Bulletin of the Korean Chemical Society

  • 제29권9호
  • /
  • Pages.1732-1736
  • /
  • 2008
  • /
  • 0253-2964(pISSN)
  • /
  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
권호 표지
DOI QR코드

DOI QR Code

Protection by Histidine Dipeptides against Acrolein-induced Neurofilament-L Aggregation

  • 발행 : 2008.09.30
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

The endogenous dipeptides, carnosine and related compounds, are the naturally occurring dipeptides with multiple neuroprotective properties. We have examined the protective effects of carnosine, homocarnosine and anserine on the aggregation of neurofilament-L (NF-L) induced by neurotoxin, acrolein. When NF-L was incubated with acrolein in the presence of carnosine, homocarnosine or anserine, protein aggregation was inhibited in a concentration-dependent manner. These compounds inhibited the formation of protein carbonyl compounds and dityrosine in acrolein-mediated NF-L aggregates. The aggregates of NF-L displayed thioflavin T reactivity, reminiscent of amyloid. This thioflavin T reactivity was inhibited by carnosine and related compounds. This effect was associated with decreased formation of oxidatively modified proteins. Our results suggested that carnosine and related compounds might have protective effects to brain proteins under pathophysiological conditions leading to degenerative damage such as neurodegenerative disorders.

키워드

참고문헌

  1. Uchida, K.; Kanematsu, M.; Morimitsu, Y.; Osawa, T.; Noguchi, N.; Niki, E. J. Biol. Chem. 1998, 273, 16058 https://doi.org/10.1074/jbc.273.26.16058
  2. Esterbauer, H.; Schaur, R. J.; Zollner, H. Free Radic. Biol. Med. 1991, 11, 81 https://doi.org/10.1016/0891-5849(91)90192-6
  3. Calingasan, N. Y.; Uchida, K.; Gibson, G. E. J. Neurochem. 1999, 72, 751 https://doi.org/10.1046/j.1471-4159.1999.0720751.x
  4. Kohen, R.; Yamamoto, Y.; Cundy, K. C.; Ames, B. N. Proc. Natl. Acad. Sci. USA 1988, 85, 3175 https://doi.org/10.1073/pnas.85.9.3175
  5. O'Dowd, J. J.; Robins, D. J.; Miller, D. J. Biochem. Biophys. Acta 1988, 967, 241 https://doi.org/10.1016/0304-4165(88)90015-3
  6. Bonfanti, L.; Peretto, P.; De Marchis, S.; Fasolo, A. Prog. Neurobiol. 1999, 59, 333 https://doi.org/10.1016/S0301-0082(99)00010-6
  7. Trombley, P. Q.; Horning, M. S.; Blakemor, L. J. Biochemistry (Mosc) 2000, 65, 807
  8. Boldyrev, A.; Bulygina, E.; Leinsoo, T.; Petrushanko, J.; Tsubone, S.; Abe, H. Comp. Biochem. Physiol. B. Biochem. Mol. Biol. 2004, 137, 81 https://doi.org/10.1016/j.cbpc.2003.10.008
  9. Boldyrev, A.; Song, R.; Lawrence, D.; Carpenter, D. O. Neuroscience 1999, 94, 571 https://doi.org/10.1016/S0306-4522(99)00273-0
  10. Hoffmann, P. N.; Griffin, J. W.; Price, D. L. J. Cell. Biol. 1984, 99, 705 https://doi.org/10.1083/jcb.99.2.705
  11. Lee, M. K.; Cleveland, D. W. Ann. Rev. Neurosci. 1996, 19, 187 https://doi.org/10.1146/annurev.ne.19.030196.001155
  12. Shepherd, C. E.; MoCann, H.; Thiel, E.; Halliday, G. M. Neurol. Dis. 2002, 9, 249 https://doi.org/10.1006/nbdi.2001.0469
  13. Galloway, P. G.; Mulvihill, P.; Perry, G. Am. J. Pathol. 1992, 140, 809
  14. Collard, J. F.; Cote, F.; Julien, J. P. Nature 1995, 375, 61 https://doi.org/10.1038/375061a0
  15. Grant, P.; Pant, H. C. J. Neurocytol. 2000, 29, 843 https://doi.org/10.1023/A:1010999509251
  16. Hirano, A.; Donnenfeld, H.; Sasaki, S.; Nakano, I. J. Neuropathol. Exp. Neurol. 1984, 43, 461 https://doi.org/10.1097/00005072-198409000-00001
  17. Smith, M. A.; Rudnicka-Nawrot, M.; Richey, P. L.; Praprotnik, D.; Mulvihill, P.; Miller, C. A.; Sayre, L. M.; Perry, G. J. Neurochem. 1995, 64, 2660 https://doi.org/10.1046/j.1471-4159.1995.64062660.x
  18. Pamplona, R.; Dalfo, E.; Ayala, V.; Bellmunt, M. J.; Prat, J.; Ferrer, I.; Portero-Otin, M. J. Biol. Chem. 2005, 280, 21522 https://doi.org/10.1074/jbc.M502255200
  19. Aksenov, M. Y.; Aksenova, M. V.; Butterfield, D. A.; Geddes, J. W.; Markesbery, W. R. Neurosience 2001, 103, 373 https://doi.org/10.1016/S0306-4522(00)00580-7
  20. Kang, J. H. Bull. Korean Chem. Soc. 2007, 28, 77 https://doi.org/10.5012/bkcs.2007.28.1.077
  21. Kang, J. H. Bull. Korean Chem. Soc. 2007, 28, 1881 https://doi.org/10.5012/bkcs.2007.28.10.1881
  22. Kang, J. H. Bull. Korean Chem. Soc. 2006, 27, 663 https://doi.org/10.5012/bkcs.2006.27.5.663
  23. Laemmli, U. K. Nature 1970, 227, 680 https://doi.org/10.1038/227680a0
  24. Reznick, A.; Packer, L. Methods Enzymol. 1994, 233, 357 https://doi.org/10.1016/S0076-6879(94)33041-7
  25. Lou, J.; Shi, R. Neurochem. Int. 2004, 44, 475 https://doi.org/10.1016/j.neuint.2003.09.006
  26. Jenner, P. Pathol. Biol. (Paris) 1996, 44, 57
  27. Tabner, B. J.; Turnbull, S.; El-Agnaf, O. M.; Allsop, D. Free Radic. Biol. Med. 2002, 32, 1076 https://doi.org/10.1016/S0891-5849(02)00801-8
  28. Levine, R. L.; Williams, J. A.; Stadtman, E. R.; Shacter, E. Methods Enzymol. 1994, 233, 346 https://doi.org/10.1016/S0076-6879(94)33040-9
  29. Brownson, C.; Hipkiss, A. R. Free Radic. Biol. Med. 2000, 28, 1564 https://doi.org/10.1016/S0891-5849(00)00270-7
  30. Berlett, B. S.; Stadtman, E. R. J. Biol. Chem. 1997, 272, 20313 https://doi.org/10.1074/jbc.272.33.20313
  31. Hipkiss, A. R.; Michaelis, J.; Syrris, P. FEBS. Lett. 1995, 371, 81 https://doi.org/10.1016/0014-5793(95)00849-5
  32. Carpenter, D. A.; Ip, W. J. Cell. Sci. 1996, 109, 2493
  33. Naiki, H.; Higuchi, K.; Hosokawa, M.; Takeda, T. Anal. Biochem. 1989, 177, 244 https://doi.org/10.1016/0003-2697(89)90046-8
  34. LeVine, H. 3rd Protein Sci. 1993, 2, 404 https://doi.org/10.1002/pro.5560020312
  35. Aldini, G.; Granata, P.; Carini, M. J. Mass Spectrom. 2002, 37, 1219 https://doi.org/10.1002/jms.381
  36. Carini, M.; Aldini, G.; Beretta, G.; Arlandini, E.; Facino, R. M. J. Mass Spectrom. 2003, 38, 996 https://doi.org/10.1002/jms.517
  37. Boldyrev, A.; Koudinov, A.; Berezov, T.; Carpenter, D. O. J. Alzheimers Dis. 2004, 6, 633
  38. Balion, C. M.; Benson, C.; Raina, P. S.; Papaioannou, A.; Patterson, C.; Ismaila, A. S. BMC Neurol. 2007, 7, 38 https://doi.org/10.1186/1471-2377-7-38

피인용 문헌

  1. Acrolein scavengers: Reactivity, mechanism and impact on health vol.55, pp.9, 2011, https://doi.org/10.1002/mnfr.201100149
  2. The effect of antioxidants on in vivo and in vitro methemoglobin formation in erythrocytes of patients with Parkinson’s disease vol.10, pp.3, 2016, https://doi.org/10.1134/S1990750816030124