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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Antiplatelet and antithrombotic activities of purpurogallin in vitro and in vivo

  • Ku, Sae-Kwang (Department of Anatomy and Histology, College of Korean Medicine, Daegu Haany University) ;
  • Bae, Jong-Sup (College of Pharmacy, CMRI, Research Institute of Pharmaceutical Sciences, Kyungpook National University)
  • Received : 2013.08.27
  • Accepted : 2013.10.21
  • Published : 2014.07.31
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Abstract

Enzymatic oxidation of pyrogallol was efficiently transformed to an oxidative product, purpurogallin (PPG). Here, the anticoagulant activities of PPG were examined by monitoring activated partial thromboplastin time (aPTT), prothrombin time (PT), and the activities of thrombin and activated factor X (FXa). And, the effects of PPG on expression of plasminogen activator inhibitor type 1 (PAI-1) and tissue-type plasminogen activator (t-PA) were evaluated in tumor necrosis factor (TNF)-${\alpha}$ activated human umbilical vein endothelial cells (HUVECs). Treatment with PPG resulted in prolonged aPTT and PT and inhibition of the activities of thrombin and FXa, as well as inhibited production of thrombin and FXa in HUVECs. In addition, PPG inhibited thrombin-catalyzed fibrin polymerization and platelet aggregation. PPG also elicited anticoagulant effects in mice. In addition, treatment with PPG resulted in significant reduction of the PAI-1 to t-PA ratio. Collectively, PPG possesses antithrombotic activities and offers a basis for development of a novel anticoagulant.

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References

  1. Hoffman, M. M. and Monroe, D. M. (2005) Rethinking the coagulation cascade. Curr. Hematol. Rep. 4, 391-396.
  2. Davie, E. W., Fujikawa, K. and Kisiel, W. (1991) The coagulation cascade: initiation, maintenance, and regulation. Biochemistry. 30, 10363-10370. https://doi.org/10.1021/bi00107a001
  3. Davie, E. W. (1995) Biochemical and molecular aspects of the coagulation cascade. Thromb. Haemost. 74, 1-6.
  4. Esmon, C. T. (2001) Role of coagulation inhibitors in inflammation. Thromb. Haemost. 86, 51-56.
  5. Quinn, C., Hill, J. and Hassouna, H. (2000) A guide for diagnosis of patients with arterial and venous thrombosis. Clin. Lab. Sci. 13, 229-238.
  6. Levi, M., Schultz, M. and van der Poll, T. (2011) Coagulation biomarkers in critically ill patients. Crit. Care Clin. 27, 281-297. https://doi.org/10.1016/j.ccc.2010.12.009
  7. Abou-Karam, M. and Shier, W. T. (1999) Inhibition of oncogene product enzyme activity as an approach to cancer chemoprevention. Tyrosine-specific protein kinase inhibition by purpurogallin from Quercus sp. nutgall. Phytother. Res. 13, 337-340. https://doi.org/10.1002/(SICI)1099-1573(199906)13:4<337::AID-PTR451>3.0.CO;2-J
  8. Das, M., Bickers, D. R. and Mukhtar, H. (1984) Plant phenols as in vitro inhibitors of glutathione S-transferase(s). Biochem. Biophys. Res. Commun. 120, 427-433. https://doi.org/10.1016/0006-291X(84)91271-3
  9. Zeng, L. H. and Wu, T. W. (1992) Purpurogallin is a more powerful protector of kidney cells than Trolox and allopurinol. Biochem. Cell Biol. 70, 684-690. https://doi.org/10.1139/o92-104
  10. Veser, J. (1987) Kinetics and inhibition studies of catechol O-methyltransferase from the yeast Candida tropicalis. J. Bacteriol. 169, 3696-3700. https://doi.org/10.1128/jb.169.8.3696-3700.1987
  11. Wu, T. W., Zeng, L. H., Wu, J. and Carey, D. (1991) Purpurogallin--a natural and effective hepatoprotector in vitro and in vivo. Biochem. Cell Biol. 69, 747-750. https://doi.org/10.1139/o91-113
  12. Wu, T. W., Zeng, L. H., Wu, J., Fung, K. P., Weisel, R. D., Hempel, A. and Camerman, N. (1996) Molecular structure and antioxidant specificity of purpurogallin in three types of human cardiovascular cells. Biochem. Pharmacol. 52, 1073-1080. https://doi.org/10.1016/0006-2952(96)00447-9
  13. Inamori, Y., Muro, C., Sajima, E., Katagiri, M., Okamoto, Y., Tanaka, H., Sakagami, Y. and Tsujibo, H. (1997) Biological activity of purpurogallin. Biosci. Biotechnol. Biochem. 61, 890-892. https://doi.org/10.1271/bbb.61.890
  14. Kim, T. H., Ku, S. K., Lee, I. C. and Bae, J. S. (2012) Anti-inflammatory functions of purpurogallin in LPS-activated human endothelial cells. BMB Rep. 45, 200-205. https://doi.org/10.5483/BMBRep.2012.45.3.200
  15. Esmon, C. T. (2005) The interactions between inflammation and coagulation. Br. J. Haematol. 131, 417-430. https://doi.org/10.1111/j.1365-2141.2005.05753.x
  16. Sugo, T., Nakamikawa, C., Tanabe, S. and Matsuda, M. (1995) Activation of prothrombin by factor Xa bound to the membrane surface of human umbilical vein endothelial cells: its catalytic efficiency is similar to that of prothrombinase complex on platelets. J. Biochem. 117, 244-250. https://doi.org/10.1093/jb/117.2.244
  17. Rao, L. V., Rapaport, S. I. and Lorenzi, M. (1988) Enhancement by human umbilical vein endothelial cells of factor Xa-catalyzed activation of factor VII. Blood 71, 791-796.
  18. Ghosh, S., Ezban, M., Persson, E., Pendurthi, U., Hedner, U. and Rao, L. V. (2007) Activity and regulation of factor VIIa analogs with increased potency at the endothelial cell surface. J. Thromb. Haemost. 5, 336-346. https://doi.org/10.1111/j.1538-7836.2007.02308.x
  19. Philip-Joet, F., Alessi, M. C., Philip-Joet, C., Aillaud, M., Barriere, J. R., Arnaud, A. and Juhan-Vague, I. (1995) Fibrinolytic and inflammatory processes in pleural effusions. Eur. Respir. J. 8, 1352-1356. https://doi.org/10.1183/09031936.95.08081352
  20. Schleef, R. R., Bevilacqua, M. P., Sawdey, M., Gimbrone, M. A., Jr. and Loskutoff, D. J. (1988) Cytokine activation of vascular endothelium. Effects on tissue-type plasminogen activator and type 1 plasminogen activator inhibitor. J. Biol. Chem. 263, 5797-5803.
  21. Hamaguchi, E., Takamura, T., Shimizu, A. and Nagai, Y. (2003) Tumor necrosis factor-alpha and troglitazone regulate plasminogen activator inhibitor type 1 production through extracellular signal-regulated kinase- and nuclear factor-kappaB-dependent pathways in cultured human umbilical vein endothelial cells. J. Pharmacol. Exp. Ther. 307, 987-994. https://doi.org/10.1124/jpet.103.054346
  22. Lopez, S., Peiretti, F., Bonardo, B., Juhan-Vague, I. and Nalbone, G. (2000) Effect of atorvastatin and fluvastatin on the expression of plasminogen activator inhibitor type-1 in cultured human endothelial cells. Atherosclerosis 152, 359-366. https://doi.org/10.1016/S0021-9150(00)00454-8
  23. Schouten, M., Wiersinga, W. J., Levi, M. and van der Poll, T. (2008) Inflammation, endothelium, and coagulation in sepsis. J. Leukoc. Biol. 83, 536-545. https://doi.org/10.1189/jlb.0607373
  24. Kim, T. H., Ku, S. K. and Bae, J. S. (2012) Antithrombotic and profibrinolytic activities of eckol and dieckol. J. Cell Biochem. 113, 2877-2883. https://doi.org/10.1002/jcb.24163
  25. Kim, S. Y., Kim, S., Kim, J. M., Jho, E. H., Park, S., Oh, D. and Yun-Choi, H. S. (2011) PKC inhibitors RO 31-8220 and Go 6983 enhance epinephrine-induced platelet aggregation in catecholamine hypo-responsive platelets by enhancing Akt phosphorylation. BMB Rep. 44, 140-145. https://doi.org/10.5483/BMBRep.2011.44.2.140
  26. Nowak, P., Zbikowska, H. M., Ponczek, M., Kolodziejczyk, J. and Wachowicz, B. (2007) Different vulnerability of fibrinogen subunits to oxidative/nitrative modifications induced by peroxynitrite: functional consequences. Thromb. Res. 121, 163-174. https://doi.org/10.1016/j.thromres.2007.03.017
  27. Bae, J. S. and Rezaie, A. R. (2008) Protease activated receptor 1 (PAR-1) activation by thrombin is protective in human pulmonary artery endothelial cells if endothelial protein C receptor is occupied by its natural ligand. Thromb Haemost 100, 101-109.
  28. Bae, J. S. (2011) Antithrombotic and profibrinolytic activities of phloroglucinol. Food Chem. Toxicol. 49, 1572-1577. https://doi.org/10.1016/j.fct.2011.04.003
  29. Dejana, E., Callioni, A., Quintana, A. and de Gaetano, G. (1979) Bleeding time in laboratory animals. II - A comparison of different assay conditions in rats. Thromb. Res. 15, 191-197. https://doi.org/10.1016/0049-3848(79)90064-1

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