Effects of Albizziae Cortex Extracts on the Elastase Activity and DPPH and NO Scavenging Activities

  • Received : 2011.03.17
  • Accepted : 2011.04.13
  • Published : 2011.04.25

Abstract

Elastic fibers are found in the skin, lungs, arteries, veins and other structures. Elastases destroy the elastic fibers and cause the emphysema and pulmonary hypertension. Oxidative stress is needed for these pathologic changes. Accordingly, present study was designed to investigate the effect of Albizziae Cortex extracts (ACE) on elastase activity and anti-oxidative effects of ACE. The in vitro inhibitory effects on elastase and di(phenyl)-(2,4,6-trinitrophenyl)iminoazanium (DPPH) and nitric oxide (NO) free radical scavenging activities of ACE were measured. The elastase activity was significantly inhibited by ACE. DPPH and NO free radicals were significantly scavenged as well. ACE showed the elastase-inhibiting effects and anti-oxidative activities in vitro. These results suggest that ACE may have potential roles in the treatment of pulmonary emphysema and pulmonary hypertension.

Keywords

References

  1. The Boncho-hak textbook committee. Boncho-Hak. Seoul, Young-Lim Press, pp 534-535, 2007.
  2. Chen, J.L., Chen, T.T. Chinese medical herbology and pharmacology. CA, Art of Medicine Press, pp 768-769, 2004.
  3. Bieth, J.G. The elastases. J Soc Biol 195(2):173-179, 2001. https://doi.org/10.1051/jbio/2001195020173
  4. Loukanov, T., Geiger, R., Agrawal, R. Animal models related to congenital heart disease and clinical research in pulmonary hypertension. Cardiology 116(1):18-25, 2010. https://doi.org/10.1159/000313865
  5. Dewachter, L., Dewachter, C., Naeije, R. New therapies for pulmonary arterial hypertension: An update on current bench to bedside translation. Expert Opin Investig Drugs 19(4):469-488, 2010. https://doi.org/10.1517/13543781003727099
  6. Stenmark, K.R., Rabinovitch, M. Emerging therapies for the treatment of pulmonary hypertension. Pediatr Crit Care Med 11(2 Suppl):S85-90, 2010. https://doi.org/10.1097/PCC.0b013e3181c76db3
  7. Huang, J.B., Liu, Y.L., Sun, P.W., Lv, X.D., Bo, K., Fan, X.M. Novel strategy for treatment of pulmonary arterial hypertension: Enhancement of apoptosis. Lung 188(3):179-189, 2010. https://doi.org/10.1007/s00408-010-9233-8
  8. Groneberg, D.A., Chung, K.F. Models of chronic obstructive pulmonary disease. Respir Res 5: 18, 2004. https://doi.org/10.1186/1465-9921-5-18
  9. Mandl, I., Darnule, T.V., Fierer, J.A., Keller, S., Turino, G.M. Elastin degradation in human and experimental emphysema. Adv Exp Med Biol 79: 221-231, 1977.
  10. Dubaybo, B.A., Crowell, L.A., Thet, L.A. Changes in tissue fibronectin in elastase induced lung injury. Cell Biol Int Rep 15(8):675-686, 1991. https://doi.org/10.1016/0309-1651(91)90068-T
  11. Lucey, E.C., Keane, J., Kuang, P.P., Snider, G.L., Goldstein, R.H. Severity of elastase-induced emphysema is decreased in tumor necrosis factor-alpha and interleukin-1beta receptor-deficient mice. Lab Invest 82(1):79-85, 2002. https://doi.org/10.1038/labinvest.3780397
  12. Hayes, J.A., Korthy, A., Snider, G.L. The pathology of elastase-induced panacinar emphysema in hamsters. J Pathol 117(1):1-14, 1975. https://doi.org/10.1002/path.1711170102
  13. Fischer, B., Voynow, J. Neutrophil elastase induces MUC5AC messenger RNA expression by an oxidant-dependent mechanism. Chest 117(5 Suppl 1): 317S-320S, 2000. https://doi.org/10.1378/chest.117.5_suppl_1.317S
  14. Fischer, B.M., Voynow, J.A. Neutrophil elastase induces MUC5AC gene expression in airway epithelium via a pathway involving reactive oxygen species. Am J Respir Cell Mol Biol 26(4):447-452, 2002. https://doi.org/10.1165/ajrcmb.26.4.4473
  15. Kawai, M., Harada, N., Takeyama, H., Okajima, K. Neutrophil elastase contributes to the development of ischemia/reperfusion-induced liver injury by decreasing the production of insulin-like growth factor-I in rats. Transl Res 155(6):294-304, 2010. https://doi.org/10.1016/j.trsl.2010.02.003
  16. Kraunsoe, J.A., Claridge, T.D.W., Lowe, G. Inhibition of human leukocyte and porcine pancreatic elastase by homologues of bovine pancreatic trypsin inhibitor. Biochemistry 35: 9090-9096, 1996. https://doi.org/10.1021/bi953013b
  17. Kim, Y.H., Chung, C.B., Kim, J.G., Ko, K.I., Park, S.H., Kim, J.H., Eom, S.Y., Kim, Y.S., Hwang, Y.I., Kim, K.H. Anti-wrinkle activity of ziyuglycoside I isolated from a Sanguisorba officinalis root extract and its application as a cosmeceutical ingredient. Biosci Biotechnol Biochem 72(2):303-311, 2008. https://doi.org/10.1271/bbb.70268
  18. Shimada, K., Fugikawa, K., Yahara, K., Nakamura, T. Antioxidative properties of xanthan on the autoxiation of soy gean oil in cyclodextrin emulsion. J Agric Food Chem 40: 945-948, 1992. https://doi.org/10.1021/jf00018a005
  19. Kato, H., Lee, I.E., Chuyen, N.V., Kim, S.B., Hayase, F. Inhibition of nitrosamine formation by nondialyzable melanoidins. Agric Biol Chem 51(5):1333-1338, 1987. https://doi.org/10.1271/bbb1961.51.1333
  20. Yang, Z.Y., Guon, G.X., Lin, Z.F. Elastolytic activity from Flavobacterium odoratum. Microbial screening and cultivation, enzyme production and purification. Process Biochem 29: 427-436, 1994. https://doi.org/10.1016/0032-9592(94)85010-0
  21. Wiltried, M., Klaus, N., Lin, Z.F. Elastic fibre arrangement in the skin of the pig. Arch Derm Res 270: 390-401, 1994.
  22. Wiedow, O., Schroder, J.M., Christophers, E. An elastase-specific inhibitor of human skin. J Biol Chem 265: 14791-14795, 1990.
  23. Lungarella, G., Cavarra, E., Lucattelli, M., Martorana, P.A. The dual role of neutrophil elastase in lung destruction and repair. Int J Biochem Cell Biol 40(6-7):1287-1296, 2008. https://doi.org/10.1016/j.biocel.2007.12.008
  24. Reboud-Ravaux, M. Elastase inhibitors. J Soc Biol 195(2):143-150, 2001. https://doi.org/10.1051/jbio/2001195020143
  25. Boyer, L., Plantier, L., Dagouassat, M., Lanone, S., Goven, D., Caramelle, P., Berrehar, F., Kerbrat, S., Dinh-Xuan, A.T., Crestani, B., Le Gouvello, S., Boczkowski, J. Role of nitric oxide synthases in elastase-induced emphysema. Lab Invest 91(3):353-362, 2011. https://doi.org/10.1038/labinvest.2010.169