한국어병학회지 (Journal of fish pathology)

  • 제21권1호
  • /
  • Pages.1-11
  • /
  • 2008
  • /
  • 1226-0819(pISSN)
  • /
  • 2233-5412(eISSN)
한국어병학회 (The Korean Society of Fish Pathology)
권호 표지

Characterization of Phosphatidylcholine-Hydrolyzing Phospholipase D in the Scuticociliate Parasite, Uronema marinum

  • Seo, Jung-Soo (Patholgy Division, National Fisheries Research and Development Institute) ;
  • Kim, Moo-Sang (Department of Aquatic Life Medicine, Pukyong National University) ;
  • Kim, Na-Young (Department of Aquatic Life Medicine, Pukyong National University) ;
  • Ahn, Sang-Jung (Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • Jee, Bo-Young (Patholgy Division, National Fisheries Research and Development Institute) ;
  • Jung, Sung-Hee (Patholgy Division, National Fisheries Research and Development Institute) ;
  • Kim, Jin-Woo (Patholgy Division, National Fisheries Research and Development Institute) ;
  • Kim, Ki-Hong (Department of Aquatic Life Medicine, Pukyong National University) ;
  • Lee, Hyung-Ho (Faculty of Food Science and Biotechnology, Pukyong National University) ;
  • Chung, Joon-Ki (Department of Aquatic Life Medicine, Pukyong National University)
  • 발행 : 20080400
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

We report the existence of new type of phosphatidylcholine-hydrolyzing phospholipase D (PLD), which has been characterized and partially purified in the scuticociliate, Uronema marinum. The enzyme from partial purification showed that it was existed in membrane fraction and was a neutral PLD, which catalyzed both transphosphatidylation and hydrolysis reaction. The activity of partially purified membrane-bound PLD was also found to be optimal at pH 7.0-7.5 for 2 hours at 37℃ and depended strictly on the presence of Ca2+ (2.5 mM) and Mg2+ (1.6 mM). Immunoblot analysis indicated that the enzyme was distinct from hPLD1 (human PLD1) and hPLD2 (human PLD2) because it was not recognized by a polyclonal antibody raised to the 12 terminal amino acid of these enzymes. We also found that the membrane-bound PLD is a PIP2-dependent PLD and that GTP-binding proteins are not implicated in the regulation of this enzyme: This enzyme activity is markedly stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) but not by the small G-protein Arf and GTPrS. In addition, this enzyme was capable of hydrolyzing phosphatidylcholine (PC) but not phosphatidylethanolamine (PE), implying that PC was a preferred substrate.

키워드

참고문헌

  1. Amsterdam, A., Dantes, A. and Liscovitch, M.: Role of phospholipase-D and phosphatidic acid in mediating gonadotropin-releasing hormone-induced inhibition of preantral granulose cell differentiation. Endocrinol., 135: 1205-1211, 1994 https://doi.org/10.1210/en.135.3.1205
  2. Banno, Y., Tamiya-Koizumi, K., Oshima, H., Morikawa, A., Yoshida, S. and Nozawa, Y.: Nuclear ADP-ribosylation factor (ARF) and oleate-dependent phospholipase D (PLD) in rat liver cells: increase of ARF-dependent PLD activity in regenerating liver cells. J. Biol. Chem., 272: 5208-5213, 1997 https://doi.org/10.1074/jbc.272.8.5208
  3. Billah, M. M.: Phospholipase D and cell signaling. Curr. Opin. Immunol., 5: 114-123, 1993 https://doi.org/10.1016/0952-7915(93)90090-F
  4. Blum, J. J., Lehman, J. A., Horn, J. M. and Cambronero, J. G..: Phospholiase D is present in Leishmania donovani and its activity increases in response to acute osmotic stress. J. Eukaryot. Microbiol., 48: 102-110, 2001 https://doi.org/10.1111/j.1550-7408.2001.tb00421.x
  5. Brown, H. A., Gutowski, S., Moomaw, C. R., Slaughter, C. and Sternweis, P. C.: ADPribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase activity. Cell, 75: 1137-1144, 1993 https://doi.org/10.1016/0092-8674(93)90323-I
  6. Cheung, P. J., Nigrelli, R. F. and Ruggieri, G. D.: Studies on the morphology of Uronema marinum Dujardin (Ciliatea: Uronematidae) with a description of the histopatology of the infection in marine fishes. J. Fish. Dis., 3: 295-303, 1980 https://doi.org/10.1111/j.1365-2761.1980.tb00400.x
  7. Chung, J. K., Sekiya, F., Kang, H. S., Lee, C. H., Han, J. S., Kim, S. R., Bae, Y. S., Morris, A. J. and Rhee, S. G..: Synaptojanin inhibition of phsopholipase D activity by hydrolysis of phsophatdidylinositol 4,5-bisphosphate. J. Biol. Chem., 272: 15980-15985. 1997 https://doi.org/10.1074/jbc.272.25.15980
  8. Cockcroft, S. 2001. Signalling roles of mammalian phospholipase D1 and D2. Cell. Mol. Life Sci., 58: 1674-1687, 1997 https://doi.org/10.1007/PL00000805
  9. Connelly, M. C. and Kierszenbaum, F.: Modulation of macrophage interaction with Trypanosoma cruzi by phospholipase A2-sensitive components of the parasite membrane. Biochem. Biophys. Res. Commun., 121: 931-939, 1984 https://doi.org/10.1016/0006-291X(84)90766-6
  10. Connelly, M. C. and Kierszenbaum, F.: Increased host cell-Trypanosoma cruzi interaction following phospholipase D treatment of the parasite surface. Mol. Biochem. Parasitol., 17: 191-202, 1985 https://doi.org/10.1016/0166-6851(85)90018-0
  11. English, D.: Phosphatidic acid: a lipid messenger involved in intracellular and extracellular signaling. Cell. Signalling., 8: 341-347, 1996 https://doi.org/10.1016/0898-6568(95)00076-3
  12. Exton, J. H.: Phospholipase D: enzymology, mechanisms of regulation, and function. Physiol. Rev., 77: 303-320, 1997 https://doi.org/10.1152/physrev.1997.77.2.303
  13. Exton, J. H.: Phospholipase D: Structure, Regulation and Function. 2002. Rev. Physiol. Biochem. Pharmacol., 144: 1-94, 2002 https://doi.org/10.1007/BFb0116585
  14. Hanahan, D. J. and Chaikoff, I. L.: A new phospholipid- splitting enzyme specific for the ester linkage between the nitrogenous base and the phosphoric acid grouping. J. Biol. Chem., 169: 699-705, 1947
  15. Iglesias, R., Parama, A., Alvarez, M. F., Leiro, J., Fernandez, J. and Sanmartin, M. L.: Philasterides dicentrarchi (Ciliophora, Scuticociliatida) as the causative agent of scuticociliatosis in farmed turbot Scophthalmus maximus in Galicia (NW Spain). Dis. Aquat. Org., 46: 47-55, 2001 https://doi.org/10.3354/dao046047
  16. Jee, B.Y., Kim, Y.C. and Park, M.S.: Morphology and biology of parasite responsible for scu-ticociliatosis of cultured olive flounder Paralichthys olivaceus. Diseases of Aquatic Organisms 47, 49-55, 2001 https://doi.org/10.3354/dao047049
  17. Kanfer, J. N. and McCartney, D.: Phospholipase D activity of isolated rat brain plasma membranes. FEBS Lett. 337: 251-254, 1994 https://doi.org/10.1016/0014-5793(94)80202-5
  18. Kim, S.M., Cho, J.B., Lee, E.H., Kwon, S.R., Kim, S.K., Nam, Y.K. and Kim, K.H.: Pseudocohnilembus persalinus (Ciliophora: Scuticociitida) is an additional causing species of scuticociliatosis in olive flounder Paralichthys olivaceus. Diseases of Aquatic Organisms 62, 239-244, 2004 https://doi.org/10.3354/dao062239
  19. Koonin, E. V.: A duplicated catalytic motif in a new superfamily of phosphohydrolases and phospholipid synthases that includes poxvirus envelope proteins. Trends Biochem. Sci., 21: 242-243, 1996 https://doi.org/10.1016/S0968-0004(96)30024-8
  20. Kovacs, P., Csaba, G., Ito, Y. and Nozawa, Y.: Effect of insulin on the phsopholipase-D activity and insulin-pretreated (Hormonally imprinted) Tetrahymena. Biochem. Biophys. Res. Commun., 222: 359-361, 1996 https://doi.org/10.1006/bbrc.1996.0748
  21. Kovacs, P., Csaba, G., Nakashima, S. and Nozawa, Y.: Phospholipase D activity in the Tetrahymena pyriformis GL. Cell. Biochem. Funct., 15: 53-60, 1997 https://doi.org/10.1002/(SICI)1099-0844(199703)15:1<53::AID-CBF720>3.0.CO;2-F
  22. Kwon, S. R., Kim, C. S., Chung, J. K., Lee, H. H. and Kim, K. H.: Inhibition of chemiluminscent response of olive flounder Paralichthys olivaceus phagocytes by the scuticociliate parasite Uronema marinum. Dis. Aquat. Org., 52: 119-122, 2002 https://doi.org/10.3354/dao052119
  23. Liscovich, M., Czarny, M., Fiucci, G. and Tang, X.: Phospholipase D: molecular and cell biology of a novel gene family. Biochem. J., 345: 401-415, 2000 https://doi.org/10.1042/0264-6021:3450401
  24. Lopez, I., Burns, D. J. and Lambeth, J. D.: Regulation of phospholipase D by protein kinase C in human neutrophils. Conventional isoforms of protein kinase C phosphorylate a phospholipase D-related component in the plasma membrane. J. Biol. Chem., 270: 19465-19472, 1995 https://doi.org/10.1074/jbc.270.33.19465
  25. Martin, T. W. and Michaelis, K.: P2-purinergic agonists stimulate phosphodiesteratic cleavage of phosphatidylcholine in endothelial cells. Evidence for activation of phospholipase D. J. Biol. Chem., 264: 8847-8856, 1989
  26. Massenburg, D., Han, J. S., Liyanage, M., Patton, W. A. and Rhee, S. G..: Activation of rat brain phopholipase D by ADP-ribosylation factors 1, 5, and 6; Separation of ADP-ribosylation factor\-dependent and oleate-dependent enzymes. Proc. Natl. Acad. Sci., 91: 11718-11722, 1994
  27. Morris, A. J., Engebrecht, J. and Frohman, M. A.: Structure and regulation of phospholipase D. Trends Pharmacol. Sci., 17: 182-185, 1996 https://doi.org/10.1016/0165-6147(96)10016-X
  28. Munnik, T.: Phosphatidic acid: an emerging plant lipid second messenger. Trends Plant Sci., 6: 227-233, 2001 https://doi.org/10.1016/S1360-1385(01)01918-5
  29. Natarajan, V., Scribner, W. M. and Vepa, S.: Regulation of phospholipase D by tyrosine kinases. Chem. Physics. Lipids., 80: 103-116, 1996 https://doi.org/10.1016/0009-3084(96)02548-0
  30. Ponting C. P. and Kerr, I. D.: A novel family of phospholipase D homologues that includes phopholipid synthases and putative endonuclase; identification of duplicated repeats and potential activate-site residues. Protein Sci., 5: 914-922, 1996 https://doi.org/10.1002/pro.5560050513
  31. Rasmussen, M. and Rasmussen, L.: Phospholipase D in Tetrahymena: activity and significance. Comp. Biochem. Physiol., 124B: 467-473, 1999
  32. Seo, J.S., Kim, M.S., Lee, S.H., Kim, K.H., Lee, H.H., Jeong, H.D. and Chung, J.K.: Urone-ma marinum: Identification and characterization of phosphatidylcholine-hydrolyzing phospholipase C. Exp. Parasitol., 110: 22-29, 2005 https://doi.org/10.1016/j.exppara.2005.01.005
  33. Siddiqui, R. A. and Exton, J. H.: Phospholipid base exchange activity in rat liver plasma membranes. Evidence for regulation by G-protein and P2y-purinergic receptor. J. Biol. Chem., 267: 5755-5761, 1992
  34. Sterud, E., Hansen, M. K. and Mo, T. A.: Systemic infecion with Uronema-like ciliates in farmed turbot, Scophtalmus maximus (L.). J. Fish. Dis., 23: 33-37, 2000 https://doi.org/10.1046/j.1365-2761.2000.00204.x
  35. Stieglitz, K. A., Seaton, B. A. and Roberts M. F.: Binding of proteolytically processed phospholipase D from Streptomyces chromofuscus to phosphatidylcholine membranes facilitates vesicle aggregation and fusion. Biochem., 40: 13954-13963, 2001 https://doi.org/10.1021/bi011338o
  36. Thompson, C. L. and Moewus, L.: Miamiensis avidus n.g.n.s., a marine facultative parasite in the ciliate order Hymenostomatida. J. Protozool., 11: 378-381, 1964 https://doi.org/10.1111/j.1550-7408.1964.tb01766.x
  37. Van Blitterswijk, W. J. and Hilkmann, H.: Rapid attenuation of receptor-induced diacylglycerol and phosphatidic acid by phospholipase D-mediated transphosphatidylation: formation of bisphosphatidic acid. EMBO J., 12: 2655-2662, 1993
  38. Waggoner, D. W., Xu, J., Singh, I., Jasinska, R., Zhang, Q. X. and Brindly, D. N.:. Structural organization of mammalian lipid phosphatase: Implication for signal transduction. Bochim. Biophys. Acta., 1439: 299-316, 1999 https://doi.org/10.1016/S1388-1981(99)00102-X
  39. Wang S., Banno, Y., Nakashima, S. and Nozawa, Y.: Enzymatic characterization of phospholiase D of Protozoan Tetrahymena cells. J. Eukaryot. Microbiol., 48: 194-201, 2001 https://doi.org/10.1111/j.1550-7408.2001.tb00303.x
  40. Yoshinaga, T. and Nakazoe, J.: Isolation and in vitro cultivation of an unidentified ciliate causing scuticociliatosis in Japanese flounder, Paralichthys olivaceus. Gyobyo Kenkyu, 28: 131-134, 1993 https://doi.org/10.3147/jsfp.28.131