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Journal articles on the topic 'Phospholipase D'

Author: Grafiati

Published: 4 June 2021

Last updated: 21 February 2023

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1

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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2

Dhand, Rajiv, Jared Young, Andelle Teng, Subbiah Krishnasamy, and Nicholas J. Gross. "Is dipalmitoylphosphatidylcholine a substrate for convertase?" American Journal of Physiology-Lung Cellular and Molecular Physiology 278, no. 1 (January 1, 2000): L19—L24. http://dx.doi.org/10.1152/ajplung.2000.278.1.l19.

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Convertase has homology with carboxylesterases, but its substrate(s) is not known. Accordingly, we determined whether dipalmitoylphosphatidylcholine (DPPC), the major phospholipid in surfactant, was a substrate for convertase. We measured [3H]choline release during cycling of the heavy subtype containing [3H]choline-labeled DPPC with convertase, phospholipases A2, B, C, and D, liver esterase, and elastase. Cycling with liver esterase or peanut or cabbage phospholipase D produced the characteristic profile of heavy and light peaks observed on cycling with convertase. In contrast, phospholipases A2, B, and C and yeast phospholipase D produced a broad band of radioactivity across the gradient without distinct peaks. [3H]choline was released when natural surfactant containing [3H]choline-labeled DPPC was cycled with yeast phospholipase D but not with convertase or peanut and cabbage phospholipases D. Similarly, yeast phospholipase D hydrolyzed [3H]choline from [3H]choline-labeled DPPC after incubation in vitro, whereas convertase, liver esterase, or peanut and cabbage phospholipases D did not. Thus convertase, liver esterase, and plant phospholipases D did not hydrolyze choline from DPPC either on cycling or during incubation with enzyme in vitro. In conclusion, conversion of heavy to light subtype of surfactant by convertase may require a phospholipase D type hydrolysis of phospholipids, but the substrate in this reaction is not DPPC.

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3

Bollag, Wendy B. "Role of phospholipases in adrenal steroidogenesis." Journal of Endocrinology 229, no. 1 (April 2016): R29—R41. http://dx.doi.org/10.1530/joe-16-0007.

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Phospholipases are lipid-metabolizing enzymes that hydrolyze phospholipids. In some cases, their activity results in remodeling of lipids and/or allows the synthesis of other lipids. In other cases, however, and of interest to the topic of adrenal steroidogenesis, phospholipases produce second messengers that modify the function of a cell. In this review, the enzymatic reactions, products, and effectors of three phospholipases, phospholipase C, phospholipase D, and phospholipase A2, are discussed. Although much data have been obtained concerning the role of phospholipases C and D in regulating adrenal steroid hormone production, there are still many gaps in our knowledge. Furthermore, little is known about the involvement of phospholipase A2, perhaps, in part, because this enzyme comprises a large family of related enzymes that are differentially regulated and with different functions. This review presents the evidence supporting the role of each of these phospholipases in steroidogenesis in the adrenal cortex.

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4

EXTON, JOHN H. "Phospholipase D." Annals of the New York Academy of Sciences 905, no. 1 (January 25, 2006): 61–68. http://dx.doi.org/10.1111/j.1749-6632.2000.tb06538.x.

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5

Exton, John H. "Phospholipase D." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1436, no. 1-2 (December 1998): 105–15. http://dx.doi.org/10.1016/s0005-2760(98)00124-6.

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6

Gomez-Cambronero, Julian, and Paul Keire. "Phospholipase D." Cellular Signalling 10, no. 6 (June 1998): 387–97. http://dx.doi.org/10.1016/s0898-6568(97)00197-6.

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7

Wakelam, Michael J. O., Matthew N. Hodgkin, Ashley Martin, and Khalid Saqib. "Phospholipase D." Seminars in Cell & Developmental Biology 8, no. 3 (June 1997): 305–10. http://dx.doi.org/10.1006/scdb.1997.0152.

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8

Inamori, K., N. Sagawa, M. Hasegawa, H. Itoh, J. Yano, and T. Mori. "Activation of phospholipase D in cultured human amnion cells." Reproduction, Fertility and Development 7, no. 6 (1995): 1591. http://dx.doi.org/10.1071/rd9951591.

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The regulation of phospholipase D (PLD) activity in the human amniotic membrane was examined using primary cultures of amnion cells. Cultured amnion cells were labelled with [3H]oleic acid, and PLD activity was determined as the amount of [3H]phosphatidylethanol (PEt) produced during incubation in the presence of 0.1% ethanol. PLD activity in cultured amnion cells was activated by addition of arginine vasopressin and oxytocin. PLD activity was also stimulated by treatment was arachidonic acid, the product of phospholipase A2 (PLA2), and phospholipase C (PLC). These results indicate that PLD in amnion cells is activated by substances present in amniotic fluid, and that cross-talk between phospholipases A2, C and D may occur in amnion cells.

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9

Min, Do Sik. "The Functional Role of Phospholipase D Isozymes in Apoptosis." Journal of Life Science 24, no. 12 (December 30, 2014): 1378–82. http://dx.doi.org/10.5352/jls.2014.24.12.1378.

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10

Alvarez-Breckenridge, Christopher A., Kristin A. Waite, and Charis Eng. "PTEN regulates phospholipase D and phospholipase C." Human Molecular Genetics 16, no. 10 (April 3, 2007): 1157–63. http://dx.doi.org/10.1093/hmg/ddm063.

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11

Song, J. G., L. M. Pfeffer, and D. A. Foster. "v-Src increases diacylglycerol levels via a type D phospholipase-mediated hydrolysis of phosphatidylcholine." Molecular and Cellular Biology 11, no. 10 (October 1991): 4903–8. http://dx.doi.org/10.1128/mcb.11.10.4903-4908.1991.

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Activating the protein-tyrosine kinase of v-Src in BALB/c 3T3 cells results in rapid increases in the intracellular second messenger, diacylglycerol (DAG). v-Src-induced increases in radiolabeled DAG were most readily detected when phospholipids were prelabeled with myristic acid, which is incorporated predominantly into phosphatidylcholine. Consistent with this observation, v-Src increased the level of intracellular choline. No increase in DAG was observed when cells were prelabeled with arachidonic acid, which is incorporated predominantly into phosphatidylinositol. Inhibiting phosphatidic acid (PA) phosphatase, which hydrolyzes PA to DAG, blocked v-Src-induced DAG production and enhanced PA production, implicating a type D phospholipase. Consistent with the involvement of a type D phospholipase, v-Src increased transphosphatidylation activity, which is characteristic of type D phospholipases. Thus, v-Src-induced increases in DAG most likely result from the activation of a type D phospholipase/PA phosphatase-mediated signaling pathway.

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12

Song, J. G., L. M. Pfeffer, and D. A. Foster. "v-Src increases diacylglycerol levels via a type D phospholipase-mediated hydrolysis of phosphatidylcholine." Molecular and Cellular Biology 11, no. 10 (October 1991): 4903–8. http://dx.doi.org/10.1128/mcb.11.10.4903.

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Activating the protein-tyrosine kinase of v-Src in BALB/c 3T3 cells results in rapid increases in the intracellular second messenger, diacylglycerol (DAG). v-Src-induced increases in radiolabeled DAG were most readily detected when phospholipids were prelabeled with myristic acid, which is incorporated predominantly into phosphatidylcholine. Consistent with this observation, v-Src increased the level of intracellular choline. No increase in DAG was observed when cells were prelabeled with arachidonic acid, which is incorporated predominantly into phosphatidylinositol. Inhibiting phosphatidic acid (PA) phosphatase, which hydrolyzes PA to DAG, blocked v-Src-induced DAG production and enhanced PA production, implicating a type D phospholipase. Consistent with the involvement of a type D phospholipase, v-Src increased transphosphatidylation activity, which is characteristic of type D phospholipases. Thus, v-Src-induced increases in DAG most likely result from the activation of a type D phospholipase/PA phosphatase-mediated signaling pathway.

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13

Tanabe, Kumiko, Osamu Kozawa, Hiroyuki Matsuno, Masayuki Niwa, Shuji Dohi, and Toshihiko Uematsu. "Effect of Propofol on Arachidonate Cascade by Vasopressin in Aortic Smooth Muscle Cells." Anesthesiology 90, no. 1 (January 1, 1999): 215–24. http://dx.doi.org/10.1097/00000542-199901000-00028.

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Background The mechanisms underlying the vascular effects of propofol are not fully understood. Vasopressin, a potent vasoactive peptide, stimulates the arachidonate cascade and the synthesis of prostacyclin (PGI2; the main metabolite of the cascade in vascular smooth muscle cells). Arachidonic acid (AA) release by phospholipases is the rate-limiting step in the cascade. We investigated the mechanisms underlying vasopressin-induced AA release and the effect of propofol on PGI2 synthesis in a rat aortic smooth muscle cell line: A10 cells. Methods In cultured A10 cells pretreated with propofol, the stimulation by vasopressin of AA release and PGI2 synthesis was evaluated by measuring [3H]AA and 6-keto PGF1alpha, respectively, in the culture medium. The effects of propofol on vasopressin-induced activation of phosphoinositide-hydrolyzing phospholipase C and phosphatidylcholine-hydrolyzing phospholipase D were evaluated by measuring inositol phosphate formation and choline formation, respectively. Results A phospholipase C inhibitor and a phosphatidic acid phosphohydrolase inhibitor both attenuated vasopressin-induced AA release and PGI2 synthesis, as did a phospholipase A2 inhibitor. Propofol inhibited vasopressin-induced activation of phosphoinositide-hydrolyzing phospholipase C and phosphatidylcholine-hydrolyzing phospholipase D, but this effect of propofol was significant only at supraclinical concentration (0.1 mM). Propofol reduced vasopressin-induced PGI2 synthesis. The inhibitory effect was observed at concentrations (10 microM-0.1 mM) higher than those used clinically. Conclusions Propofol suppresses the arachidonate cascade caused by vasopressin at least partly by inhibiting phosphoinositide-hydrolyzing phospholipase C and phosphatidylcholine-hydrolyzing phospholipase D, resulting in the inhibition of PGI2 synthesis. Propofol-mediated inhibition of vasopressin-stimulated synthesis of PGI2 may reduce the vasorelaxation by propofol.

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14

Cross, M. J., M. N. Hodgkin, S. Roberts, E. Landgren, M. J. Wakelam, and L. Claesson-Welsh. "Tyrosine 766 in the fibroblast growth factor receptor-1 is required for FGF-stimulation of phospholipase C, phospholipase D, phospholipase A(2), phosphoinositide 3-kinase and cytoskeletal reorganisation in porcine aortic endothelial cells." Journal of Cell Science 113, no. 4 (February 15, 2000): 643–51. http://dx.doi.org/10.1242/jcs.113.4.643.

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Fibroblast growth factor-mediated signalling was studied in porcine aortic endothelial cells expressing either wild-type fibroblast growth factor receptor-1 or a mutant receptor (Y766F) unable to bind phospholipase C-(γ). Stimulation of cells expressing the wild-type receptor resulted in activation of phospholipases C, D and A(2) and increased phosphoinositide 3-kinase activity. Stimulation of the wild-type receptor also resulted in stress fibre formation and a cellular shape change. Cells expressing the Y766F mutant receptor failed to stimulate phospholipase C, D and A(2) as well as phosphoinositide 3-kinase. Furthermore, no stress fibre formation or shape change was observed. Both the wild-type and Y766F receptor mutant activated MAP kinase and elicited proliferative responses in the porcine aortic endothelial cells. Thus, fibroblast growth factor receptor-1 mediated activation of phospholipases C, D and A(2) and phosphoinositide 3-kinase was dependent on tyrosine 766. Furthermore, whilst tyrosine 766 was not required for a proliferative response, it was required for fibroblast growth factor receptor-1 mediated cytoskeletal reorganisation.

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15

Exton, J. H. "Regulation of phospholipase D." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1439, no. 2 (July 1999): 121–33. http://dx.doi.org/10.1016/s1388-1981(99)00089-x.

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16

Exton, John H. "Regulation of phospholipase D." FEBS Letters 531, no. 1 (September 17, 2002): 58–61. http://dx.doi.org/10.1016/s0014-5793(02)03405-1.

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17

González-Mendoza, Víctor M., M. E. Sánchez-Sandoval, Lizbeth A. Castro-Concha, and S. M. Teresa Hernández-Sotomayor. "Phospholipases C and D and Their Role in Biotic and Abiotic Stresses." Plants 10, no. 5 (May 4, 2021): 921. http://dx.doi.org/10.3390/plants10050921.

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Plants, as sessile organisms, have adapted a fine sensing system to monitor environmental changes, therefore allowing the regulation of their responses. As the interaction between plants and environmental changes begins at the surface, these changes are detected by components in the plasma membrane, where a molecule receptor generates a lipid signaling cascade via enzymes, such as phospholipases (PLs). Phospholipids are the key structural components of plasma membranes and signaling cascades. They exist in a wide range of species and in different proportions, with conversion processes that involve hydrophilic enzymes, such as phospholipase-C (PLC), phospholipase-D (PLD), and phospholipase-A (PLA). Hence, it is suggested that PLC and PLD are highly conserved, compared to their homologous genes, and have formed clusters during their adaptive history. Additionally, they generate responses to different functions in accordance with their protein structure, which should be reflected in specific signal transduction responses to environmental stress conditions, including innate immune responses. This review summarizes the phospholipid systems associated with signaling pathways and the innate immune response.

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18

Houle, Martin G., and Sylvain Bourgoin. "Small GTPase-regulated phospholipase D in granulocytes." Biochemistry and Cell Biology 74, no. 4 (July 1, 1996): 459–67. http://dx.doi.org/10.1139/o96-050.

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This review examines the functional role of phospholipase D in the neutrophil. Phospholipase D is emerging as an important component in the signal transduction pathways leading to granulocyte activation. Through the second messenger it produces, phosphatidic acid, phospholipase D plays an active role in the regulation of granulocyte NADPH oxidase activation and granular secretion. Many factors from both the cytosol and the membrane are necessary for maximal phospholipase D activation. This paper will focus on the regulation of phospholipase D by low molecular weight GTP-binding proteins, tyrosine kinases, and protein kinase C.Key words: phospholipase D, low molecular weight GTP-binding proteins, tyrosine kinases, protein kinase C, granulocytes.

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19

Chabot, M. C., L. C. McPhail, R. L. Wykle, D. A. Kennerly, and C. E. McCall. "Comparison of diglyceride production from choline-containing phosphoglycerides in human neutrophils stimulated with N-formylmethionyl-leucylphenylalanine, ionophore A23187 or phorbol 12-myristate 13-acetate." Biochemical Journal 286, no. 3 (September 15, 1992): 693–99. http://dx.doi.org/10.1042/bj2860693.

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The turnover of choline-containing phosphoglycerides (PC) in response to agonist stimulation is well documented in human neutrophils. We have now compared the enzymic pathways of N-formylmethionyl-leucylphenylalanine (fMLP)-, A23187- and phorbol-12-myristate 13-acetate (PMA)-induced diglyceride (DG) and phosphatidic acid (PA) generation in these cells. In order to distinguish between phospholipase C- and D-mediated PC breakdown, human neutrophils were radiolabelled with 1-O-[3H]alkyl-2-acyl-glycero-3-phosphocholine and stimulated in the presence of ethanol or propranolol. The addition of 0.5% ethanol to the incubation mixture resulted in the production of phosphatidylethanol, indicative of phospholipase D activation, in response to all three stimuli. Concomitant with phosphatidylethanol formation was a partial block of PA production. The production of DG was also partially blocked by addition of ethanol. Propranolol (200 microM) was also used to assess the contributions of phospholipases C and D toward DG generation. Inhibition of PA phosphohydrolase by propranolol resulted in the complete abolition of DG generation when neutrophils were stimulated with fMLP. In contrast, propranolol only partially inhibited DG generation in response to A23187 and PMA. These results suggested that DG production in response to fMLP stimulation is mediated via the activation of phospholipase D, whereas A23187- or PMA-induced DG generation may involve more than one pathway. However, examination of the water-soluble choline metabolites produced indicated that phospholipase D was responsible for the production of PA and DG in response to all three stimuli.

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20

Gilbert, Jonathan J., Trevor R. Pettitt, Sandra D. Seatter, Steven D. Reid, Michael J. O. Wakelam, and Margaret M. Harnett. "Antagonistic Roles for Phospholipase D Activities in B Cell Signaling: While the Antigen Receptors Transduce Mitogenic Signals Via a Novel Phospholipase D Activity, Phosphatidylcholine-Phospholipase D Mediates Antiproliferative Signals." Journal of Immunology 161, no. 12 (December 15, 1998): 6575–84. http://dx.doi.org/10.4049/jimmunol.161.12.6575.

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Abstract Cross-linking of the Ag receptors on B cells induces DNA synthesis and proliferation. Butanol trap experiments suggest that one or more phospholipase D activities play a key role in this process. Although phosphatidylcholine-phospholipase D has been shown to play a central role in the transduction of proliferative responses for a wide variety of calcium-mobilizing receptors, we show that the Ag receptors are not coupled to this phospholipase. In addition, phosphatidylcholine-phospholipase D is not stimulated under conditions that mimic T cell-dependent B cell activation. In contrast, ATP, which inhibits surface Ig (sIg)-mediated DNA synthesis in murine B cells via P2-purinoceptors, activates phosphatidylcholine-phospholipase D. Phosphatidylcholine-phospholipase D is therefore associated with antiproliferative signal transduction in mature B cells, but it does not transduce early signals associated with sIg-mediated growth arrest or apoptosis in immature B cells. Mitogenic stimulation of sIg is, however, coupled to a novel nonphosphatidylcholine-hydrolyzing phospholipase D activity. The resultant sIg-generated phosphatidic acid, unlike the phosphatidylcholine-derived phosphatidic acid generated via the purinoceptors, is converted to diacylglycerol. These data provide the first evidence that while the novel sIg-coupled phospholipase D and resultant diacylglycerol generation may play a role in B cell survival and proliferation, phosphatidylcholine-phospholipase D may transduce, via phosphatidic acid, negative immunomodulatory signals in mature B lymphocytes.

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21

Heo, Yunseok, Inhwan Lee, Sunjin Moon, Ji-Hye Yun, Eun Yu Kim, Sam-Yong Park, Jae-Hyun Park, Woo Taek Kim, and Weontae Lee. "Crystal Structures of the Plant Phospholipase A1 Proteins Reveal a Unique Dimerization Domain." Molecules 27, no. 7 (April 2, 2022): 2317. http://dx.doi.org/10.3390/molecules27072317.

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Phospholipase is an enzyme that hydrolyzes various phospholipid substrates at specific ester bonds and plays important roles such as membrane remodeling, as digestive enzymes, and the regulation of cellular mechanism. Phospholipase proteins are divided into following the four major groups according to the ester bonds they cleave off: phospholipase A1 (PLA1), phospholipase A2 (PLA2), phospholipase C (PLC), and phospholipase D (PLD). Among the four phospholipase groups, PLA1 has been less studied than the other phospholipases. Here, we report the first molecular structures of plant PLA1s: AtDSEL and CaPLA1 derived from Arabidopsis thaliana and Capsicum annuum, respectively. AtDSEL and CaPLA1 are novel PLA1s in that they form homodimers since PLAs are generally in the form of a monomer. The dimerization domain at the C-terminal of the AtDSEL and CaPLA1 makes hydrophobic interactions between each monomer, respectively. The C-terminal domain is also present in PLA1s of other plants, but not in PLAs of mammals and fungi. An activity assay of AtDSEL toward various lipid substrates demonstrates that AtDSEL is specialized for the cleavage of sn-1 acyl chains. This report reveals a new domain that exists only in plant PLA1s and suggests that the domain is essential for homodimerization.

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22

Boarder, M. R. "Phospholipase D in Chromaffin Cells?" Journal of Neurochemistry 60, no. 5 (May 1993): 1978–79. http://dx.doi.org/10.1111/j.1471-4159.1993.tb13435.x.

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23

Exton, John H. "New Developments in Phospholipase D." Journal of Biological Chemistry 272, no. 25 (June 20, 1997): 15579–82. http://dx.doi.org/10.1074/jbc.272.25.15579.

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24

Jones, David, Clive Morgan, and Shamshad Cockcroft. "Phospholipase D and membrane traffic." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1439, no. 2 (July 1999): 229–44. http://dx.doi.org/10.1016/s1388-1981(99)00097-9.

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25

Venable, Mark E., and Lina M. Obeid. "Phospholipase D in cellular senescence." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1439, no. 2 (July 1999): 291–98. http://dx.doi.org/10.1016/s1388-1981(99)00101-8.

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26

Frohman, Michael A., and Andrew J. Morris. "Phospholipase D structure and regulation." Chemistry and Physics of Lipids 98, no. 1-2 (April 1999): 127–40. http://dx.doi.org/10.1016/s0009-3084(99)00025-0.

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27

Wang, Xuemin. "Molecular analysis of phospholipase D." Trends in Plant Science 2, no. 7 (July 1997): 261–66. http://dx.doi.org/10.1016/s1360-1385(97)86348-0.

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28

Lan, Wanwen, and Louis Tong. "Focus on Molecules: Phospholipase D." Experimental Eye Research 103 (October 2012): 121–22. http://dx.doi.org/10.1016/j.exer.2011.11.009.

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29

Simpson, T. D. "Phospholipase D activity in hexane." Journal of the American Oil Chemists’ Society 68, no. 3 (March 1991): 176–78. http://dx.doi.org/10.1007/bf02657764.

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Seaman, Matthew N. J. "Phospholipase D in vesicle budding." Trends in Cell Biology 6, no. 12 (December 1996): 473. http://dx.doi.org/10.1016/0962-8924(96)84944-0.

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31

Cockcroft, Shamshad, and Michael Frohman. "Special Issue on Phospholipase D." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1791, no. 9 (September 2009): 837–38. http://dx.doi.org/10.1016/j.bbalip.2009.08.003.

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32

Dai, Jian, Song-Yan Liu, and Vincenzo Panagia. "Kinetics of myocardial phospholipase D." Molecular and Cellular Biochemistry 160-161, no. 1 (1996): 83–87. http://dx.doi.org/10.1007/bf00240035.

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33

TRIFAN, OVIDIU C., LAURENTIU M. POPESCU, ARPAD TOSAKI, GERALD CORDIS, and DIPAK K. DAS. "Ischemic Preconditioning Involves Phospholipase D." Annals of the New York Academy of Sciences 793, no. 1 Myocardial Pr (September 1996): 485–88. http://dx.doi.org/10.1111/j.1749-6632.1996.tb33546.x.

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34

Morris, Andrew J., Michael A. Frohman, and JoAnne Engebrecht. "Measurement of Phospholipase D Activity." Analytical Biochemistry 252, no. 1 (October 1997): 1–9. http://dx.doi.org/10.1006/abio.1997.2299.

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35

Motasim Billah, M. "Phospholipase D and cell signaling." Current Opinion in Immunology 5, no. 1 (February 1993): 114–23. http://dx.doi.org/10.1016/0952-7915(93)90090-f.

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36

Hoener, Marius C., Reinhard Bolli, and Urs Brodbeck. "Glycosyl-phosphatidylinositol-specific phospholipase D." FEBS Letters 327, no. 2 (July 26, 1993): 203–6. http://dx.doi.org/10.1016/0014-5793(93)80170-y.

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37

Kam, Yoonseok, and John H. Exton. "Dimerization of Phospholipase D Isozymes." Biochemical and Biophysical Research Communications 290, no. 1 (January 2002): 375–80. http://dx.doi.org/10.1006/bbrc.2001.6146.

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38

Cuevas, W. A., and J. G. Songer. "Arcanobacterium haemolyticum phospholipase D is genetically and functionally similar to Corynebacterium pseudotuberculosis phospholipase D." Infection and Immunity 61, no. 10 (1993): 4310–16. http://dx.doi.org/10.1128/iai.61.10.4310-4316.1993.

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39

Kramer, R. M., G. C. Checani, and D. Deykin. "Stimulation of Ca2+-activated human platelet phospholipase A2 by diacylglycerol." Biochemical Journal 248, no. 3 (December 15, 1987): 779–83. http://dx.doi.org/10.1042/bj2480779.

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We examined the effect of diacylglycerol on Ca2+-dependent phospholipase A2 from human platelets. Phospholipase A2 was solubilized and partially purified to a stable form in the presence of n-octyl beta-D-glucopyranoside (octyl glucoside), and its enzymic activity was determined with sonicated 2.5 microM-1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine (arachidonoyl-PC) as substrate. Phospholipase A2 activity was increased when diacylglycerol was incorporated into the substrate arachidonoyl-PC. Stimulation was maximal in the presence of greater than or equal to 29 mol% (1 microM) diacylglycerol, and was greater than 4-fold for both 1,2-dioleoylglycerol and 1-stearoyl-2-arachidonoylglycerol. 1-Stearoyl-2-arachidonoylglycerol at concentrations of 2-5 mol% increased phospholipase A2 activity 1.3-1.8-fold. Exogenously added 1-oleoyl-2-acetylglycerol also enhanced phospholipase A2 activity, producing a maximal stimulation of 1.6-fold at a concentration of 25 microM. Comparative studies conducted with pancreatic, bee-venom and snake-venom phospholipase A2 showed that the activity of these extracellular phospholipases towards the arachidonoyl-PC substrate was also increased by diacylglycerol, but stimulation was less than observed for platelet phospholipase A2. Our results suggest that diacylglycerol, known to be generated in stimulated platelets, may enhance Ca2+-activated phospholipase A2.

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Li, Xianping, Meihua Gao, Xuelin Han, Sha Tao, Dongyu Zheng, Ying Cheng, Rentao Yu, Gaige Han, Martina Schmidt, and Li Han. "Disruption of the Phospholipase D Gene Attenuates the Virulence of Aspergillus fumigatus." Infection and Immunity 80, no. 1 (November 14, 2011): 429–40. http://dx.doi.org/10.1128/iai.05830-11.

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ABSTRACTAspergillus fumigatusis the most prevalent airborne fungal pathogen that induces serious infections in immunocompromised patients. Phospholipases are key enzymes in pathogenic fungi that cleave host phospholipids, resulting in membrane destabilization and host cell penetration. However, knowledge of the impact of phospholipases onA. fumigatusvirulence is rather limited. In this study, disruption of thepldgene encoding phospholipase D (PLD), an important member of the phospholipase protein family inA. fumigatus, was confirmed to significantly decrease both intracellular and extracellular PLD activity ofA. fumigatus. Thepldgene disruption did not alter conidial morphological characteristics, germination, growth, and biofilm formation but significantly suppressed the internalization ofA. fumigatusinto A549 epithelial cells without affecting conidial adhesion to epithelial cells. Importantly, the suppressed internalization was fully rescued in the presence of 100 μM phosphatidic acid, the PLD product. Indeed, complementation ofpldrestored the PLD activity and internalization capacity ofA. fumigatus. Phagocytosis ofA. fumigatusconidia by J774 macrophages was not affected by the absence of thepldgene. Pretreatment of conidia with 1-butanol and a specific PLD inhibitor decreased the internalization ofA. fumigatusinto A549 epithelial cells but had no effect on phagocytosis by J774 macrophages. Finally, loss of thepldgene attenuated the virulence ofA. fumigatusin mice immunosuppressed with hydrocortisone acetate but not with cyclophosphamide. These data suggest that PLD ofA. fumigatusregulates its internalization into lung epithelial cells and may represent an important virulence factor forA. fumigatusinfection.

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Hui, Li, Vanessa Rodrik, Rafal M. Pielak, Stefan Knirr, Yang Zheng, and David A. Foster. "mTOR-dependent Suppression of Protein Phosphatase 2A Is Critical for Phospholipase D Survival Signals in Human Breast Cancer Cells." Journal of Biological Chemistry 280, no. 43 (August 18, 2005): 35829–35. http://dx.doi.org/10.1074/jbc.m504192200.

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A critical aspect of tumor progression is the generation of survival signals that overcome default apoptotic programs. Recent studies have revealed that elevated phospholipase D activity generates survival signals in breast and perhaps other human cancers. We report here that the elevated phospholipase D activity in the human breast cancer cell line MDA-MB-231 suppresses the activity of the putative tumor suppressor protein phosphatase 2A in a mammalian target of rapamycin (mTOR)-dependent manner. Increasing the phospholipase D activity in MCF7 cells also suppressed protein phosphatase 2A activity. Elevated phospholipase D activity suppressed association of protein phosphatase 2A with both ribosomal subunit S6-kinase and eukaryotic initiation factor 4E-binding protein 1. Suppression of protein phosphatase 2A by SV40 small t-antigen has been reported to be critical for the transformation of human cells with SV40 early region genes. Consistent with a critical role for protein phosphatase 2A in phospholipase D survival signals, either SV40 small t-antigen or pharmacological suppression of protein phosphatase 2A restored survival signals lost by the suppression of either phospholipase D or mTOR. Blocking phospholipase D signals also led to reduced phosphorylation of the pro-apoptotic protein BAD at the protein phosphatase 2A dephosphorylation site at Ser-112. The ability of phospholipase D to suppress protein phosphatase 2A identifies a critical target of an emerging phospholipase D/mTOR survival pathway in the transformation of human cells.

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Singer, William D., H. Alex Brown, and, and Paul C. Sternweis. "REGULATION OF EUKARYOTIC PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C AND PHOSPHOLIPASE D." Annual Review of Biochemistry 66, no. 1 (June 1997): 475–509. http://dx.doi.org/10.1146/annurev.biochem.66.1.475.

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OHGUCHI, Kenji. "Regulation of Melanogenesis and Phospholipase D." Oleoscience 8, no. 7 (2008): 293–98. http://dx.doi.org/10.5650/oleoscience.8.293.

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Exton, J. H. "Phospholipase D: enzymology, mechanisms of regulation, and function." Physiological Reviews 77, no. 2 (April 1, 1997): 303–20. http://dx.doi.org/10.1152/physrev.1997.77.2.303.

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Phospholipase D exists in various forms that differ in their regulation but predominantly hydrolyze phosphatidylcholine. The Ca(2+)-dependent isozymes of protein kinase C regulate phospholipase D in vitro and play a major role in its control by growth factors and G protein-linked agonists in vivo. Recent studies have demonstrated that small G proteins of the ADP-ribosylation factor (ARF) and Rho families activate the enzyme in vitro, and evidence is accumulating that they also are involved in its control in vivo. Both types of G protein play important roles in cellular function, and the possible mechanisms by which they are activated by agonists are discussed. There is also emerging evidence of the control of phospholipase D and Rho proteins by soluble tyrosine kinases and novel serine/threonine kinases. The possible role of these kinases in agonist regulation of phospholipase D is discussed. The function of phospholipase D in cells is still poorly defined. Postulated roles of phosphatidic acid produced by phospholipase D action include the activation of Ca(2+)-independent isoforms of protein kinase C, the regulation of growth and the cytoskeleton in fibroblasts, and control of the respiratory burst in neutrophils. Another important function of phosphatidic acid is to act as a substrate for a specific phospholipase A2 to generate lysophosphatidic acid, which is becoming increasingly recognized as a major intercellular messenger. Finally, it is possible that the phospholipid changes induced in various cellular membranes by phospholipase D may per se play an important role in vesicle trafficking and other membrane-associated events.

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Ghosh, S. S., and Richard C. Franson. "Use of [1-14C]oleate labelled autoclaved Escherichia coli as a membranous substrate for measurement of in vitro phospholipase D activity." Biochemistry and Cell Biology 70, no. 1 (January 1, 1992): 43–48. http://dx.doi.org/10.1139/o92-006.

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Autoclaved Escherichia coli labelled with [1-14C]oleate in the 2-acyl position have been used extensively to measure phospholipase A2 activity in vitro. The present study demonstrates that this membranous substrate is also useful for the measurement of in vitro phospholipase D activity. Phospholipase D from Streptomyces chromofuscus catalyzed the hydrolysis of [1-14C]oleate labelled, autoclaved E. coli optimally at pH 7.0–8.0 to generate [14C]phosphatidic acid in the presence of 5 mM added Ca2+. Other divalent cations would not substitute for Ca2+. Activity was linear with time and protein up to 30% of the hydrolysis of substrate. Phospholipase D activity was stimulated in a dose-dependent manner by the addition of Triton X-100. The activity was increased 5.5-fold with 0.05% Triton, a concentration that totally inhibited hydrolysis of E. coli by human synovial fluid phospholipase A2. Accumulation of [14C]diglyceride was observed after 10 min of incubation. This accumulation was inhibited by NaF (IC50 = 18 μM) or propanolol (IC50 = 180 μM) suggesting the S. chromofuscus phospholipase D was contaminated with phosphatidate phosphohydrolase. Phosphatidic acid released by the action of cabbage phospholipase D was converted to phosphatidylethanol in an ethanol concentration dependent manner. These results demonstrate that [1-14C]oleate labelled, autoclaved E. coli can be used to measure phospholipase D activity by monitoring accumulation of either [14C]phosphatidic acid or [14C]phosphatidylethanol.Key words: Escherichia coli, substrate, phospholipase D, Streptomyces chromofuscus, sodium fluoride, propranolol.

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SAKMANOĞLU, Aslı, and Osman ERGANİŞ. "Comparison of the efficiency of concentrated soluble recombinant phospholipase D and natural phospholipase D enzymes." TURKISH JOURNAL OF VETERINARY AND ANIMAL SCIENCES 40 (2016): 675–80. http://dx.doi.org/10.3906/vet-1602-61.

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Iwasaki, Y., H. Nakano, and T. Yamane. "Phospholipase D fromStreptomyces antibioticus: Cloning, sequencing, expression, and relationship to other phospholipases." Applied Microbiology and Biotechnology 42, no. 2-3 (November 1994): 290–99. http://dx.doi.org/10.1007/bf00902731.

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Kang, Han-Chul, Sang-Hong Yoon, Chang-Muk Lee, and Bon-Sung Koo. "Expression and Biochemical Characteristics of a Phospholipase D from Bacillus licheniformis." Journal of Applied Biological Chemistry 54, no. 2 (June 30, 2011): 94–100. http://dx.doi.org/10.3839/jabc.2011.017.

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Horwitz, J., and L. L. Davis. "The substrate specificity of brain microsomal phospholipase D." Biochemical Journal 295, no. 3 (November 1, 1993): 793–98. http://dx.doi.org/10.1042/bj2950793.

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Neurotransmitters activate a phospholipase D that is though to specifically hydrolyse phosphatidylcholine. This enzyme has a unique property known as transphosphatidylation: in the presence of an appropriate nucleophilic receptor such as an alcohol, phospholipase D will catalyse the production of phosphatidyl-alcohol. We have studied phospholipase D using an in vitro assay that uses [3H]butanol of high specific radioactivity (15 Ci/mmol) as an acceptor. In the presence of [3H]butanol and phosphatidylcholine, a microsomal membrane fraction from rat brain catalysed the production of phosphatidyl[3H]butanol. Phospholipase D activity was dependent upon the presence of a detergent; the optimal sodium oleate concentration was between 4 and 6 mM. The RF of the phosphatidyl[3H]butanol on t.l.c. was identical to the RF of the phosphatidylbutanol formed when [3H]phosphatidylcholine was incubated with 100 mM butanol. These data confirm the identity of phosphatidyl[3H]butanol. One important advantage of this assay is that the substrate does not need to be labelled. We have used this advantage to examine the substrate specificity of phospholipase D. Microsomal phospholipase D appears to hydrolyse phosphatidylcholine most efficiently. There is a relatively small but significant activity against phosphatidylethanolamine and phosphatidylserine, and there is no significant activity against phosphatidylinositol. As the head-group becomes more like choline, the phospholipid becomes a better substrate for phospholipase D. The addition of one methyl group leads to a large increase in activity. Fatty acid composition does not play a role in determining the substrate specificity. This assay should be useful in furthering our understanding of this important enzyme.

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Badiani, K., and G. Arthur. "Evidence for receptor and G-protein regulation of a phosphatidylethanolamine-hydrolysing phospholipase A1 in guinea-pig heart microsomes: stimulation of phospholipase A1 activity by DL-isoprenaline and guanine nucleotides." Biochemical Journal 312, no. 3 (December 15, 1995): 805–9. http://dx.doi.org/10.1042/bj3120805.

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While evidence has been presented for the receptor-mediated activation of phospholipases A2, C and D, the activation of phospholipase A1 subsequent to receptor activation has not been established. Phospholipase A1-catalysed hydrolysis of 1-palmitoyl-2-linoleoyl-glycerophosphoethanolamine (GPE) by guinea-pig heart microsomes was stimulated 40-60% by isoprenaline. This isoprenaline-mediated increase in activity was blocked by propranolol and butoxamine, a specific beta 2-adrenergic antagonist, but not by atenolol, a specific beta 1-adrenergic antagonist. Neither clonidine nor phenylephrine, alpha 1- and alpha 2-adrenergic agonists respectively, had a stimulatory effect on the hydrolysis of the PE substrate. Guanosine 5′(-)[gamma-thio]triphosphate (GTP[S]) and guanosine 5′(-)[beta, gamma-imido]triphosphate, but not guanosine 5′(-)[beta-thio]diphosphate (GDP[S]) or adenosine 5′(-)[gamma-thio]triphosphate, stimulated the hydrolysis of 1-palmitoyl-2-linoleoyl-GPE by phospholipase A1. GDP[S] inhibited the isoprenaline-mediated stimulation of phospholipase A1 activity. Phospholipase A1 hydrolysis of 1-palmitoyl-2-linoleoyl-GPE was not dependent on cations; however, the stimulatory effects of isoprenaline and GTP[S] on the hydrolytic activity were abolished by cation chelators. The above data suggest that phospholipase A1 activity in guinea-pig heart microsomes is activated by the binding of isoprenaline to beta 2-adrenergic receptors. Furthermore the stimulation of phospholipase A1 activity by the agonist may be mediated via activation of G-proteins.

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