ATP on the release of choline metabolites was reproduced by bradykinin (1 microM), the tumor promoter phorbol 12-myristate 13-acetate (PMA, 50 nM), and the calcium ionophore A23187 (0.5 microM). Down-regulation of protein kinase C, following a 24-hour exposure of endothelial cells to PMA, abolished the effects of PMA and ATP on the release of choline and P-choline, whereas the response to A23187 was maintained. These results suggest that in aortic endothelial cells, ATP produces a sustained activation of a phospholipase D hydrolyzing phosphatidylcholine. The resulting accumulation of phosphatidic acid might have an important role in the modulation of endothelial cell function by adenine nucleotides. Stimulation of phospholipase D appears to involve protein kinase C, activated following the release of diacylglycerol from phosphatidylinositol bisphosphate by a phospholipase C coupled to the P2Y receptors (Pirotton et al., 1987a).

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

Fisk

Kano-Sueoka

1992

Journal Cellular Physiology

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Cells of epithelial origin generally require ethanolamine (Etn) to grow in defined culture medium. When such cells are grown without Etn, the membrane phospholipid composition changes drastically, becoming phosphatidylethanolamine (PE)-deficient due to a reduced de novo rate of PE synthesis, and growth stops. We have hypothesized that the cessation of growth occurs because this membrane phospholipid environment is no longer suitable for membrane-associated functions. Phospholipid has long been known to play a role in the transduction of some signals across membranes. In addition to the well-known phosphatidylinositol cycles, hydrolysis of phosphatidylcholine (PC) and PE has recently been shown to play a central role in signal transduction. Using an Etn-requiring rat mammary cell line 64-24, we have studied the metabolism of PC and PE in response to the phorbol ester phorbol 12,13-dibutyrate (PDBu) under conditions where cells have either normal or PE-deficient membrane phospholipid. In cells having normal membrane phospholipid, the synthesis of PC was stimulated by PDBu (approximately fourfold), as was the degradation of PC and PE (by twofold and fourfold, respectively). Product analysis suggested that PDBu stimulated hydrolysis of PC by both phospholipases C and D (PLC and PLD), and of PE by PLD. However, in PE-deficient cells, neither lipid synthesis or degradation were significantly stimulated by PDBu. Analysis of the CDP-choline pathway of PC synthesis indicated that the regulatory enzyme, CTP:phosphorylcholine cytidylyltransferase, was stimulated about twofold by PDBu in cells having normal membrane, but not in PE-deficient cells. These results indicate that the membrane phospholipid environment profoundly affects phospholipid metabolism, which no doubt influences cell growth and regulation.

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Vasopressin, phorbol diesters and serum elicit choline glycerophospholipid hydrolysis and diacylglycerol formation in nontransformed cells: transformed derivatives do not respond

Cited by 68 publications

References 40 publications

The phosphatidylcholine pathway of diacylglycerol formation stimulated by phorbol diesters occurs via phospholipase D activation

The phosphatidylcholine pathway of diacylglycerol formation stimulated by phorbol diesters occurs via phospholipase D activation

Adenine nucleotides modulate phosphatidylcholine metabolism in aortic endothelial cells

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

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