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Journal articles on the topic 'Phosphatidic acid'

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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-PAPase; both saturated and unsaturated long chain phosphatidic acids were relatively resistant to hydrolysis. Both long (C18:1) and short (C8) chain lyso-phosphatidic acids were hydrolysed at rates comparable with those observed for short chain (diC8) phosphatidic acid. Activity of the ecto-enzyme accounted for essentially all of the N-ethylmaleimide-insensitive, Mg2+-independent PAPase activity recovered from disrupted neutrophils. At 37 °C and pH 7.2, the apparent Km for dioctanoyl phosphatidic acid (diC8PA) was 1.4×10-3 M. Other phosphatidic acids and lysophosphatidic acids inhibited hydrolysis of [32P]diC8PA in a rank order that correlated with competitor solubility, lysophosphatidic acids and unsaturated phosphatidic acids being much more effective inhibitors than long chain saturated phosphatidic acids. Dioleoyl (C18:1) phosphatidic acid was an unexpectedly strong inhibitor of activity, in comparison with its ability to act as a direct substrate in the absence of detergent. Other inhibitors of neutrophil ecto-PAPase included sphingosine, dimethyl- and dihydro-sphingosine, propranolol, NaF and MgCl2. Of several leucocyte populations isolated from human blood by FACS, including T cells, B cells, NK lymphocytes and monocytes, ecto-PAPase was most prevalent on neutrophils; erythrocytes were essentially devoid of activity. A non-hydrolysable, phosphonate analogue of phosphatidic acid, phosphonate 1, efficiently solubilized catalytic activity from intact neutrophils without causing cell disruption or increasing permeability. Enzyme activity in solubilized extracts was purified in the absence of detergent by successive heparin–Sepharose, gel filtration and anion exchange chromatography. By assaying activity in renatured SDS/polyacrylamide gel slices, the molecular mass of neutrophil ecto-PAPase was estimated to be between 45 and 52 kDa, similar to the molecular mass of previously purified plasma membrane PAPases. Since a large portion of neutrophil plasma membrane PAPase is available for hydrolysis of exogenous substrates, ecto-PAPase may play an important role in regulating inflammatory cell responses to extracellular phosphatidic acid in biological systems.
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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 prelabelled with [1-14C]oleic acid, EGF (10 and 100 nM respectively) caused a 3-fold increase in radioactive phosphatidylbutanol within 5 min at the expense of labelled phosphatidic acid. Dose-response relationships showed 10 nM- and 100 nM-EGF to be maximally effective in HeLa cells and A431 cells respectively. Mass determinations showed that the phosphatidylbutanol formed within 5 min represented only part of the phosphatidic acid. Depletion of protein kinase C by pretreatment of A431 cells for 17 h with the phorbol ester phorbol 12-myristate 13-acetate (0.1 microM) did not impair EGF-induced formation of phosphatidylbutanol, thus indicating that the reaction was independent of this enzyme. Since phosphatidic acid is suggested to exert second-messenger functions as well as to induce biophysical changes in cellular membranes, its formation, including that via the phospholipase D pathway, may represent an important link between extracellular signals and intracellular targets.
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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 intracellular source. The co-administration of glucagon (or cyclic AMP) and phosphatidic acid, and also of glucagon and arachidonic acid, led to a synergistic stimulation of Ca2+ uptake of the liver, a feature similar to that observed after the co-administration of glucagon and other Ca2+-mobilizing hormones [Altin & Bygrave (1986) Biochem. J. 238, 653-661]. A notable difference, however, is that the synergistic stimulation of Ca2+ uptake induced by the co-administration of glucagon and arachidonic acid was inhibited by indomethacin, whereas that induced by glucagon and phosphatidic acid, or glucagon and other Ca2+-mobilizing agents, was not. The results suggest that the synergistic action of glucagon and arachidonic acid in stimulating Ca2+ influx is mediated by prostanoids, but that of glucagon and phosphatidic acid is evoked by a mechanism similar to that of Ca2+-mobilizing agents.
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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 accumulated in triacylglycerol from phosphatidic acid. Diacylglycerol acyltransferase, therefore, may not play a major role in oil formation as originally envisaged and other enzymes, including diacylglycerol: diacylglycerol transacylase [Stobart, Mancha, Lenman, Dahlqvist and Stymne (1997) Planta 203, 58–66] may have important biosynthetic functions.
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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 and further confirms the amidation reaction. The main acyl residue of the synthesized surfactants are hydrocarbon chain of linoleic acid however, while the detection of methylene groups near double bonds indicates the presence of other fatty acids (oleic, linolenic and gadolein), this corresponds to the fatty acid composition of the original phosphatidic sludge. Synthesized surfactants are effective emulsifiers-stabilizers for dispersed systems. The use of environmentally friendly components in the composition of surfactants improves their biodegradability to 83–86%.
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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 has been generally thought that all DGK isozymes utilize the DG species derived from the turnover. However, it was recently revealed that DGK isozymes, except for DGKε, phosphorylate diverse DG species, which are not derived from phosphatidylinositol turnover. In addition, various PA-binding proteins (PABPs), which have different selectivities for PA species, were recently found. These results suggest that DGK–PA–PABP axes can potentially construct a large and complex signaling network and play physiologically and pathologically important roles in addition to DGK-dependent attenuation of DG–DG-binding protein axes. For example, 1-stearoyl-2-docosahexaenoyl-PA produced by DGKδ interacts with and activates Praja-1, the E3 ubiquitin ligase acting on the serotonin transporter, which is a target of drugs for obsessive-compulsive and major depressive disorders, in the brain. This article reviews recent research progress on PA species produced by DGK isozymes, the selective binding of PABPs to PA species and a phosphatidylinositol turnover-independent DG supply pathway.
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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 phosphatidic acid protected against immune mediated liver inflammation induced by concanavalin A, but worsened tumor spread in the B16F10 melanoma lung metastasis model. Phosphatidic acid reduced pro-inflammatory cytokines but increased anti-inflammatory cytokine interleukin-10 in the liver. Phosphatidic acid did so by inducing the mobilization and migration from the bone marrow to peripheral organs of Ly6C+ myeloid cells that upon adoptive transfer protected against autoimmune liver inflammation. Our novel observations indicating immune suppressive functions of phosphatidic acid may have wide implications for a variety of conditions with altered lipid metabolism and inflammation such as atherosclerosis and autoimmune disease and conditions with local or systemic alterations in phosphatidic acid such as osteoarthritis and Alzheimer’s disease.
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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 required extracellular Ca2+ ions and was regulated by protein kinase C. Ethanol treatment of cells also inhibited by 60-70% contraction-dependent release of arachidonic acid and cAMP but had no effect on increased cAMP synthesis after addition of exogenous arachidonic acid or on phospholipase A2 activity measured in cell extracts. Moreover, other treatments that inhibited the burst of phosphatidic acid release after contraction--chelating extracellular Ca2+ or down-regulating protein kinase C--also blocked contraction activated cyclic AMP signaling. These results were consistent with the idea that phosphatidic acid production occurred upstream of arachidonic acid in the contraction-activated cAMP signaling pathway.
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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 and biological networks. In this review article, we summarized recent progress in the complex and non-redundant roles of diacylglycerol kinases, which is expected to aid in restoring dysregulated biochemical and biological networks in various pathological conditions at the bed side.
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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 phosphatidyl inositol, phosphatidyl ethanolamine, phosphatidyl serine, cardiolipin, and beta-2 glycoprotein I, as well as antizona pellucida antibodies in IgG isotype. According to the levels of autoantibodies we have to choose preventive treatment to protect mother and her foetus.
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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 phosphatidic acid and a small decrease in phosphatidyl inositol. When the platelets were returned to pH 7.6, the 32P labeling of the 20,000 and 47,000 dalton bands was greatly reduced, and that of phosphatidic acid reduced to the control value, while the labeling of phosphatidyl inositol was increased above control. Incubation at pH 5.3 for 60 min gave the same pattern, but return to pH 7.6 resulted in only partial reversal of labeling of the two protein bands and little decrease in the label associated with phosphatidic acid, but the radioactivity in phosphatidyl inositol was greatly increased. The changes in the 32P-labeling of phospholipids and proteins after incubation of platelets at pH 5.3 may reflect an increase in cytoplasmic Ca++ resulting from leakage of Ca++ from intracellular storage sites, a process which becomes irreversible after longer time exposure to the low pH. The activation of human platelets at pH 5.3 is a slow process which may not be directly comparable to the fast events in the normal stimulation-response coupling, but which is accompanied by changes common to platelet activation. Most interesting in this respect is that a return to physiological conditions will reverse these events, although prolonged exposure will make them irreversible. These studies may therefore present a way to study the boundary between reversible and irreversible processes in platelets.
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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 yeast phospholipases D are also potently stimulated by phosphatidylinositol 4,5-bisphosphate. This review discusses the identification, characterization, structure, and regulation of phospholipase D. Genetic and pharmacological approaches implicate phospholipase D in a diverse range of cellular processes that include receptor signaling, control of intracellular membrane transport, and reorganization of the actin cytoskeleton. Most ideas about phospholipase D function consider that the phosphatidic acid product is an intracellular lipid messenger. Candidate targets for phospholipase-D-generated phosphatidic acid include phosphatidylinositol 4-phosphate 5-kinases and the raf protein kinase. Phosphatidic acid can also be converted to two other lipid mediators, diacylglycerol and lyso phosphatidic acid. Coordinated activation of these phospholipase-D-dependent pathways likely accounts for the pleitropic roles for these enzymes in many aspects of cell regulation.Key words: phospholipase D, phosphatidic acid, GTP-binding proteins, membrane transport, cytoskeletal regulation.
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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 diacylglycerol in F(-)-treated neutrophils. This effect was accompanied by a corresponding decrease in the recovery of phosphatidic acid. In either the presence or absence of extracellular Ca2+, phosphatidic acid accumulated before diacylglycerol in F(-)-treated cells, suggesting the latter was derived from the former. Consistent with this hypothesis, the phosphatidic acid phosphohydrolase inhibitor, propranolol, suppressed generation of diacylglycerol as it potentiated the accumulation of phosphatidic acid in F(-)-treated neutrophils. This effect was observed both in the presence and absence of extracellular Ca2+. Moreover, high levels of propranolol (160 mumol/L) effected complete inhibition of diacylglycerol generation in F(-)-treated neutrophils with a corresponding increase in phosphatidic acid generation. Phosphatidylethanol accumulated in neutrophils stimulated with F- in the presence of ethanol. The extent of phosphatidylethanol accumulation at all time points after addition of F- corresponded to decreased levels of both phosphatidic acid and diacylglycerol, indicating that phosphatidylethanol was derived from the phospholipase D-catalysed transphosphatidylation reaction. The results indicate that F- activates a Ca(2+)-independent phospholipase D, which appears to be the major, if not sole, catalyst for both phosphatidic acid and diacylglycerol generation in F(-)-treated neutrophils. Ca2+, mobilized as a result of F- stimulation and possibly as a consequence of phospholipase D activation, exerts a profound effect on cellular second messenger levels by modulating the conversion of phosphatidic acid to diacylglycerol.
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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 diacylglycerol in F(-)-treated neutrophils. This effect was accompanied by a corresponding decrease in the recovery of phosphatidic acid. In either the presence or absence of extracellular Ca2+, phosphatidic acid accumulated before diacylglycerol in F(-)-treated cells, suggesting the latter was derived from the former. Consistent with this hypothesis, the phosphatidic acid phosphohydrolase inhibitor, propranolol, suppressed generation of diacylglycerol as it potentiated the accumulation of phosphatidic acid in F(-)-treated neutrophils. This effect was observed both in the presence and absence of extracellular Ca2+. Moreover, high levels of propranolol (160 mumol/L) effected complete inhibition of diacylglycerol generation in F(-)-treated neutrophils with a corresponding increase in phosphatidic acid generation. Phosphatidylethanol accumulated in neutrophils stimulated with F- in the presence of ethanol. The extent of phosphatidylethanol accumulation at all time points after addition of F- corresponded to decreased levels of both phosphatidic acid and diacylglycerol, indicating that phosphatidylethanol was derived from the phospholipase D-catalysed transphosphatidylation reaction. The results indicate that F- activates a Ca(2+)-independent phospholipase D, which appears to be the major, if not sole, catalyst for both phosphatidic acid and diacylglycerol generation in F(-)-treated neutrophils. Ca2+, mobilized as a result of F- stimulation and possibly as a consequence of phospholipase D activation, exerts a profound effect on cellular second messenger levels by modulating the conversion of phosphatidic acid to diacylglycerol.
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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 phosphatidic acid formation from sn-[3H]glycero-3-phosphate and oleoyl-CoA. Using oleate or palmitate, fraction R had superior specific rates to N1 at low lysophosphatidic acid concentrations. With increasing lysophospholipid concentrations the specific rates of N1 and R came closer together and maintained at least a twofold superiority over fraction P. Fraction S had the lowest specific rates of phosphatidic acid formation. Fractions N1, R, and P showed a preference for palmitate and oleate over arachidonate, particularly at low concentrations of lysophosphatidic acid. For N1 and R, the preference was also more marked at higher concentrations of fatty acid. Thus a selectivity for saturated and monounsaturated fatty acids was shown in the formation of phosphatidic acid, as was a concentration of acylating activity in the neuronal nucleus and the rough endoplasmic reticulum.Key words: 1-acyl-sn-glycero-3-phosphate, acylation, neuronal nuclei, microsomes, cerebral cortex.
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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−1, which is the accepted lateral pressure value for a cellular bilayer.
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Wright, T. M., S. Willenberger, and 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, no. 2 (July 15, 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 transient activation of PLD. We observed a concomitant decrease in the mitogen-stimulated increase of radiolabelled phosphatidic acid. In contrast, ethanol did not significantly effect the elevation of sn-1,2-diacylglycerol levels stimulated by alpha-thrombin or EGF as determined by measurement of sn-1,2-diacylglycerol mass or the appearance of [3H]1,2-diacylglycerol. A novel lipid, detected by two-dimensional t.l.c. analysis, was generated in [3H]myristic acid-labelled cells stimulated with alpha-thrombin, but not EGF, in the presence of ethanol. Treatment in vitro of cellular lipids isolated from [3H]myristic acid-labelled cultures with PLD in the presence of ethanol also resulted in the generation of this novel lipid species, supporting the role of this enzyme in its production. These data indicate that in quiescent IIC9 cells: (a) alpha-thrombin or EGF rapidly and transiently activates a PLD; (b) although this activation is responsible for part of the mitogen-induced increases in phosphatidic acid, it does not contribute to induced increases in sn-1,2-diacylglycerol; and (c) activation of this enzyme appears to be involved in the formation of a novel lipid generated in response to alpha-thrombin, but not EGF, in IIC9 fibroblasts.
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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, decreased but did not abolish [32P]phosphatidic acid formation elicited by either thrombin alone or thrombin in combination with EP171. The serine protease, trypsin, stimulated an increase in [32P]phosphatidic acid and this effect was additive with that of EP171. This augmentation by trypsin of EP171-induced [32P]phosphatidic acid formation was inhibited by leupeptin. These results are consistent with the concept that thrombin-induced activation of phospholipase C occurs by two distinct mechanisms: one via proteolysis, which is sensitive to leupeptin, and the other via receptor activation, a process shared by EP171. The individual components of this dual mechanism can be mimicked by the co-addition of a receptor-directed agonist (EP171) and a proteolytic agent (trypsin).Key words: platelet, thrombin, proteolysis, phosphoinositide.
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29

Jose Lopez-Andreo, Maria, Juan C. Gomez-Fernandez, and 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, no. 12 (December 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 phospholipase D (PLD)-dependent pathway, in addition to the diacylglycerol generated via phosphoinosite-phospholipase C (PLC), are involved in the localization of PKCϵ in the plasma membrane. Direct stimulation of RBL-2H3 cells with very low concentrations of permeable phosphatidic acid and diacylglycerol exerted a synergistic effect on the plasma membrane localization of PKCϵ. Moreover, the in vitro kinase assays showed that both phosphatidic acid and diacylglycerol are essential for enzyme activation. Together, these results demonstrate that phosphatidic acid is an important and essential activator of PKCϵ through the C2 domain and locate this isoenzyme in a new scenario where it acts as a downstream target of PLD.
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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 cells under conditions of phospholipase D-catalysed phosphatidic acid formation. Such PMA-induced inhibition in G2 phase is largely attenuated in the presence of 1-propanol (but not of 2-propanol). In this case the amount of phosphatidic acid is reduced to almost control levels, and instead phosphatidylpropanol is formed. In the case of EGF-induced activation of a phospholipase D the amount of phosphatidic acid is only slightly decreased in the presence of a primary alcohol. Under these conditions the EGF-induced G2 delay was not affected. The correlation between the formation of phosphatidic acid and the G2 delay induced by PMA, as well as by an exogenous bacterial phospholipase D (from Streptomyces chromofuscus), could be supported by using synchronized cells in order to increase the population of cells in G2 phase. This study indicates that the formation of substantial amounts of phosphatidic acid immediately before entry into mitosis seems to be important for establishing a delay in the cell cycle at the G2/M border by exogenous ligands.
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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 the antisera were inhibited by soluble phosphorylated haptens (e.g., phosphocholine but not choline), but one of the antisera to phosphatidylserine was inhibited both by phosphoserine and by serine alone. Liposomal membrane composition influenced the activity of antiserum to phosphatidylserine. Regardless of whether unsaturated (beef brain) or saturated (dimyristoyl) phosphatidylserine was used in the immunizing liposomes, the antisera reacted more vigorously with liposomes containing unsaturated than saturated phosphatidylserine. We conclude that liposomes containing lipid A can serve as vehicles for stimulating polyclonal antisera to phosphatidylserine and phosphatidic acid. Although cross-reactivity with certain other phospholipids can be observed, sera from selected animals apparently can exhibit a high degree of specific activity to the immunizing phospholipid antigen.Key words: liposomes, antibodies, phospholipids, phosphatidylserine, phosphatidic acid.
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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+ and was mostly transient (completed within 3 min), whereas the initial stimulation of phospholipase C was independent of extracellular Ca2+, followed by a Ca(2+)-dependent phase. The agonist stimulation of phospholipase D was dependent on protein kinase C, as judged by its sensitivity to the relatively selective protein kinase C inhibitor Ro 31-8220. These results show that purinergic-receptor-mediated stimulation of phosphatidic acid has three phases: an initial Ca(2+)-independent stimulation of phospholipase C, an early but transient Ca(2+)- and protein kinase C-dependent stimulation of phospholipase D, and a sustained Ca(2+)-dependent stimulation of phospholipase C. Using propranolol to inhibit phosphatidate phosphohydrolase, we provide evidence that phosphatidic acid derived from purinergic-receptor-mediated stimulation of the phospholipase C/diacylglycerol kinase route can itself be converted back into diacylglycerol.
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42

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 phosphatidic acid phosphohydrolase, which led to a 76% decrease in PET within 1 h. Inhibition of phosphohydrolase with propranolol increased the phosphatidic acid and decreased the 1,2-diacylglycerol (DAG) content of 5-HT-stimulated cells. Finally, exogenous PLD induced mesangial cell proliferation as well as increases in phosphatidic acid, PET, and DAG. We conclude that phosphatidic acid contributes to DAG formation in mesangial cells. Furthermore, we suggest that PLD is involved in 5-HT-mediated mesangial cell proliferation.
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43

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. The interaction requires multiple PDZ domains, and conserved patches of positively charged amino acid residues appear to mediate the interaction. Increasing or decreasing levels of diacylglycerol kinase or phospholipase D—enzymes that produce phosphatidic acid—reveal a role for phosphatidic acid in Bazooka embryonic epithelial activity but not its localization. Mutating residues implicated in phosphatidic acid binding revealed a possible role in Bazooka localization and function. These data implicate a closer connection between Bazooka and membrane lipids than previously recognized. Bazooka polarity landmarks may be conglomerates of proteins and plasma membrane lipids that modify each other's activities for an integrated effect on cell polarity.
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44

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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45

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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46

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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47

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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48

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 agonists (platelet-activating factor, adrenaline and ADP, as well as fetal-calf serum) stimulated the appearance of phosphatidylethanol, an indicator of phospholipase D activity. The Ca2+ ionophore A23187 and the protein kinase C activator phorbol myristate acetate (PMA) also elicited phosphatidylethanol formation, although A23187 was at least 5-fold more effective than PMA. Phosphatidylethanol production stimulated by agonists or A23187 was Ca2(+)-dependent, whereas that with PMA was not. These result suggest that phosphatidic acid is generated in agonist-stimulated HEL cells by two routes: phospholipase C/diacylglycerol kinase and phospholipase D. Activation of the HEL-cell phospholipase D in response to agonists may be mediated by a rise in intracellular Ca2+.
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49

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 to superoxide production in the human neutrophil.
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50

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 intracellular stores was determined by experiments with permeabilized cells, where SPC failed to evoke Ca2+ release, whereas lysophosphatidic acid was shown to be effective. The level of phosphatidic acid was increased by SPC only in the presence of AACOCF3, a specific inhibitor of phospholipase A2 (PLA2) and blocked by both pertussis toxin and R59022, an inhibitor of diacylglycerol kinase. R59022 enhanced diacylglycerol production by SPC and also significantly reduced [Ca2+]i mobilization. Only polyunsaturated diacylglycerol and phosphatidic acid were generated by SPC. Lastly, SPC caused stimulation of arachidonic acid release, indicating the involvement of PLA2. Taken together, these data suggest that, after SPC stimulation, phospholipase C-derived diacylglycerol is phosphorylated by a diacylglycerol kinase to phosphatidic acid, which is further hydrolysed by PLA2 activity to arachidonic and lysophosphatidic acids. We propose that lysophosphatidic acid might be the intracellular messenger able to release Ca2+ from internal stores.
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