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Journal articles on the topic 'Phosphatidic acid'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 May 2024

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1

ENGLISH, Denis, Margaret MARTIN, Kevin A. HARVEY, Luke P. AKARD, Ruth ALLEN, Theodore S. WIDLANSKI, Joe G. N. GARCIA, and Rafat A. SIDDIQUI. "Characterization and purification of neutrophil ecto-phosphatidic acid phosphohydrolase." Biochemical Journal 324, no. 3 (June 15, 1997): 941–50. http://dx.doi.org/10.1042/bj3240941.

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Phosphatidic acid and its derivatives play potentially important roles as extracellular messengers in biological systems. An ecto-phosphatidic acid phosphohydrolase (ecto-PAPase) has been identified which effectively regulates neutrophil responses to exogenous phosphatidic acid by converting the substrate to diacylglycerol. The present study was undertaken to characterize this ecto-enzyme on intact cells and to isolate the enzyme from solubilized neutrophil extracts. In the absence of detergent, short chain phosphatidic acids were hydrolysed most effectively by neutrophil plasma membrane ecto-

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2

Kaszkin, M., L. Seidler, R. Kast, and V. Kinzel. "Epidermal-growth-factor-induced production of phosphatidylalcohols by HeLa cells and A431 cells through activation of phospholipase D." Biochemical Journal 287, no. 1 (October 1, 1992): 51–57. http://dx.doi.org/10.1042/bj2870051.

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In response to epidermal growth factor (EGF), HeLa cells and A431 cells rapidly accumulate substantial amounts of phosphatidic acid (up to 0.16 and 0.2 micrograms/10(6) cells respectively), which represents approx. 0.17% of total phospholipid. Phosphatidic acid may be a potential product of diacylglycerol kinase and/or of phospholipase D. To evaluate the contribution of phospholipase D, the phosphatidyl-transfer reaction to a primary alcohol (mostly butan-1-ol; 0.2%) was measured; this reaction is known to be mediated exclusively by phospholipase D in intact cells. In HeLa and in A431 cells pr

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3

Altin, J. G., and F. L. Bygrave. "Phosphatidic acid and arachidonic acid each interact synergistically with glucagon to stimulate Ca2+ influx in the perfused rat liver." Biochemical Journal 247, no. 3 (November 1, 1987): 613–19. http://dx.doi.org/10.1042/bj2470613.

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The administration of phosphatidic acid to rat livers perfused with media containing either 1.3 mM- or 10 microM-Ca2+ was followed by a stimulation of Ca2+ efflux, O2 uptake and glucose output. The responses elicited by 100 microM-phosphatidic acid were similar to those induced by the alpha-adrenergic agonist phenylephrine. Contrary to suggestions that phosphatidic acid acts like a Ca2+-ionophore, no net influx of Ca2+ was detected until the phosphatidic acid was removed. Sequential infusions of phenylephrine and phosphatidic acid indicate that the two agents release Ca2+ from the same intrace

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4

Raben, Daniel M., and Casey N. Barber. "Phosphatidic acid and neurotransmission." Advances in Biological Regulation 63 (January 2017): 15–21. http://dx.doi.org/10.1016/j.jbior.2016.09.004.

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5

Fraser, T., A. Waters, S. Chatrattanakunchai, and K. Stobart. "Does triacylglycerol biosynthesis require diacylglycerol acyltransferase (DAGAT)?" Biochemical Society Transactions 28, no. 6 (December 1, 2000): 698–700. http://dx.doi.org/10.1042/bst0280698.

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Microsomal membrane preparations from the developing seeds of sunflower (Helianthus annuus L.) catalyse the conversion of sn-glycerol-3-phosphate and acyl-CoA to triacylglycerol via phosphatidic acid and diacylglycerol. The formation of diacylglycerol from phosphatidic acid was Mg2+ dependent and in the presence of EDTA phosphatidic acid accumulated. This property was used to generate large quantities of endogenous radioactive phosphatidic acid in the membranes. On addition of Mg2+ the phosphatidic acid was used in triacylglycerol formation. Acyl-CoA had little effect on the label which accumu

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6

Bodachivska, L. Yu. "Biodegradable surfactants from side streams of the vegetable oils production in technical systems." Voprosy Khimii i Khimicheskoi Tekhnologii, no. 6 (December 2022): 3–11. http://dx.doi.org/10.32434/0321-4095-2022-145-6-3-11.

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This work reports the structure of surfactants synthesized from by-products of the vegetable oil production. These are raw materials that do not compete with food products; they are low-cost phosphatidic sludge that can be used directly for chemical transformation. Fatty acid monoetanolamides derived from side streams of the vegetable oils production do not have residues of the original phosphatides or acylglycerols as determined by spectral methods. There are clearly reflected cross-peaks between the amide group and the adjacent methylene group. This indicates a high conversion of substrate a

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7

Andringa, Ruben L. H., Marijn Jonker, and Adriaan J. Minnaard. "Synthesis of phosphatidic acids via cobalt(salen) catalyzed epoxide ring-opening with dibenzyl phosphate." Organic & Biomolecular Chemistry 20, no. 11 (2022): 2200–2204. http://dx.doi.org/10.1039/d2ob00168c.

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8

Sakane, Fumio, Fumi Hoshino, and Chiaki Murakami. "New Era of Diacylglycerol Kinase, Phosphatidic Acid and Phosphatidic Acid-Binding Protein." International Journal of Molecular Sciences 21, no. 18 (September 16, 2020): 6794. http://dx.doi.org/10.3390/ijms21186794.

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Diacylglycerol kinase (DGK) phosphorylates diacylglycerol (DG) to generate phosphatidic acid (PA). Mammalian DGK consists of ten isozymes (α–κ) and governs a wide range of physiological and pathological events, including immune responses, neuronal networking, bipolar disorder, obsessive-compulsive disorder, fragile X syndrome, cancer, and type 2 diabetes. DG and PA comprise diverse molecular species that have different acyl chains at the sn-1 and sn-2 positions. Because the DGK activity is essential for phosphatidylinositol turnover, which exclusively produces 1-stearoyl-2-arachidonoyl-DG, it

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9

Kolesnikov, Y. S., S. V. Kretynin, V. S. Kravets, and Y. K. Bukhonska. "Phosphatidic acid formation and signaling in plant cells." Ukrainian Biochemical Journal 96, no. 1 (February 23, 2024): 5–21. http://dx.doi.org/10.15407/ubj96.01.005.

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This review conteins updated information on the structure, localization and regulation of phosphatidic acid (PA)-producing enzymes phospholipase D, phosphoinositide-specific and non-specific phospholipases C and diacylglycerol kinases is analyzed. The specific role of PA and PA-producing enzymes in plant stress signaling is discussed.

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10

Singh, Ram Raj, Priti Prasad, Cynthia Tran, and Ramesh Halder. "A self-glycerophospholipid suppresses immunity and inflammation via recruitment of Ly6C+ myeloid cells." Journal of Immunology 198, no. 1_Supplement (May 1, 2017): 221.19. http://dx.doi.org/10.4049/jimmunol.198.supp.221.19.

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Abstract Membrane lipids function as essential components of biological membranes, as signaling molecules, and as energy storage molecules. Phosphatidic acid is a vital membrane lipid that serves as a precursor for the synthesis of all acylglycerol lipids in the cell. Phosphatidic acid participates in a wide range of cellular processes, including cytoskeletal organization, secretion, endocytosis, and cell proliferation. Here, we examined the effect of phosphatidic acid on myeloid cells and its ability to modulate tumor immunity and inflammatory disease. We found that in vivo administration of

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11

Chakraborty, Tandra Roy, Ales Vancura, Vivekanand S. Balija, and Dipak Haldar. "Phosphatidic Acid Synthesis in Mitochondria." Journal of Biological Chemistry 274, no. 42 (October 15, 1999): 29786–90. http://dx.doi.org/10.1074/jbc.274.42.29786.

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12

Wright, Lindsay M., Emily M. Carpinone, Terry L. Bennett, Mary K. Hondalus, and Vincent J. Starai. "VapA ofRhodococcus equibinds phosphatidic acid." Molecular Microbiology 107, no. 3 (December 22, 2017): 428–44. http://dx.doi.org/10.1111/mmi.13892.

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13

WANG, X., S. DEVAIAH, W. ZHANG, and R. WELTI. "Signaling functions of phosphatidic acid." Progress in Lipid Research 45, no. 3 (May 2006): 250–78. http://dx.doi.org/10.1016/j.plipres.2006.01.005.

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14

Yao, Jiangwei, and Charles O. Rock. "Phosphatidic acid synthesis in bacteria." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1831, no. 3 (March 2013): 495–502. http://dx.doi.org/10.1016/j.bbalip.2012.08.018.

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15

English, Denis, Yi Cui, and Rafat A. Siddiqui. "Messenger functions of phosphatidic acid." Chemistry and Physics of Lipids 80, no. 1-2 (May 1996): 117–32. http://dx.doi.org/10.1016/0009-3084(96)02549-2.

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16

Zhukovsky, Mikhail A., Angela Filograna, Alberto Luini, Daniela Corda, and Carmen Valente. "Phosphatidic acid in membrane rearrangements." FEBS Letters 593, no. 17 (August 31, 2019): 2428–51. http://dx.doi.org/10.1002/1873-3468.13563.

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17

Yang, Chia-Ying, and Michael A. Frohman. "Mitochondria: Signaling with phosphatidic acid." International Journal of Biochemistry & Cell Biology 44, no. 8 (August 2012): 1346–50. http://dx.doi.org/10.1016/j.biocel.2012.05.006.

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18

He, Y., and F. Grinnell. "Role of phospholipase D in the cAMP signal transduction pathway activated during fibroblast contraction of collagen matrices." Journal of Cell Biology 130, no. 5 (September 1, 1995): 1197–205. http://dx.doi.org/10.1083/jcb.130.5.1197.

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Fibroblast contraction of stressed collagen matrices results in activation of a cAMP signal transduction pathway. This pathway involves influx of extracellular Ca2+ ions and increased production of arachidonic acid. We report that within 5 min after initiating contraction, a burst of phosphatidic acid release was detected. Phospholipase D was implicated in production of phosphatidic acid based on observation of a transphosphatidylation reaction in the presence of ethanol that resulted in formation of phosphatidylethanol at the expense of phosphatidic acid. Activation of phospholipase D require

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19

Sim, Jae Ang, Jaehong Kim, and Dongki Yang. "Beyond Lipid Signaling: Pleiotropic Effects of Diacylglycerol Kinases in Cellular Signaling." International Journal of Molecular Sciences 21, no. 18 (September 18, 2020): 6861. http://dx.doi.org/10.3390/ijms21186861.

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The diacylglycerol kinase family, which can attenuate diacylglycerol signaling and activate phosphatidic acid signaling, regulates various signaling transductions in the mammalian cells. Studies on the regulation of diacylglycerol and phosphatidic acid levels by various enzymes, the identification and characterization of various diacylglycerol and phosphatidic acid-regulated proteins, and the overlap of different diacylglycerol and phosphatidic acid metabolic and signaling processes have revealed the complex and non-redundant roles of diacylglycerol kinases in regulating multiple biochemical a

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20

Ulcova-Gallova, Zdenka, Alice Mockova, and Miroslava Cedikova. "Screening Tests of Reproductive Immunology in Systemic Lupus Erythematosus." Autoimmune Diseases 2012 (2012): 1–6. http://dx.doi.org/10.1155/2012/812138.

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Female patients in reproductive age with systemic lupus erythematosus and fertility complications together are observed by rheumatologists, gynecologists, and reproductive immunologists. The paper notes the presence of autoantibodies to zona pellucida, to phospholipids (phosphatidyl serine, phosphatidyl ethanolamine, phosphatidyl inositol, phosphatidyl glycerol, phosphatidic acid, annexin V, beta-2 glycoprotein I, and cardiolipin) and of isoantibodies to sperm cells. Isoantibodies to sperm cells are not significantly predominant, but autoimmunity is well expressed in IgG positivity against pho

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21

Mürer, Erik H., and James L. Daniel. "Phosphorus Labeling of Proteins and Phospholipids in Intact Platelets in Response to pH 5.3." Thrombosis and Haemostasis 53, no. 01 (1985): 032–35. http://dx.doi.org/10.1055/s-0038-1661231.

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SummaryPrevious studies had shown that when gel-filtered or washed human platelets were incubated at pH 5.3, the cells secreted their granule-stored materials suggesting that low pH can act as a platelet activator. We determined here whether the effects of low pH on platelet protein phosphorylation and on platelet lipid metabolism were consistent with this view. When washed human platelets were incubated for 20 min at pH 5.3 and electrophoresed on SDS-PAGE, there was a great increase in 32P-label in the 20,000 and 47,000 dalton protein bands. There was also an increase in the labeling of phosp

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22

McDermott, Mark, Michael J. O. Wakelam, and Andrew J. Morris. "Phospholipase D." Biochemistry and Cell Biology 82, no. 1 (February 1, 2004): 225–53. http://dx.doi.org/10.1139/o03-079.

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Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals. Although enzymes with broader selectivity are found in some of the lower organisms, the plant, yeast, and mammalian enzymes are selective for phosphatidylcholine. The two mammalian phospholipase D isoforms are regulated by protein kinases and GTP binding proteins of the ADP-ribosylation and Rho families. Mammalian and ye

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23

English, D., G. Taylor, and JG Garcia. "Diacylglycerol generation in fluoride-treated neutrophils: involvement of phospholipase D." Blood 77, no. 12 (June 15, 1991): 2746–56. http://dx.doi.org/10.1182/blood.v77.12.2746.2746.

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Abstract Neutrophils exposed to fluoride ion (F-) respond with a delayed and sustained burst of superoxide anion release that is both preceded by and dependent on the influx of Ca2+ from the extracellular medium. The results of this study demonstrate a similarly delayed and sustained generation of 1,2-diglyceride in F(-)-treated neutrophils, over 90% of which was 1,2-diacylglycerol. Diacylglycerol generation was not dependent on the presence of extracellular Ca2+. Conversely, in contrast to results obtained with other agonists, removal of extracellular Ca2+ markedly potentiated synthesis of di

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24

English, D., G. Taylor, and JG Garcia. "Diacylglycerol generation in fluoride-treated neutrophils: involvement of phospholipase D." Blood 77, no. 12 (June 15, 1991): 2746–56. http://dx.doi.org/10.1182/blood.v77.12.2746.bloodjournal77122746.

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Neutrophils exposed to fluoride ion (F-) respond with a delayed and sustained burst of superoxide anion release that is both preceded by and dependent on the influx of Ca2+ from the extracellular medium. The results of this study demonstrate a similarly delayed and sustained generation of 1,2-diglyceride in F(-)-treated neutrophils, over 90% of which was 1,2-diacylglycerol. Diacylglycerol generation was not dependent on the presence of extracellular Ca2+. Conversely, in contrast to results obtained with other agonists, removal of extracellular Ca2+ markedly potentiated synthesis of diacylglyce

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25

Baker, R. Roy, and H. Y. Chang. "The acylation of 1-acyl-sn-glycero-3-phosphate by neuronal nuclei and microsomal fractions of immature rabbit cerebral cortex." Biochemistry and Cell Biology 68, no. 3 (March 1, 1990): 641–47. http://dx.doi.org/10.1139/o90-091.

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The acylation of 1-acyl-sn-glycero-3-phosphate to form phosphatidic acid was studied using a neuronal nuclear fraction N1 and microsomal fractions P3, R (rough), S (smooth), and P (neuronal microsomes from nerve cell bodies) isolated from cerebral cortices of 15-day-old rabbits. The assays contained this lysophospholipid, ATP, CoA, MgCl2, NaF, dithiothreitol, and radioactive palmitate, oleate, or arachidonate. Of the subfractions, N1 and R had the highest specific activities (expressed per micromole phospholipid in the fraction). The rates with oleate were two to four times the values seen for

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26

Viada, Benjamin, Candelaria I. Cámara, and Lidia M. Yudi. "Destabilizing effect of perfluorodecanoic acid on simple membrane models." Soft Matter 15, no. 11 (2019): 2447–62. http://dx.doi.org/10.1039/c8sm02301h.

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The surfactant perfluorodecanoic acid (PFD), widely used in different industrial applications and an important environmental contaminant, can penetrate distearoyl phosphatidic acid (DSPA), dilauroyl phosphatidic acid (DLPA) and distearoyl phosphatidylethanolamine (DSPE) monolayers, even at high pressures values, above 30 mN m<sup>−1</sup>, which is the accepted lateral pressure value for a cellular bilayer.

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27

Wright, T. M., S. Willenberger та D. M. Raben. "Activation of phospholipase D by α-thrombin or epidermal growth factor contributes to the formation of phosphatidic acid, but not to observed increases in 1,2-diacylglycerol". Biochemical Journal 285, № 2 (15 липня 1992): 395–400. http://dx.doi.org/10.1042/bj2850395.

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The receptor-mediated activation of a phosphatidylcholine-hydrolysing phospholipase D (PLD) has recently been described. We investigated the effect of alpha-thrombin and epidermal growth factor (EGF) on cellular PLD activity in order to determine the role of this enzyme in mitogen-induced increases in phosphatidic acid and sn-1,2-diacylglycerol. In the presence of ethanol, stimulation of [3H]myristic acid-labelled quiescent IIC9 cells with alpha-thrombin or EGF resulted in a rapid increase in radiolabelled phosphatidyl-ethanol which reached a plateau at 1 min, indicating the rapid and transien

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28

McNicol, Archibald, Jon M. Gerrard, and D. Euan MacIntyre. "Evidence for two mechanisms of thrombin-induced platelet activation: one proteolytic, one receptor mediated." Biochemistry and Cell Biology 67, no. 7 (July 1, 1989): 332–36. http://dx.doi.org/10.1139/o89-052.

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The possibility that thrombin-induced platelet reactivity could occur via both a receptor-related and a proteolytic process was examined. Thrombin elicited the formation of considerably more [32P)phosphatidic acid (an index of phospholipase C catalysed phosphoinositide metabolism) than did platelet activating factor, 5-hydroxytryptamine, ADP, and the thromboxane A2 analogue EP171, when these agents were added either alone or in combination. Co-addition of thrombin and EP171 did not evoke significantly more [32P]phosphatidic acid than did thrombin alone. The protease inhibitor leupeptin, decrea

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Jose Lopez-Andreo, Maria, Juan C. Gomez-Fernandez та Senena Corbalan-Garcia. "The Simultaneous Production of Phosphatidic Acid and Diacylglycerol Is Essential for the Translocation of Protein Kinase Cϵ to the Plasma Membrane in RBL-2H3 Cells". Molecular Biology of the Cell 14, № 12 (грудень 2003): 4885–95. http://dx.doi.org/10.1091/mbc.e03-05-0295.

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To evaluate the role of the C2 domain in protein kinase Cϵ (PKCϵ) localization and activation after stimulation of the IgE receptor in RBL-2H3 cells, we used a series of mutants located in the phospholipid binding region of the enzyme. The results obtained suggest that the interaction of the C2 domain with the phospholipids in the plasma membrane is essential for anchoring the enzyme in this cellular compartment. Furthermore, the use of specific inhibitors of the different pathways that generate both diacylglycerol and phosphatidic acid has shown that the phosphatidic acid generated via phosph

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30

Kooijman, Edgar E., Vladimir Chupin, Nola L. Fuller, Michael M. Kozlov, Ben de Kruijff, Koert N. J. Burger, and Peter R. Rand. "Spontaneous Curvature of Phosphatidic Acid and Lysophosphatidic Acid†." Biochemistry 44, no. 6 (February 2005): 2097–102. http://dx.doi.org/10.1021/bi0478502.

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31

Virto, Carmen, Ingemar Svensson, and Patrick Adlercreutz. "Enzymatic synthesis of lysophosphatidic acid and phosphatidic acid." Enzyme and Microbial Technology 24, no. 10 (July 1999): 651–58. http://dx.doi.org/10.1016/s0141-0229(98)00153-7.

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32

KASZKIN, Marietta, James RICHARDS, and Volker KINZEL. "Phosphatidic acid mobilized by phospholipase D is involved in the phorbol 12-myristate 13-acetate-induced G2 delay of A431 cells." Biochemical Journal 314, no. 1 (February 15, 1996): 129–38. http://dx.doi.org/10.1042/bj3140129.

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This study was aimed at gaining an understanding of metabolic events responsible for the inhibition of cells in G2 phase, a known physiological restriction site in the cell cycle of multicellular organisms. In an earlier study, phosphatidic acid was proposed as an inhibitory mediator in the epidermal growth factor (EGF)-induced inhibition of A431 cells in G2 phase via the phospholipase C pathway [Kaszkin, Richards and Kinzel (1992) Cancer Res. 52, 5627–5634]. We show here that the phorbol ester phorbol 12-myristate 13-acetate (PMA) induces a reversible inhibition of the G2/M transition in A431

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33

Banerji, Benoy, and Carl R. Alving. "Antibodies to liposomal phosphatidylserine and phosphatidic acid." Biochemistry and Cell Biology 68, no. 1 (January 1, 1990): 96–101. http://dx.doi.org/10.1139/o90-012.

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Polyclonal antisera to phosphatidylserine or phosphatidic acid were induced in rabbits by injecting liposomes containing phosphatidylserine or phosphatidic acid and lipid A. Adsorption of antisera with liposomes containing different phospholipids revealed that some degree of reactivity with one or more phospholipids other than the immunizing phospholipid was often observed. However, cross-reactivity with other phospholipids was not a universal phenomenon, and one antiserum to phosphatidylserine failed to cross-react (i.e., was not adsorbed) with liposomes containing other phospholipids. All of

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34

Tei, Reika, Johannes Morstein, Andrej Shemet, Dirk Trauner, and Jeremy M. Baskin. "Optical Control of Phosphatidic Acid Signaling." ACS Central Science 7, no. 7 (July 14, 2021): 1205–15. http://dx.doi.org/10.1021/acscentsci.1c00444.

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35

Gotoh, Mari, Aya Nagano, Ryoko Tsukahara, Hiromu Murofushi, Toshiro Morohoshi, Kazuyuki Otsuka, and Kimiko Murakami-Murofushi. "Cyclic Phosphatidic Acid Relieves Osteoarthritis Symptoms." Molecular Pain 10 (January 2014): 1744–8069. http://dx.doi.org/10.1186/1744-8069-10-52.

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36

Roberts, Roy, Vicki A. Sciorra, and Andrew J. Morris. "Human Type 2 Phosphatidic Acid Phosphohydrolases." Journal of Biological Chemistry 273, no. 34 (August 21, 1998): 22059–67. http://dx.doi.org/10.1074/jbc.273.34.22059.

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37

Gough, N. R. "Scaffolding Through Phosphatidic Acid-Enriched Domains." Science Signaling 2, no. 52 (January 6, 2009): ec6-ec6. http://dx.doi.org/10.1126/scisignal.252ec6.

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38

Guo, Liang, Girish Mishra, Kyle Taylor, and Xuemin Wang. "Phosphatidic Acid Binds and StimulatesArabidopsisSphingosine Kinases." Journal of Biological Chemistry 286, no. 15 (February 17, 2011): 13336–45. http://dx.doi.org/10.1074/jbc.m110.190892.

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39

STACE, C., and N. KTISTAKIS. "Phosphatidic acid- and phosphatidylserine-binding proteins." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1761, no. 8 (August 2006): 913–26. http://dx.doi.org/10.1016/j.bbalip.2006.03.006.

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40

Gomez-Cambronero, Julian. "Phosphatidic acid, phospholipase D and tumorigenesis." Advances in Biological Regulation 54 (January 2014): 197–206. http://dx.doi.org/10.1016/j.jbior.2013.08.006.

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41

Purkiss, J. R., and M. R. Boarder. "Stimulation of phosphatidate synthesis in endothelial cells in response to P2-receptor activation. Evidence for phospholipase C and phospholipase D involvement, phosphatidate and diacylglycerol interconversion and the role of protein kinase C." Biochemical Journal 287, no. 1 (October 1, 1992): 31–36. http://dx.doi.org/10.1042/bj2870031.

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To investigate the stimulation of phosphatidic acid formation in bovine aortic endothelial cells by P2-purinergic agonists, we labelled AG4762 cells with [32P]P1 and stimulated in the presence of butanol. Under these conditions phospholipase D generated [32P]phosphatidylbutanol, whereas the [32P]phosphatidic acid from phospholipase C and diacylglycerol kinase was unchanged. The action of various purinergic agonists on both [32P]phosphatidic acid and [32P]phosphatidylbutanol was consistent with the presence of a P2Y receptor. The stimulation of phospholipase D was dependent on extracellular Ca2

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Kurscheid-Reich, D., D. C. Throckmorton, and H. Rasmussen. "Serotonin activates phospholipase D in rat mesangial cells." American Journal of Physiology-Renal Physiology 268, no. 6 (June 1, 1995): F997—F1003. http://dx.doi.org/10.1152/ajprenal.1995.268.6.f997.

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We tested the hypothesis that serotonin activates phospholipase D (PLD) in cultured rat mesangial cells. The formation of phosphatidylethanol (PET) in ethanol was used as a measure of PLD activity. Serotonin [5-hydroxytryptamine (5-HT)] stimulated PET production, with an initial 10-fold increase in PET content within 15–30 s, followed by a decrease in PET to values only sixfold above baseline at 45–60 s. Thereafter, the values increased again at 5 min to a plateau 10-fold above baseline. The decrease in PET values, following the initial increase, was due to metabolism of PET, possibly by a pho

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Yu, Cao Guo, and Tony J. C. Harris. "Interactions between the PDZ domains of Bazooka (Par-3) and phosphatidic acid: in vitro characterization and role in epithelial development." Molecular Biology of the Cell 23, no. 18 (September 15, 2012): 3743–53. http://dx.doi.org/10.1091/mbc.e12-03-0196.

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Bazooka (Par-3) is a conserved polarity regulator that organizes molecular networks in a wide range of cell types. In epithelia, it functions as a plasma membrane landmark to organize the apical domain. Bazooka is a scaffold protein that interacts with proteins through its three PDZ (postsynaptic density 95, discs large, zonula occludens-1) domains and other regions. In addition, Bazooka has been shown to interact with phosphoinositides. Here we show that the Bazooka PDZ domains interact with the negatively charged phospholipid phosphatidic acid immobilized on solid substrates or in liposomes.

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Elabbadi, Noureddine, Christopher P. Day, Richard Virden, and Stephen J. Yeaman. "Regulation of phosphatidic acid phosphohydrolase 1 by fatty acids." Lipids 37, no. 1 (January 2002): 69–73. http://dx.doi.org/10.1007/s11745-002-0865-7.

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Craddock, Christian P., Nicolette Adams, Fiona M. Bryant, Smita Kurup, and Peter J. Eastmond. "PHOSPHATIDIC ACID PHOSPHOHYDROLASE Regulates Phosphatidylcholine Biosynthesis in Arabidopsis by Phosphatidic Acid-Mediated Activation of CTP:PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE Activity." Plant Cell 27, no. 4 (April 2015): 1251–64. http://dx.doi.org/10.1105/tpc.15.00037.

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Perry, D. K., V. L. Stevens, T. S. Widlanski, and J. D. Lambeth. "A novel ecto-phosphatidic acid phosphohydrolase activity mediates activation of neutrophil superoxide generation by exogenous phosphatidic acid." Journal of Biological Chemistry 268, no. 34 (December 1993): 25302–10. http://dx.doi.org/10.1016/s0021-9258(19)74392-0.

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Nozaki, Emi, Mari Gotoh, Ryo Tanaka, Masaru Kato, Takahiro Suzuki, Atsuo Nakazaki, Harumi Hotta, Susumu Kobayashi, and Kimiko Murakami-Murofushi. "Pharmacological evaluation of a novel cyclic phosphatidic acid derivative 3-S-cyclic phosphatidic acid (3-S-cPA)." Bioorganic & Medicinal Chemistry 20, no. 10 (May 2012): 3196–201. http://dx.doi.org/10.1016/j.bmc.2012.03.060.

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Halenda, S. P., and A. G. Rehm. "Evidence for the calcium-dependent activation of phospholipase D in thrombin-stimulated human erythroleukaemia cells." Biochemical Journal 267, no. 2 (April 15, 1990): 479–83. http://dx.doi.org/10.1042/bj2670479.

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Human erythroleukaemia (HEL) cells were exposed to thrombin and other platelet-activating stimuli, and changes in radiolabelled phospholipid metabolism were measured. Thrombin caused a transient fall in PtdInsP and PtdInsP2 levels, accompanied by a rise in diacylglycerol and phosphatidic acid, indicative of a classical phospholipase C/diacylglycerol kinase pathway. However, the rise in phosphatidic acid preceded that of diacylglycerol, which is inconsistent with phospholipase C/diacylglycerol kinase being the sole source of phosphatidic acid. In the presence of ethanol, thrombin and other agon

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Bonser, R. W., N. T. Thompson, R. W. Randall, and L. G. Garland. "Phospholipase D activation is functionally linked to superoxide generation in the human neutrophil." Biochemical Journal 264, no. 2 (December 1, 1989): 617–20. http://dx.doi.org/10.1042/bj2640617.

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Neutrophils stimulated with formylmethionyl-leucylphenylalanine (fMet-Leu-Phe) in the presence of butanol and ethanol formed phosphatidyl alcohols through a phospholipase D mechanism. The alcohols inhibited phosphatidic acid and diradylglycerol (DRG) formation, but did not block inositol 1, 4, 5-trisphosphate release. fMet-Leu-Phe-stimulated superoxide production was inhibited by alcohol concentrations which blocked DRG formation, whereas opsonized-zymosan-stimulated superoxide production was only partially decreased. These results suggest that phospholipase D activation is functionally linked

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ORLATI, Silvia, Anna M. PORCELLI, Silvana HRELIA, Antonello LORENZINI, and Michela RUGOLO. "Intracellular calcium mobilization and phospholipid degradation in sphingosylphosphorylcholine-stimulated human airway epithelial cells." Biochemical Journal 334, no. 3 (September 15, 1998): 641–49. http://dx.doi.org/10.1042/bj3340641.

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Extracellular sphingosylphosphorylcholine (SPC) caused a remarkable elevation in the intracellular Ca2+ concentration ([Ca2+]i) in immortalized human airway epithelial cells (CFNP9o-). An increase in total inositol phosphates formation was determined; however, the dose responses for [Ca2+]i elevation and inositol phosphates production were slightly different and, furthermore, PMA and pertussis toxin almost completely inhibited [Ca2+]i mobilization by SPC, whereas inositol phosphates production was only partially reduced. The possible direct interaction of SPC with Ca2+ channels of intracellula

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