Phosphatidylcholine hydrolysis stimulated by phorbol myristate acetate is mediated principally by phospholipase D in endothelial cells

Martin, Thomas W.; Feldman, Dorothy R.; Michaelis, Kevin C.

doi:10.1016/0167-4889(90)90009-3

Cited by 29 publications

(5 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Phosphatidate and diacylglycerol were found to increase simultaneously (Fig. 8), in agreement with the results of Martin and co-workers [33][34][35]. Phosphatidate did not precede diacylglycerol, in contrast with the findings of Bocckino et al [36] in freshly isolated rat hepatocytes.…”

Section: Phosphatidylethanol Accumulation (% Of Basal)supporting

confidence: 91%

Activation of membrane protein kinase C by glucagon and Ca2+-mobilizing hormones in cultured rat hepatocytes. Role of phosphatidylinositol and phosphatidylcholine hydrolysis

Pittner

Fain

1991

Biochemical Journal

View full text Add to dashboard Cite

We found that glucagon stimulated membrane protein kinase C (PKC) activity and phosphatidylcholine hydrolysis in 24 h-cultured rat hepatocytes. Phorbol myristate acetate, 8-bromo cyclic AMP, vasopressin, noradrenaline and the Ca2+ ionophore A23187 also stimulated membrane PKC activity. However, only vasopressin and noradrenaline stimulated inositol phosphate accumulation, whereas all agonists stimulated the rate of release of water-soluble choline metabolites into the medium. Choline, and to a much lesser extent phosphocholine, were released, suggesting predominantly phospholipase D activation. This was supported by the finding that the accumulation of phosphatidate and diacylglycerol was enhanced by the agents in [3H]myristate-labelled hepatocytes, as was [32P]phosphatidylethanol formation. Since the time courses for the release of choline into the medium and the accumulation of phosphatidate and diacylglycerol caused by vasopressin and glucagon were similar, the more rapid activation of PKC by vasopressin probably reflects diacylglycerol formation from phosphoinositide breakdown. The inability of glucagon to stimulate inositol phosphate production was not due to the prolonged culture, since similar results were obtained in 4 h cultures. We conclude that the stimulation of membrane PKC activity by glucagon correlates with accumulation of diacylglycerol and phosphatidate derived from the hydrolysis of phosphatidylcholine.

show abstract

Section: Phosphatidylethanol Accumulation (% Of Basal)supporting

confidence: 91%

Activation of membrane protein kinase C by glucagon and Ca2+-mobilizing hormones in cultured rat hepatocytes. Role of phosphatidylinositol and phosphatidylcholine hydrolysis

Pittner

Fain

1991

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…However, in many cells, phorbol esters such as phorbol 12-myristate 13-acetate (PMA) are also potent activators of this enzyme, suggesting that physiological increases in PLD activity may be secondary effects of the activation of phospholipase C and that protein kinase C (PKC) may play an important role in the regulation of PLD [7,[12][13][14][15]. In some cells, inhibitors of PKC have been shown to block the activation of PLD by phorbol esters [12][13][14]16], whereas in other cell types they have been ineffective or only partially effective [7,17,18]. In accord with the latter results, it has been reported that purified PKC can activate PLD by a phosphorylation-independent mechanism [19].…”

Section: Introductionmentioning

confidence: 99%

Stimulation of phospholipase D in rabbit platelet membranes by nucleoside triphosphates and by phosphocreatine: roles of membrane-bound GDP, nucleoside diphosphate kinase and creatine kinase

Fan

Sherwood

Haslam

1994

Biochemical Journal

View full text Add to dashboard Cite

Previous work has shown that guanosine 5'-[gamma-thio]triphosphate (GTP[S]) and GTP stimulate phospholipase D (PLD) in rabbit platelet membranes and that these effects are greatly enhanced by pretreatment of platelets with phorbol esters that activate protein kinase C [Van der Meulen and Haslam (1990), Biochem. J. 271, 693-700]. In the present study, the effects of Mg2+, various nucleoside triphosphates and phosphocreatine (PCr) were investigated. Platelet membranes containing phospholipids labelled with [3H]glycerol were assayed for PLD in the presence of an optimal Mg2+ concentration (10 mM) by measuring [3H]phosphatidylethanol formation in incubations that included 300 mM ethanol. In membranes from phorbolester-treated platelets, the same maximal increases in PLD activity (5-fold) were seen with 1 microM GTP[S]), and 100 microM GTP. Addition of adenosine 5'-[gamma-thio]triphosphate (ATP[S]), ITP, XTP, UTP and CTP had similar stimulatory effects, but only at > or = 1 mM. In contrast, ATP had a biphasic action, causing a maximal (2-fold) stimulation at 10 microM and smaller effects at higher concentrations; the inhibitory component of the action of ATP was blocked by 2 microM staurosporine. Guanosine 5'-[beta-thio]diphosphate decreased the stimulatory effects of ATP and ATP[S]. UDP, which can inhibit nucleoside diphosphate kinase (NDPK), decreased the activation of PLD by ATP[S], ATP, XTP, CTP and to a lesser extent ITP, but had no effect on the actions of GTP[S] and GTP. Rabbit platelet membranes contained NDPK and addition of [gamma-32P]ATP led to the formation of [32P]GTP in amounts sufficient to explain most or all of the activation of PLD; UDP prevented GTP formation. PCr (0.04-1 mM) also stimulated membrane PLD activity, an effect that was dependent on endogenous membrane-bound creatine kinase (CK). UDP and guanosine 5'-[beta-thio]diphosphate each inhibited this effect of PCr. The results show that in rabbit platelet membranes, CK, NDPK and the GTP-binding protein that activates PLD can be functionally coupled. However, assay of membrane preparations at increasing dilutions showed that stimulation of PLD by the compounds studied, with the partial exception of ATP[S], involved diffusible rather than protein-bound intermediates.

show abstract

“…The involvement of PLD activity on PC hydrolysis stimulated by different pancreatic stimuli was then investi gated in pancreatic acini prelabeled with 3H myristic acid, the label of choice for the PC fatty acid domain [27], Upon hydrolysis by PLD. PC gives rise to phosphatidic acid and free choline, and the newly formed PA can be transformed into DAG by phosphatidic acid phosphohydrolase [28].…”

Section: Effects O F Different Pancreatic Agonists On Pa Productionmentioning

confidence: 99%

Specificity of Phospholipase D Activation by Cholecystokinin and Phorbol Myristate Acetate but Not by Carbamylcholine and A23187 in Rat Pancreatic Acini

Rydzewska¹,

Morisset²

1995

Digestion

View full text Add to dashboard Cite

The gastrointestinal hormone cholecystokinin and the muscarinic agonist carbamylcholine are involved in pancreatic enzyme secretion through phospholipase C activation and production of the second messengers inositol trisphosphate and diacylglycerol. However, cholecystokinin induces growth of the pancreas whereas carbamylcholine does not. This study investigated the possibility of a specific cellular signalling transduction system through which cholecystokinin may induce pancreatic growth. Rat pancreatic acini were preincubated with ³H choline or ³H myristic acid to label phosphatidylcholine. They were then stimulated by caerulein, phorbol myristate acetate, and carbamylcholine; choline and phosphocholine release as well as phosphatidic acid and phosphatidylethanol production were measured to establish phospholipase D (PLD) activation. Caerulein, phorbolester and carbamylcholine increased phosphocholine release. Choline release was induced early by caerulein and later by phorbolester but not by carbachol. PLD was activated by caerulein and phorbolester but not by carbamylcholine. Increased intracellular calcium by A23187 had no effect on PLD activation but its chelation by BAPTA prevented caerulein-induced PLD activation. In conclusion, PLD seems to be selectively activated by caerulein and phorbol ester by two different mechanisms which are insensitive to carbamylcholine. It is suggested that the PLD pathway might be the cellular signalling system leading to pancreatic growth.

show abstract

Phosphatidylcholine hydrolysis stimulated by phorbol myristate acetate is mediated principally by phospholipase D in endothelial cells

Cited by 29 publications

References 49 publications

Activation of membrane protein kinase C by glucagon and Ca2+-mobilizing hormones in cultured rat hepatocytes. Role of phosphatidylinositol and phosphatidylcholine hydrolysis

Activation of membrane protein kinase C by glucagon and Ca2+-mobilizing hormones in cultured rat hepatocytes. Role of phosphatidylinositol and phosphatidylcholine hydrolysis

Stimulation of phospholipase D in rabbit platelet membranes by nucleoside triphosphates and by phosphocreatine: roles of membrane-bound GDP, nucleoside diphosphate kinase and creatine kinase

Specificity of Phospholipase D Activation by Cholecystokinin and Phorbol Myristate Acetate but Not by Carbamylcholine and A23187 in Rat Pancreatic Acini

Contact Info

Product

Resources

About