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Archives of Pharmacal Research

, Volume 21, Issue 6, pp 774–778 | Cite as

Effects of brazilin on the phospholipase A2 activity and changes of intracellular free calcium concentration in rat platelets

  • Gwi-Seo Hwang
  • Ji-Young Kim
  • Tong-Shin Chang
  • Sun-Duck Jeon
  • Dhong-Su So
  • Chang-Kiu Moon
Research Articles

Abstract

Brazilin {7,11 b-dihydrobenz[b]indeno[1,2-d]pyran-3,6a,9,10(6H)-tetrol} inhibited thrombin-, collagen-and ADP-induced aggregation of washed rat platelets. Thrombin- and collagen-induced ATP release were also inhibited by brazilin in a concentration-dependent manner. Brazilin inhibited the formation of platelet thromboxane A2 caused by thrombin, whereas it had no effect on the prostaglandin D2 formation. Brazilin inhibited [3H]-arachidonic acid liberation from membrane phospholipids of thrombin-stimulated platelets. Brazilin inhibited the rise of intracellular free calcium caused by thrombin. These results indicate that the inhibition of phospholipase (PLA2) activity and [Ca2+]i elevation might be at least a part of antiplatelet mechanism of brazilin.

Key words

Brazilin Caesalpinia sappan Aggregation Phospholipase A2 Platelet Intracellular free calcium 

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References Cited

  1. Alarayyed, N. A., Cooper, M. B., Prichard, B. N., Betteridge, D. J. and Smith, C. C.,In vitro adrenaline and collagen-induced mobilization of platelet calcium and its inhibition by naftopidil, doxazosin and nifedipine.Br. J. Clin. Pharmacol., 43, 415–420 (1997).PubMedCrossRefGoogle Scholar
  2. Choi, S. Y. and Moon, C. K., Effects of brazilin on the altered immune functions in the early phase of halothane intoxication of C57BL/6 mice.Planta Med., 63, 400–404 (1997a).PubMedCrossRefGoogle Scholar
  3. Choi, S. Y., Yang, K. M., Jeon, S. D., Kim, J. H., Khil, L. Y., Chang, T. S. and Moon, C. K., Brazilin modulates immune function mainly by augmenting T cell activity in halothane administered mice.Planta Med., 63, 405–408 (1997b).PubMedCrossRefGoogle Scholar
  4. Clark, J. D., Lin, L. L., Kriz, R. W., Ramesha, C. S., Sultzman, L. A., Lin, A. Y., Milona, N. and Knopf, J. L., A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP.Cell, 65, 1043–1051 (1991).PubMedCrossRefGoogle Scholar
  5. DeLuca, M. and McElroy, W. D., Purification and properties of firefly luciferase.Methods Enzymol., 57, 3–15 (1978).CrossRefGoogle Scholar
  6. FitzGerald, G. A., Healy, C. and Daugherty, J., Thromboxane A2 biosynthesis in human disease.Fed. Proc., 46, 154–158 (1987).PubMedGoogle Scholar
  7. FitzGerald, G. A., Mechanisms of platelet activation: thromboxane A2 as an amplifying signal for other agonists.Am. J. Cardiol., 68, 11B-15B (1991).PubMedCrossRefGoogle Scholar
  8. Gresele, P., Deckmyn, H., Nenci, G. G. and Vermylen, J., Thromboxane synthase inhibitors, thromboxane receptor antagonists and dual blockers in thrombotic disorders.Trends Pharmacol. Sci., 12, 158–163 (1991).PubMedCrossRefGoogle Scholar
  9. Hornby, E. J. and Skidmore, I. F., Evidence that prostaglandin endoperoxides can induce platelet aggregation in the absence of thromboxane A2 production.Biochem. Pharmacol., 31, 1158–60 (1982).PubMedCrossRefGoogle Scholar
  10. Johnson, P. C., Ware, J. A., Cliveden, P. B., Smith, M., Dvorak, A. M. and Salzman, E. W., Measurement of ionized calcium in blood platelets with the photoprotein aequorin.J. Biol. Chem., 260, 2069–2076 (1985).PubMedGoogle Scholar
  11. Khil, L. Y., Cheon, A. J., Chang, T. S. and Moon, C. K., Effects of calcium on brazilin-induced glucose transport in isolated rat epididymal adipocytes.Biochem. Pharmacol., 54, 97–101 (1997).PubMedCrossRefGoogle Scholar
  12. Kim, D. K., Kudo, I. and Inoue, K., Purification and characterization of rabbit platelet cytosolic phospholipase A2.Biochim. Biophys. Acta, 1083, 80–88 (1991).PubMedGoogle Scholar
  13. Kim, Y. M., Kim, S. G., Khil, L. Y. and Moon, C. K., Brazilin stimulates the glucose transport in 3T3-L1 cells.Planta Med., 61, 297–301 (1995).PubMedCrossRefGoogle Scholar
  14. Kondo, K., Kitada, C., Yoshioka, A., Sakane, H., Kokawa, T. and Yasunaga, K., Inhibition of platelet aggregation by low concentrations of sodium fluoride. Significance of the intracellular calcium ion concentration.Int. J. Hematol., 54, 411–417 (1991).PubMedGoogle Scholar
  15. Loeb, L. A. and Gross, R. W., Identification and purification of sheep platelet phospholipase A2 isoforms. Activation by physiologic concentrations of calcium ion.J. Biol. Chem., 261, 10467–10470 (1986).PubMedGoogle Scholar
  16. Moon, C. K., Lee, S. H., Lee, M. O. and Kim, S. G., Effects of brazilin on glucose oxidation, lipogenesis and therein involved enzymes in adipose tissues from diabetic KK-mice.Life Sci., 53, 1291–1297 (1993).PubMedCrossRefGoogle Scholar
  17. Mounier, C., Faili, A., Vargaftig, B. B., Bon, C. and Hatmi, M., Secretory phospholipase A2 is not required for arachidonic acid liberation during platelet activation.Eur. J. Biochem., 216, 169–175 (1993).PubMedCrossRefGoogle Scholar
  18. Mustard, J. F., Perry, D. W., Ardlie, N. G. and Packham, M. A., Preparation of suspensions of washed platelets from humans.Br. J. Haematol., 22, 193–204 (1972).PubMedCrossRefGoogle Scholar
  19. Nalefski, E. A., Sultzman, L. A., Martin, D. M., Kriz, R. W., Towler, P. S., Knopf, J. L. and Clark, J. D., Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain.J. Biol. Chem., 269, 18239–18249 (1994).PubMedGoogle Scholar
  20. Smith, J. B., Dangelmaier, C. and Mauco, G., Measurement of arachidonic acid liberation in thrombin-stimulated human platelets. Use of agents that inhibit both the cyclooxygenase and lipoxygenase enzymes.Biochim. Biophys. Acta, 835, 344–351 (1985).PubMedGoogle Scholar
  21. Takayama, K., Kudo, I., Kim, D. K., Nagata, K., Nozawa, Y. and Inoue, K., Purification and characterization of human platelet phospholipase A2 which preferentially hydrolyzes an arachidonoyl residue.FEBS Lett., 282, 326–330 (1991).PubMedCrossRefGoogle Scholar

Copyright information

© The Pharmaceutical Society of Korea 1998

Authors and Affiliations

  • Gwi-Seo Hwang
    • 1
  • Ji-Young Kim
    • 2
  • Tong-Shin Chang
    • 2
  • Sun-Duck Jeon
    • 2
  • Dhong-Su So
    • 2
  • Chang-Kiu Moon
    • 2
  1. 1.College of Oriental MedicineKyung Won UniversitySeongnamKorea
  2. 2.College of PharmacySeoul National UniversitySeoulKorea

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