Bulletin of the Korean Chemical Society

  • 제25권7호
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  • Pages.1055-1060
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  • 2004
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  • 0253-2964(pISSN)
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  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
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A New Cyclophilin Inhibitor from Ganoderma lucidum: Purification and Characterization

  • Lim, Jin-Ik (Department of Chemistry, College of Sciences and Research Institute of Basic Sciences, Kyung Hee University) ;
  • Jeong, Ki-Chul (Department of Chemistry, College of Sciences and Research Institute of Basic Sciences, Kyung Hee University) ;
  • Kang, In-Sug (Department of Molecular Biology, College of Medicine, Kyung Hee University) ;
  • Kim, Soo-Ja (Department of Chemistry, College of Sciences and Research Institute of Basic Sciences, Kyung Hee University)
  • 발행 : 2004.07.20
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초록

A new inhibitor for peptidylprolyl cis-trans isomerase (PPIase) has been isolated from Ganoderma lucidum and purified to homogeneous state by organic solvent extraction. The purified PPIase inhibitor (GPI) is assumed to be a membrane-associated glycoprotein. GPI inhibits specifically the bovine brain PPIase, a cyclophilin, and has no effect on the FKBP activity. The results of our chemical modification study of GPI indicate the presence of Lys residue(s) at or near its binding site. Like CsA-cyclophilin complex, GPI-bovine brain PPIase complex strongly inhibits the calcineurin activity in vitro, suggesting the possible involvement of GPI in immunomodulating pathway by the formation of PPIase-inhibitor-calcineurin complex.

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참고문헌

  1. Fischer, G.; Bang, H.; Mech, C. Biomed. Biochim. Acta 1984, 43, 1101.
  2. Fischer, G.; Bang, H. Biochim. Biophys. Acta 1984, 828, 39.
  3. Handschmacher, R. E.; Harding, M. W.; Rice, J.; Drugge, R. J.; Speicher, D. W. Science 1984, 226, 544. https://doi.org/10.1126/science.6238408
  4. Harding, M. W.; Handschmacher, R. E.; Speicher, D. W. J. Biol. Chem. 1986, 261, 8547.
  5. Takahashi, N.; Hayano, T.; Suzuki, M. Nature 1989, 337, 473. https://doi.org/10.1038/337473a0
  6. Fischer, G.; Wittmann-Liebold, B.; Lang, K.; Kiethaber, T.; Schmid, F. X. Nature 1989, 337, 476. https://doi.org/10.1038/337476a0
  7. Siekierks, J. J.; Hung, S. H. Y.; Poe, M.; Liu, C. S.; Sigal, N. H. Nature 1989, 341, 755. https://doi.org/10.1038/341755a0
  8. Harding, M. W.; Galat, A.; Uehling, D. E.; Schreiber, S. L. Nature 1989, 341, 758. https://doi.org/10.1038/341758a0
  9. Dumont, F. J.; Melino, M. R.; Staruch, M. J.; Koprak, S. L.; Fischer, P. A.; Sigal, N. H. J. Immunol. 1990, 144, 1418.
  10. Schreiber, S. L. Science 1991, 251, 283 https://doi.org/10.1126/science.1702904
  11. Handschmacher, R. E.; Harding, M. W. Transplantation 1988, 46, 298. https://doi.org/10.1097/00007890-198808000-00021
  12. Bierer, B. E.; Somers, R. K.; Wandless, S. J.; Burakoff, S. L.; Schreiber, S. L. Science 1990, 250, 556. https://doi.org/10.1126/science.1700475
  13. Bierer, B. E.; Mattila, P. S.; Standaert, R. F.; Herzencerg, L. A.; Burakoff, S. J.; Crabtree, G.; Schreiber, S. L. Proc. Nat. Acad. Sci. U.S.A. 1990, 87, 9231. https://doi.org/10.1073/pnas.87.23.9231
  14. Rahfeld, J. U.; Schierhorn, A.; Moun, K.; Fischer, G. FEBS Lett. 1994, 343, 65. https://doi.org/10.1016/0014-5793(94)80608-X
  15. Rudd, K. E.; Sofia, H. J.; Koonn, E. V.; Plunkett, G.; Lazar, S.; Rouvieree, P. R. Trends. Biochem. Sci. 1995, 20, 12. https://doi.org/10.1016/S0968-0004(00)88940-9
  16. Liu, J.; Farmer, J. D. J.; Lane, W. S.; Friedman, J.; Weissman, I.; Schreiber, S. L. Cell 1990, 66, 807.
  17. Liu, J.; Albers, M. W.; Wandless, T. J.; Luan, S.; Aqlberg, D. G.; Belshaw, P. J.; Cohen, P.; MacKintosh, C.; Klee, C. B.; Schreiber, S. L. Biochemistry 1992, 31, 3896. https://doi.org/10.1021/bi00131a002
  18. Fiedman, J.; Weissmann, I. Cell 1991, 66, 799. https://doi.org/10.1016/0092-8674(91)90123-G
  19. Sabatini, D. M.; Erdjument-Bromage, H.; Lui, M.; Tempst, P.; Snyder, S. H. Cell 1994, 78, 35. https://doi.org/10.1016/0092-8674(94)90570-3
  20. Sabatini, D. M.; Pierchala, B. A.; Barrow, R. K.; Schell, M. J.; Snyder, S. H. J. Biol. Chem. 1995, 270, 20875. https://doi.org/10.1074/jbc.270.36.20875
  21. Huang, S.; Bjornsti, M. A.; Houghton, P. J. Cancer Biol. Ther. 2003, 222.
  22. Durette, P. L.; Boger, J.; Dumont, F.; Firestone, R.; Frankshun, R. A.; Koprak, S. L.; Lin, C. S.; Melino, M. R.; Pessolano, A. A.; Pisano, J.; Schmidt, J. A.; Sigal, N. H.; Staruch, M. J.; Witzel, B. E. Transplant. Proc. 1988, 20, 51.
  23. Dumont, F. J.; Staruch, M. J.; Koprak, S. L.; Melino, M. R.; Sigal, N. H. J. Immunol. 1990, 144, 251.
  24. Clarissa, R. A.; Damaso, G.; Missin, M. J. Gen. Virol. 1988, 79, 339.
  25. Sigal, N. H.; Dumont, F. J.; Durette, P. L.; Siekierka, J. J.; Petersson, L.; Rich, D. H.; Dunlap, B. E.; Staruch, M. J.; Melino, M. R.; Koprak, S. L.; Williams, D.; Witzel, B.; Pisano, J. M. J. Exp. Med. 1991, 173, 619. https://doi.org/10.1084/jem.173.3.619
  26. Ocain, T. D.; Longhi, D.; Steffan, R. J.; Caccese, R. G.; Sehgal, S. N. Biochem. Biophys. Res. Commun. 1993, 192, 1340. https://doi.org/10.1006/bbrc.1993.1563
  27. Liu, J.; Walsh, C. T. Proc. Natl. Acad. Sci. U.S.A. 1993, 87, 4028. https://doi.org/10.1073/pnas.87.11.4028
  28. Skruzny, M.; Ambrozkova, M.; Fukzova, I.; Martinkova, K.; Blahuskova, A.; Hanplova, L.; Puta, F.; Folk, P. Biochim. Biophys. Acta 2001, 1521, 146. https://doi.org/10.1016/S0167-4781(01)00301-3
  29. Wasser, S. P.; Weis, L. Crit. Ev. Immunol. 1999, 65.
  30. Lee, S.; Park, S.; Oh, J. W.; Yang, C. Planta Med. 1988, 64, 303. https://doi.org/10.1055/s-2006-957439
  31. van der Hem, L. G.; van der Vliet, J. A.; Bocken, C. F.; Kino, K.; Hoitsma, A. J.; Tax, W. J. Transplantation 1995, 15, 438.
  32. Lim, J. I.; Bae, B. N.; Jhun, B. S.; Kang, I. S.; Kim, S. J. Bull. Korean Chem. Soc. 2003, 24, 1531. https://doi.org/10.5012/bkcs.2003.24.10.1531
  33. Cao, L. Z.; Lin, Z. B. Acta Pharmacol. Sin. 2003, 24, 321.
  34. Laemmli, U. K. Nature 1970, 227, 680. https://doi.org/10.1038/227680a0
  35. Davis, B. J. Ann. N. Y. Acad. Sci. 1964, 121, 404. https://doi.org/10.1111/j.1749-6632.1964.tb14213.x
  36. Rauchsen, P. Anal. Biochem.1979, 99, 474. https://doi.org/10.1016/S0003-2697(79)80035-4
  37. Kofron, J. L.; kuzmic, P.; Kischore, V.; Colon, B. E.; Rich, D. H. Biochemistry 1999, 30, 6127. https://doi.org/10.1021/bi00239a007
  38. Kim, S. J.; Lee, C. J. Biochem. Mol. Biol. 1996, 29, 519.
  39. Webb, M. R. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 4884. https://doi.org/10.1073/pnas.89.11.4884
  40. Lu, H. S.; Talent, J. M.; Gracy, R. W. J. Biol. Chem. 1981, 256, 785.
  41. Kim, S. H.; Park, E. J.; Yoon, S. S.; Choi, J. D. Bull. Korean Chem. Soc. 2003, 24, 1799. https://doi.org/10.5012/bkcs.2003.24.12.1799
  42. Butler, P. J.; Harris, J. I.; Hartley, J. I.; Lebeman, R. Biochem. J. 1969, 112, 679.
  43. Lisowska, E. Arch. Immunol. Ther. Exp.(Warsz) 1966, 14, 484.
  44. Damon, C. E.; Pettitt, B. S. Jr. Assoc. Off. Anal. Chem. 1980, 63, 476.
  45. Bradford, M. M. Biochem. J. 1976, 72, 248.
  46. Dubois, M.; Gilles, K. A.; Hamilton, J. K.; Rober, P. A.; Smith, F. Anal. Chem. 1956, 28, 350. https://doi.org/10.1021/ac60111a017
  47. Schreiber, S. L.; Crabtree, R. Immunol. Today 1992, 13, 136. https://doi.org/10.1016/0167-5699(92)90111-J
  48. Zenke, G.; Strittmatter, U.; Fuchs, S.; Quesniaux, V. F.; Brinkmann, V.; Schuler, W.; Zurini, M.; Enz, A.; Billich, A.; Sanglier, J. J.; Fehr, T. J. Immunol. 2001, 166, 7165. https://doi.org/10.4049/jimmunol.166.12.7165
  49. Wang, Y. Y.; Khoo, K. H.; Chen, S. T.; Lin, C. C.; Wong, C. H.; Lin, C. H. Bioorganic Med. Chem. 2002, 10, 1057 https://doi.org/10.1016/S0968-0896(01)00377-7
  50. Kino, K.; Yamashita, A.; YaNomaoka, K.; Watanabe, J.; Tanaka, S.; Ko, K.; Shimizu, K.; Tsunoo, H. J. Biol. Chem. 1988, 264, 472.
  51. Lakshimi, B.; Ajith, TA.; Sheena, N.; Gunapalan, N.; Hanardhanan, K. K. Teratog. Carcinog. Mutagen Suppl. 2003, 1, 85.

피인용 문헌

  1. A New Cyclophilin Inhibitor from Ganoderma lucidum: Purification and Characterization vol.35, pp.51, 2004, https://doi.org/10.1002/chin.200451168