Transphosphatidylation by Phospholipase D

Yang, Shue Fen; Freer, Sofia M.; Benson, A. A.

doi:10.1016/s0021-9258(18)96298-8

Cited by 536 publications

(61 citation statements)

References 27 publications

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“…To provide further evidence that PLD is not involved in DAG production, we next assessed PLD more directly by investigation of possible formation of labeled phosphatidylethanol (PEt), which would be expected from PLD's transphosphatidylation activity in the presence of ethanol (57,59,60). In various cell lines, activation of PLD by phorbol esters results in formation of PA and of PEt, in the presence of ethanol (61)(62)(63).…”

Section: Tnf-induced Dag Production Does Not Results From Phosphotipase D (Pld)activationmentioning

confidence: 99%

“…Since propranolol prevents dephosphorylation of PA (55,58), an inhibition of DAG production, would have been expected if PLD and PA-phosphohydrolase were involved in TNF-induced DAG generation. Finally, in the presence of ethanol, which substitutes for H20 in the transphosphatidylation reaction catalyzed by PLD (57,59,60), TNF-induced formation of PEt was not detectable. Since PA metabolization to PEt in the presence of ethanol prevents production of DAG (57), an inhibition of TNF-stimulated DAG formation would be expected, if PA was the source for DAG.…”

Section: Discussionmentioning

confidence: 96%

See 1 more Smart Citation

Tumor necrosis factor induces rapid production of 1'2'diacylglycerol by a phosphatidylcholine-specific phospholipase C.

Schütze

Berkovic

Tomsing

et al. 1991

The Journal of Experimental Medicine

182

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SummaryTumor necrosis factor (TNF) is a proinflammatory polypeptide that is able to induce a great diversity of cellular responses via modulating the expression of a number of different genes. One major pathway by which TNF receptors communicate signals from the membrane to the cell nucleus involves protein kinase C (PKC). In the present study, we have addressed the molecular mechanism of TNF-induced PKC activation. To this, membrane lipids of the human histiocytic cell line U937 were labeled by incubation with various radioactive precursors, and TNF-induced changes in phospholipid, neutral lipid, and water-soluble metabolites were analyzed by thin layer chromatography. TNF treatment of U937 cells resulted in a rapid and transient increase of l'2'diacylglycerol (DAG), a well-known activator of PKC. The increase in DAG was detectable as early as 15 s after TNF treatment and peaked at 60 s. DAG increments were most pronounced (~360% of basal levels) when cells were preincubated with [14C]lysophosphatidylcholine, which was predominantly incorporated into the phosphatidylcholine (PC) pool of the plasmamembranes. Further extensive examination of changes in metabolically labeled phospholipids indicated that TNF-stimulated hydrolysis of PC is accompanied by the generation of phosphorylcholine and DAG. These results suggest the operation of a PC-specific phospholipase C. Since no changes in phosphatidic acid (PA) and choline were observed and the production of DAG by TNF could not be blocked by either propranolol or ethanol, a combined activation of phospholipase D and PA-phosphohydrolase in DAG production appears unlikely. TNF-stimulated DAG production as well as PKC activation could be blocked by the phospholipase inhibitor/~-bromopbenacylbromide (BPB). Since BPB did not inactivate PKC directly, these findings underscore that TNF activates PKC via formation of DAG. TNF stimulation of DAG production could be inhibited by preincubation of cells with a monoclonal anti-TNF receptor (p55-60) antibody, indicating that activation of a PC-specific phospholipase C is a TNF receptor-mediated event.

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Section: Tnf-induced Dag Production Does Not Results From Phosphotipase D (Pld)activationmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 96%

Tumor necrosis factor induces rapid production of 1'2'diacylglycerol by a phosphatidylcholine-specific phospholipase C.

Schütze

Berkovic

Tomsing

et al. 1991

The Journal of Experimental Medicine

182

View full text Add to dashboard Cite

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“…Resting levels were normalized to the mean resting counts per minute of three experiments : ['Hlaa-PI = 70,000 ; ['°Clgly-PI = 5,000 . We used these inhibitors as a second approach to determine the role of PLD in the generation of slow diacylglycerol after FMLP In the presence of alcohols, PLD can catalyze a transphosphatidylation of these organic alcohols to phosphatidate (23,68), thus depleting substrate for PPH and inhibiting generation of DG by this dual-enzyme pathway. We treated neutrophils with 0.5% ethanol after labeling with 3H-a .a.…”

Section: Effect Ofprotein I On Diacylglycerol Metabolism In Neutrophilsmentioning

confidence: 99%

Effects of protein I of Neisseria gonorrhoeae on neutrophil activation: generation of diacylglycerol from phosphatidylcholine via a specific phospholipase C is associated with exocytosis.

Haines

Reibman

Tang

et al. 1991

The Journal of Cell Biology

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. Upon engagement of chemoattractant receptors, neutrophils generate inositol trisphosphate and diacylglycerol (DG) by means of a phosphatidylinositolspecific phospholipase C (PI-PLC) which is regulated by a GTP-binding protein(s) . We have previously reported (Reibman, J., H. M. Korchak, L. B. Vosshall, K. A. Haines, A. M. Rich, and G. Weissmann. 1988. J. Biol. Chem. 263 :6322-6328) a biphasic rise in DG after exposure of neutrophils to the chemoattractant FMLP: a rapid (<15 s) phase ("triggering") and a slow (>,30 s) phase ("activation") . These derive from distinct intracellular lipid pools. To study the source of rapid and slow DG, we have used a unique probe, protein I, a porin that is the major outer membrane protein of Neisseria gonorrhoeae. Treatment of neutrophils with protein I inhibits exocytosis and homotypic cell adhesion provoked by FMLP without inhibiting assembly of the NADPH oxidase responsible for OZ genera-

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“…As discussed before, MPA supposedly recognized in microgreen lipid extracts could be generated by a transphosphatidylation reaction involving GPL and methanol and catalysed by endogenous PLD 22–24 . To find an indirect confirmation of this hypothesis, an alternative lipid extraction procedure was attempted, using chia microgreens as matrix.…”

Section: Resultsmentioning

confidence: 93%

HILIC‐ESI‐MS analysis of phosphatidic acid methyl esters artificially generated during lipid extraction from microgreen crops

et al. 2021

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The uncontrolled activation of endogenous enzymes may introduce both qualitative and quantitative artefacts when lipids are extracted from vegetal matrices. In the present study, a method based on hydrophilic interaction liquid chromatography coupled either to high‐resolution/accuracy Fourier‐transform mass spectrometry (HILIC‐ESI‐FTMS) or to linear ion trap multiple stage mass spectrometry (HILIC‐ESI‐MSn, with n = 2 and 3) with electrospray ionization was developed to unveil one of those artefacts. Specifically, the artificial generation of methyl esters of phosphatidic acids (MPA), catalysed by endogenous phospholipase D (PLD) during lipid extraction from five oleaginous microgreen crops (chia, soy, flax, sunflower and rapeseed), was studied. Phosphatidylcholines (PC) and phosphatidylglycerols (PG) were found to be the most relevant precursors of MPA among glycerophospholipids (GPLs), being involved in a transphosphatidylation process catalysed by PLD and having methanol as a coreactant. The combination of MS2 and MS3 measurements enabled the unambiguous recognition of MPA from their fragmentation pathways, leading to distinguish them from isobaric PA including a further CH2 group on their side chains. PLD was also found to catalyse the hydrolysis of PC and PG to phosphatidic acids (PAs). The described transformations were confirmed by the remarkable decrease of MPA abundance observed when isopropanol, known to inhibit PLD, was tentatively adopted instead of water during the homogenization of microgreens. The unequivocal identification of MPA might be exploited to assess if GPL alterations are actually triggered by endogenous PLD during lipid extractions from specific vegetal tissues.

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Transphosphatidylation by Phospholipase D

Cited by 536 publications

References 27 publications

Tumor necrosis factor induces rapid production of 1'2'diacylglycerol by a phosphatidylcholine-specific phospholipase C.

Tumor necrosis factor induces rapid production of 1'2'diacylglycerol by a phosphatidylcholine-specific phospholipase C.

Effects of protein I of Neisseria gonorrhoeae on neutrophil activation: generation of diacylglycerol from phosphatidylcholine via a specific phospholipase C is associated with exocytosis.

HILIC‐ESI‐MS analysis of phosphatidic acid methyl esters artificially generated during lipid extraction from microgreen crops

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