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. 1994 Jun 15;300(Pt 3):619–622. doi: 10.1042/bj3000619

The localization of phospholipase A2 in the secretory granule.

S P Chock 1, E A Schmauder-Chock 1, E Cordella-Miele 1, L Miele 1, A B Mukherjee 1
PMCID: PMC1138211  PMID: 8010941

Abstract

A heat-resistant phospholipase A2 has been detected in the secretory granules of the mast cell [Chock, Rhee, Tang and Schmauder-Chock (1991) Eur. J. Biochem. 195, 707-713]. By using ultrastructural immunocytochemical techniques, we have now localized this enzyme to the matrix of the secretory granule. Like the cyclo-oxygenase [Schmauder-Chock and Chock (1989) J. Histochem. Cytochem. 37, 1319-1328], this enzyme also adheres tightly to the ribbon-like granule matrix components. The results from Western-blot analysis suggest that it has a molecular mass of about 14 kDa. The localization of the phospholipase A2, the presence of a phospholipid store with millimolar concentrations of calcium and the localization of the enzymes of the arachidonic acid cascade make the secretory granule a natural site for lipid-mediator synthesis. The packaging of phospholipase A2, together with its substrate and the components of the arachidonic acid cascade, in the secretory granule represents a physical arrangement by which the initiation of the cascade and the release of mediators can be directly linked to the stimulation of cell-surface receptors.

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Selected References

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  1. Aarsman A. J., Leunissen-Bijvelt J., Van den Koedijk C. D., Neys F. W., Verkleij A. J., Van den Bosch H. Phospholipase A2 activity in platelets. Immuno-purification and localization of the enzyme in rat platelets. J Lipid Mediat. 1989 Jan-Feb;1(1):49–61. [PubMed] [Google Scholar]
  2. Arita H., Hanasaki K., Nakano T., Oka S., Teraoka H., Matsumoto K. Novel proliferative effect of phospholipase A2 in Swiss 3T3 cells via specific binding site. J Biol Chem. 1991 Oct 15;266(29):19139–19141. [PubMed] [Google Scholar]
  3. Bach M. K. Mediators of anaphylaxis and inflammation. Annu Rev Microbiol. 1982;36:371–413. doi: 10.1146/annurev.mi.36.100182.002103. [DOI] [PubMed] [Google Scholar]
  4. Baek S. H., Takayama K., Kudo I., Inoue K., Lee H. W., Do J. Y., Chang H. W. Detection and characterization of extracellular phospholipase A2 in pleural effusion of patients with tuberculosis. Life Sci. 1991;49(15):1095–1102. doi: 10.1016/0024-3205(91)90597-5. [DOI] [PubMed] [Google Scholar]
  5. Basso D., Fabris C., Panozzo M. P., Meggiato T., Del Favero G., Naccarato R. Serum phospholipase A2 activity in chronic pancreatic diseases. Clin Biochem. 1990 Jun;23(3):229–232. doi: 10.1016/0009-9120(90)90653-c. [DOI] [PubMed] [Google Scholar]
  6. Bito L. Z., Baroody R. A. Impermeability of rabbit erythrocytes to prostaglandins. Am J Physiol. 1975 Dec;229(6):1580–1584. doi: 10.1152/ajplegacy.1975.229.6.1580. [DOI] [PubMed] [Google Scholar]
  7. Burnette W. N. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate--polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem. 1981 Apr;112(2):195–203. doi: 10.1016/0003-2697(81)90281-5. [DOI] [PubMed] [Google Scholar]
  8. Chock S. P., Rhee S. G., Tang L. C., Schmauder-Chock E. A. Linking phospholipase A2 to phospholipid turnover and prostaglandin synthesis in mast cell granules. Eur J Biochem. 1991 Feb 14;195(3):707–713. doi: 10.1111/j.1432-1033.1991.tb15757.x. [DOI] [PubMed] [Google Scholar]
  9. Chock S. P., Schmauder-Chock E. A. A new model for the mechanism of stimulus-secretion coupling. Biofactors. 1990 Jul;2(3):133–146. [PubMed] [Google Scholar]
  10. Chock S. P., Schmauder-Chock E. A. Phospholipid storage in the secretory granule of the mast cell. J Biol Chem. 1989 Feb 15;264(5):2862–2868. [PubMed] [Google Scholar]
  11. Chock S. P., Schmauder-Chock E. A. Synthesis of prostaglandins and eicosanoids by the mast cell secretory granule. Biochem Biophys Res Commun. 1988 Nov 15;156(3):1308–1315. doi: 10.1016/s0006-291x(88)80775-7. [DOI] [PubMed] [Google Scholar]
  12. Chock S. P., Schmauder-Chock E. A. The secretory granule and the mechanism of stimulus-secretion coupling. Curr Top Cell Regul. 1992;32:183–208. doi: 10.1016/b978-0-12-152832-4.50006-9. [DOI] [PubMed] [Google Scholar]
  13. Chung K. F., Barnes P. J. Role for platelet-activating factor in asthma. Lipids. 1991 Dec;26(12):1277–1279. doi: 10.1007/BF02536547. [DOI] [PubMed] [Google Scholar]
  14. Coceani F., Pace-Asciak C., Volta F., Wolfe L. S. Effect of nerve stimulation on prostaglandin formation and release from the rat stomach. Am J Physiol. 1967 Oct;213(4):1056–1064. doi: 10.1152/ajplegacy.1967.213.4.1056. [DOI] [PubMed] [Google Scholar]
  15. Cordella-Miele E., Miele L., Mukherjee A. B. Identification of a specific region of low molecular weight phospholipases A2 (residues 21-40) as a potential target for structure-based design of inhibitors of these enzymes. Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10290–10294. doi: 10.1073/pnas.90.21.10290. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Davies B. N., Horton E. W., Withrington P. G. The occurrence of prostaglandin E2 in splenic venous blood of the dog following splenic nerve stimulation. Br J Pharmacol Chemother. 1968 Jan;32(1):127–135. doi: 10.1111/j.1476-5381.1968.tb00436.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Dennis E. A., Rhee S. G., Billah M. M., Hannun Y. A. Role of phospholipase in generating lipid second messengers in signal transduction. FASEB J. 1991 Apr;5(7):2068–2077. doi: 10.1096/fasebj.5.7.1901288. [DOI] [PubMed] [Google Scholar]
  18. Hara S., Kudo I., Chang H. W., Matsuta K., Miyamoto T., Inoue K. Purification and characterization of extracellular phospholipase A2 from human synovial fluid in rheumatoid arthritis. J Biochem. 1989 Mar;105(3):395–399. doi: 10.1093/oxfordjournals.jbchem.a122675. [DOI] [PubMed] [Google Scholar]
  19. Kramer R. M., Johansen B., Hession C., Pepinsky R. B. Characterization of a secretable phospholipase A2 from human platelets. Adv Prostaglandin Thromboxane Leukot Res. 1990;20:79–86. [PubMed] [Google Scholar]
  20. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  21. Lai C. Y., Wada K. Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme. Biochem Biophys Res Commun. 1988 Dec 15;157(2):488–493. doi: 10.1016/s0006-291x(88)80275-4. [DOI] [PubMed] [Google Scholar]
  22. Lands W. E., Samuelsson B. Phospholipid precursors of prostaglandins. Biochim Biophys Acta. 1968 Oct 22;164(2):426–429. doi: 10.1016/0005-2760(68)90168-9. [DOI] [PubMed] [Google Scholar]
  23. Lanni C., Becker E. L. Release of phospholipase A2 activity from rabbit peritoneal neutrophils by f-Met-Leu-Phe. Am J Pathol. 1983 Oct;113(1):90–94. [PMC free article] [PubMed] [Google Scholar]
  24. Lin L. L., Wartmann M., Lin A. Y., Knopf J. L., Seth A., Davis R. J. cPLA2 is phosphorylated and activated by MAP kinase. Cell. 1993 Jan 29;72(2):269–278. doi: 10.1016/0092-8674(93)90666-e. [DOI] [PubMed] [Google Scholar]
  25. Mican J. M., Metcalfe D. D. Arthritis and mast cell activation. J Allergy Clin Immunol. 1990 Oct;86(4 Pt 2):677–683. doi: 10.1016/s0091-6749(05)80240-4. [DOI] [PubMed] [Google Scholar]
  26. Mukherjee A. B., Cordella-Miele E., Miele L. Regulation of extracellular phospholipase A2 activity: implications for inflammatory diseases. DNA Cell Biol. 1992 Apr;11(3):233–243. doi: 10.1089/dna.1992.11.233. [DOI] [PubMed] [Google Scholar]
  27. Murakami M., Kudo I., Fujimori Y., Suga H., Inoue K. Group II phospholipase A2 inhibitors suppressed lysophosphatidylserine-dependent degranulation of rat peritoneal mast cells. Biochem Biophys Res Commun. 1991 Dec 16;181(2):714–721. doi: 10.1016/0006-291x(91)91249-c. [DOI] [PubMed] [Google Scholar]
  28. Murakami M., Kudo I., Inoue K. Eicosanoid generation from antigen-primed mast cells by extracellular mammalian 14-kDa group II phospholipase A2. FEBS Lett. 1991 Dec 9;294(3):247–251. doi: 10.1016/0014-5793(91)81440-j. [DOI] [PubMed] [Google Scholar]
  29. Neale M. L., Fiera R. A., Matthews N. Involvement of phospholipase A2 activation in tumour cell killing by tumour necrosis factor. Immunology. 1988 May;64(1):81–85. [PMC free article] [PubMed] [Google Scholar]
  30. Pernas P., Masliah J., Olivier J. L., Salvat C., Rybkine T., Bereziat G. Type II phospholipase A2 recombinant overexpression enhances stimulated arachidonic acid release. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1298–1305. doi: 10.1016/0006-291x(91)91035-b. [DOI] [PubMed] [Google Scholar]
  31. Ramwell P. W., Shaw J. E., Douglas W. W., Poisner A. M. Efflux of prostaglandin from adrenal glands stimulated with acetylcholine. Nature. 1966 Apr 16;210(5033):273–274. doi: 10.1038/210273a0. [DOI] [PubMed] [Google Scholar]
  32. Schalkwijk C. G., Märki F., Wiesenberg I., van den Bosch H. The detection of multimeric forms of phospholipase A2 upon sodium dodecylsulfate-polyacrylamide electrophoresis. J Lipid Mediat. 1991 Jul-Aug;4(1):83–95. [PubMed] [Google Scholar]
  33. Schmauder-Chock E. A., Chock S. P. Localization of cyclo-oxygenase and prostaglandin E2 in the secretory granule of the mast cell. J Histochem Cytochem. 1989 Sep;37(9):1319–1328. doi: 10.1177/37.9.2504812. [DOI] [PubMed] [Google Scholar]
  34. Smith L. J. The role of platelet-activating factor in asthma. Am Rev Respir Dis. 1991 May;143(5 Pt 2):S100–S102. doi: 10.1164/ajrccm/143.5_Pt_2.S100. [DOI] [PubMed] [Google Scholar]
  35. Stefanski E., Pruzanski W., Sternby B., Vadas P. Purification of a soluble phospholipase A2 from synovial fluid in rheumatoid arthritis. J Biochem. 1986 Nov;100(5):1297–1303. doi: 10.1093/oxfordjournals.jbchem.a121836. [DOI] [PubMed] [Google Scholar]
  36. Ulevitch R. J., Watanabe Y., Sano M., Lister M. D., Deems R. A., Dennis E. A. Solubilization, purification, and characterization of a membrane-bound phospholipase A2 from the P388D1 macrophage-like cell line. J Biol Chem. 1988 Mar 5;263(7):3079–3085. [PubMed] [Google Scholar]
  37. Vadas P., Pruzanski W. Role of secretory phospholipases A2 in the pathobiology of disease. Lab Invest. 1986 Oct;55(4):391–404. [PubMed] [Google Scholar]
  38. Vane J. R. Antiinflammatory drugs and the many mediators of inflammation. Int J Tissue React. 1987;9(1):1–14. [PubMed] [Google Scholar]

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