Phosphatidate Kinase, A Novel Enzyme in Phospholipid Metabolism (Characterization of the Enzyme from Suspension-Cultured Catharanthus roseus Cells)

Wissing, Josef; Kornak, Brigitte; Funke, Almuth; Riedel, Bettina

doi:10.1104/pp.105.3.903

Cited by 26 publications

(11 citation statements)

References 27 publications

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“…Northern blot analysis of mRNA from P388D 1 macrophages failed to detect expression of the vzg-1/lpA1/edg-2 lyso-PA receptor (27,28) on these cells. 4 Moreover, this receptor does not bind DGPP when assayed by a specific receptor binding assay (28,29). 4 Therefore, the DGPP effects reported herein are not mediated by this lyso-PA receptor.…”

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confidence: 81%

“…4 Moreover, this receptor does not bind DGPP when assayed by a specific receptor binding assay (28,29). 4 Therefore, the DGPP effects reported herein are not mediated by this lyso-PA receptor. Recently, two other lyso-PAlike receptors have been identified (30,31).…”

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confidence: 81%

“…The biochemical routes leading to biosynthesis and degradation of DGPP in those cells which produce it have recently been elucidated (3)(4)(5)(6)(7)(8). DGPP is produced by phosphorylation of phosphatidic acid (PA), a reaction catalyzed by a specific kinase that has been purified from plants (3).…”

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confidence: 99%

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Proinflammatory Macrophage-activating Properties of the Novel Phospholipid Diacylglycerol Pyrophosphate

Balboa

Balsinde

Dillon

et al. 1999

Journal of Biological Chemistry

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We have found that the novel phospholipid diacylglycerol pyrophosphate (DGPP), identified in bacteria, yeast, and plants, but not in mammalian cells, is able to potently activate macrophages for enhanced secretion of arachidonate metabolites, a key event in the immunoinflammatory response of leukocytes. Macrophage responses to DGPP are specific and are not mediated by its conversion into other putative lipid mediators such as phosphatidic acid, lysophosphatidic acid, or diacylglycerol. The responses to DGPP are compatible with a receptor-recognition event because they are blocked by suramin. Intracellular signaling initiated by DGPP includes phosphorylation and activation of the Group IV cytosolic phospholipase A 2 and of the extracellular-signal regulated p42 mitogen-activated protein kinase (MAPK) and p44 MAPK, and membrane translocation of the protein kinase C isoenzymes ␣, ⑀, ␦. These results establish DGPP as a novel macrophage-activating factor and suggest a potential role for this compound in triggering homeostatic cellular responses.

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confidence: 81%

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confidence: 81%

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Proinflammatory Macrophage-activating Properties of the Novel Phospholipid Diacylglycerol Pyrophosphate

Balboa

Balsinde

Dillon

et al. 1999

Journal of Biological Chemistry

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“…Reactions were stopped, and lipids were extracted and analyzed as described previously. Lipid kinases activities were assayed essentially according to Kamada and Muto (1991), except for PtdOH kinase activity (Wissing et al, 1994). To assay DAG kinase, lipids (10 mg of DAG and 40 mg of phosphatidylglycerol) were mixed, dried under gaseous nitrogen, and resuspended in 10 mL of reaction buffer (50 mM Tris-HCl, pH 7.5, 10 mM MgCl 2 , 0.02% [v/v] ) in a 50-mL final reaction volume.…”

Section: Measurement Of Enzymatic Activitiesmentioning

confidence: 99%

Polyphosphoinositides Are Enriched in Plant Membrane Rafts and Form Microdomains in the Plasma Membrane

et al. 2010

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In this article, we analyzed the lipid composition of detergent-insoluble membranes (DIMs) purified from tobacco (Nicotiana tabacum) plasma membrane (PM), focusing on polyphosphoinositides, lipids known to be involved in various signal transduction events. Polyphosphoinositides were enriched in DIMs compared with whole PM, whereas all structural phospholipids were largely depleted from this fraction. Fatty acid composition analyses suggest that enrichment of polyphosphoinositides in DIMs is accompanied by their association with more saturated fatty acids. Using an immunogold-electron microscopy strategy, we were able to visualize domains of phosphatidylinositol 4,5-bisphosphate in the plane of the PM, with 60% of the epitope found in clusters of approximately 25 nm in diameter and 40% randomly distributed at the surface of the PM. Interestingly, the phosphatidylinositol 4,5-bisphosphate cluster formation was not significantly sensitive to sterol depletion induced by methyl-b-cyclodextrin. Finally, we measured the activities of various enzymes of polyphosphoinositide metabolism in DIMs and PM and showed that these activities are present in the DIM fraction but not enriched. The putative role of plant membrane rafts as signaling membrane domains or membrane-docking platforms is discussed.

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“…Recently, a new enzyme activity was extracted from many different higher plants that was able to phosphorylate PtdOH to diacylglycerol pyrophosphate (DGPP) and was called phosphatidate kinase Behrbohm, 1993a, 1993b;Wissing et al, 1994). As yet, all demonstrations of activity were in vitro.…”

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Identification of Diacylglycerol Pyrophosphate as a Novel Metabolic Product of Phosphatidic Acid during G-protein Activation in Plants

Munnik

Vrije²,

Irvine

et al. 1996

Journal of Biological Chemistry

133

159

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We provide evidence that phosphatidic acid (PtdOH) formed during signaling in plants is metabolized by a novel pathway. In much of this study, 32Pi-labeled Chlamydomonas cells were used, and signaling was activated by adding the G-protein activator mastoparan. Within seconds of activation, large amounts of [32P]PtdOH were formed, with peak production at about 4 min, when the level was 5-25-fold higher than the control. As the level of [32P]PtdOH subsequently decreased, an unknown phospholipid (PLX) increased in radiolabeling; before activation it was barely detectable. The chromatographic properties of PLX resembled those of lyso-PtdOH and CMP.PtdOH but on close inspection were found to be different. PLX was shown to be diacylglycerol pyrophosphate (DGPP), the product of a newly discovered enzyme, phosphatidate kinase, whose in vitro activity was described recently (Wissing, J. B., and Behrbohm, H. (1993) Plant Physiol. 102, 1243-1249). The identity of DGPP was established by co-chromatrography with a standard and by degradation analysis as follows: [32P]DGPP was deacylated, and the product (glycerolpyrophosphate, GroPP) was hydrolyzed by mild acid treatment or pyrophosphatase to produce GroP and Pi as the only radioactive products. Since DGPP is the pyrophosphate derivative of PtdOH and is formed as the concentration of PtdOH decreases, we assumed that PtdOH was converted in vivo to DGPP. This was confirmed by showing that during a short labeling protocol while the specific radioactivity of DGPP was increasing, the specific radioactivity of the 32Pi derived from DGPP as above was higher than that of [32P]GroP. DGPP was also formed in suspension cultures of tomato and potato cells, and its synthesis was activated by mastoparan. Moreover, it was also found in intact tissues of a number of higher plants, for example, carnation flower petals, vetch roots, leaves of fig-leaved goosefoot, and common persicaria and microspores of rape seed. Our results suggest that DGPP is a common but minor plant lipid that increases in concentration when signaling is activated. Possible functions of DGPP in phospholpase C and D signaling cascades are discussed.

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Phosphatidate Kinase, A Novel Enzyme in Phospholipid Metabolism (Characterization of the Enzyme from Suspension-Cultured Catharanthus roseus Cells)

Cited by 26 publications

References 27 publications

Proinflammatory Macrophage-activating Properties of the Novel Phospholipid Diacylglycerol Pyrophosphate

Proinflammatory Macrophage-activating Properties of the Novel Phospholipid Diacylglycerol Pyrophosphate

Polyphosphoinositides Are Enriched in Plant Membrane Rafts and Form Microdomains in the Plasma Membrane

Identification of Diacylglycerol Pyrophosphate as a Novel Metabolic Product of Phosphatidic Acid during G-protein Activation in Plants

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