Journal of Thermal Analysis and Calorimetry

, Volume 95, Issue 3, pp 709–712 | Cite as

Effect of phalloidin on the skeletal muscle ADP-actin filaments

  • Réka Dudás
  • Tünde Kupi
  • Andrea Vig
  • J. Orbán
  • D. LőrinczyEmail author
Biochemical and Pharmaceutical Aspects


The effect of phalloidin on the thermal stability of skeletal actin filaments polymerized from ADP-binding monomers was investigated with the method of differential scanning calorimetry. Phalloidin shifted the melting temperature of the ADP-F-actin from 59.1±1.0 to 80.0±1.2°C. The stabilizing effect of phalloidin propagated cooperatively along the filament. The cooperativity factor according to the applied model was 1.07±0.11. With these measurements it was possible to demonstrate that the binding of phalloidin has lower influence on the adjacent protomers in ADP- (k=1) than in ATP-actin filaments (k=3).


ADP-actin filament calorimetry phalloidin stability thermodynamics 


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  1. 1.
    P. Cossart, Curr. Opin. Cell Biol., 7 (1995) 94.CrossRefGoogle Scholar
  2. 2.
    C. Lamaze, L. M. Fujimoto, H. L. Yin and S. L. Schmid, J. Biol. Chem., 272 (1997) 20332.CrossRefGoogle Scholar
  3. 3.
    J. E. Estes, L. A. Selden, H. J. Kinosian and L. C. Gershman, J. Muscle Res. Cell Motil., 13 (1992) 272.CrossRefGoogle Scholar
  4. 4.
    G. Hild, M. Nyitrai, J. Belágyi and B. Somogyi, Biophys. J., 75 (1998) 3015.CrossRefGoogle Scholar
  5. 5.
    G. Hild, M. Nyitrai and B. Somogyi, Eur. J. Biochem., 269 (2002) 842.CrossRefGoogle Scholar
  6. 6.
    M. Nyitrai, G. Hild, J. Belágyi and B. Somogyi, Biophys. J., 73 (1997) 2023.CrossRefGoogle Scholar
  7. 7.
    M. Nyitrai, G. Hild, J. Belágyi and B. Somogyi, J. Biol. Chem., 274 (1999) 12996.CrossRefGoogle Scholar
  8. 8.
    M. Nyitrai, G. Hild, Z. Lakos and B. Somogyi, Biophys. J., 74 (1998) 2474.CrossRefGoogle Scholar
  9. 9.
    M. F. Carlier, Curr. Opin. Cell. Biol., 3 (1991) 12.CrossRefGoogle Scholar
  10. 10.
    B. Gaszner, M. Nyitrai, N. Hartvig, T. Kőszegi, B. Somogyi and J. Belágyi, Biochemistry, 38 (1999) 12885.CrossRefGoogle Scholar
  11. 11.
    M. Nyitrai, G. Hild, N. Hartvig, J. Belágyi and B. Somogyi, J. Biol. Chem., 275 (2000) 41143.CrossRefGoogle Scholar
  12. 12.
    J. Orbán, D. Lőrinczy, M. Nyitrai and G. Hild, Biochem. Biophys. Res. Commun., 368 (2008) 696.CrossRefGoogle Scholar
  13. 13.
    J. Orbán, K. Pozsonyi, K. Szarka, S. Barkó, E. Bódis and D. Lőrinczy, J. Therm. Anal. Cal., 84 (2006) 619.CrossRefGoogle Scholar
  14. 14.
    T. D. Pollard, I. Goldberg and W. H. Schwarz, J. Biol. Chem., 267 (1992) 20339.Google Scholar
  15. 15.
    I. Löw, P. Dancker and T. Wieland, FEBS Lett., 65 (1976) 358.Google Scholar
  16. 16.
    T. Wieland, Int. J. Pept. Protein Res., 22 (1983) 257.Google Scholar
  17. 17.
    H. Faulstich, A. J. Schafer and M. Weckauf, Hoppe Seylers Z. Physiol. Chem., 358 (1977) 181.Google Scholar
  18. 18.
    B. Visegrády, D. Lőrinczy, G. Hild, B. Somogyi and M. Nyitrai, FEBS Lett., 565 (2004) 163.CrossRefGoogle Scholar
  19. 19.
    B. Visegrády, D. Lőrinczy, G. Hild, B. Somogyi and M. Nyitrai, FEBS Lett., 579 (2005) 6.CrossRefGoogle Scholar
  20. 20.
    M. O. Steinmetz, K. N. Goldie and U. Aebi, J. Cell Biol., 138 (1997) 559.CrossRefGoogle Scholar
  21. 21.
    J. A. Barden, M. Miki, B. D. Hambly and C. G. Dos Remedios, Eur. J. Biochem., 162 (1987) 583.CrossRefGoogle Scholar
  22. 22.
    E. M. De La Cruz and T. D. Pollard, Biochemistry, 35 (1996) 14054.CrossRefGoogle Scholar
  23. 23.
    H. Faulstich, S. Zobeley, D. Heintz and G. Drewes, FEBS Lett., 318 (1993) 218.CrossRefGoogle Scholar
  24. 24.
    R. A. Milligan, M. Whittaker and D. Safer, Nature, 348 (1990) 217.CrossRefGoogle Scholar
  25. 25.
    H. M. Warrick, R. M. Simmons, J. T. Finer, T. Q. Uyeda, S. Chu and J. A. Spudich, Methods Cell Biol., 39 (1993) 1.CrossRefGoogle Scholar
  26. 26.
    J. Orbán, D. Lőrinczy, G. Hild and M. Nyitrai, Biochemistry, 47 (2008) 4530.CrossRefGoogle Scholar
  27. 27.
    N. L. Golitsina, A. A. Bobkov, I. V. Dedova, D. A. Pavlov, O. P. Nikolaeva, V. N. Orlov and D. I. Levitsky, J. Muscle Res. Cell. Motil., 17 (1996) 475.CrossRefGoogle Scholar
  28. 28.
    S. Halasi, G. Papp, B. Bugyi, S. Barkó, J. Orbán, Z. Ujfalusi and B. Visegrády, Thermochim. Acta, 445 (2006) 185.CrossRefGoogle Scholar
  29. 29.
    N. Hartvig, B. Gaszner, M. Kiss, D. Lőrinczy and J. Belágyi, J. Biochem. Biophys. Methods, 53 (2002) 67.CrossRefGoogle Scholar
  30. 30.
    R. Kardos, A. Vig, J. Orbán, G. Hild, M. Nyitrai and D. Lőrinczy, Thermochim. Acta, 463 (2007) 77.CrossRefGoogle Scholar
  31. 31.
    D. I. Levitsky, O. P. Nikolaeva, V. N. Orlov, D. A. Pavlov, M. A. Ponomarev and E. V. Rostkova, Biochemistry (Mosc.), 63 (1998) 322.Google Scholar
  32. 32.
    D. I. Levitsky, E. V. Rostkova, V. N. Orlov, O. P. Nikolaeva, L. N. Moiseeva, M. V. Teplova and N. B. Gusev, Eur. J. Biochem., 267 (2000) 1869.CrossRefGoogle Scholar
  33. 33.
    D. Lőrinczy and J. Belágyi, Thermochim. Acta, 259 (1995) 153.CrossRefGoogle Scholar
  34. 34.
    J. Orbán, S. Halasi, G. Papp, S. Barkó and B. Bugyi, J. Therm. Anal. Cal., 82 (2005) 287.CrossRefGoogle Scholar
  35. 35.
    G. Papp, B. Bugyi, Z. Ujfalusi, S. Halasi and J. Orbán, J. Therm. Anal. Cal., 82 (2005) 281.CrossRefGoogle Scholar
  36. 36.
    D. Lőrinczy and J. Belágyi, J. Therm. Anal. Cal., 90 (2007) 611.CrossRefGoogle Scholar
  37. 37.
    D. Lőrinczy, Zs. Vértes, F. Könczöl and J. Belágyi, J. Therm. Anal. Cal., 95 (2009) 713.CrossRefGoogle Scholar
  38. 38.
    A. Vig, R. Dudás, T. Kupi, J. Orbán, G. Hild, D. Lőrinczy and M. Nyitrai, J. Therm. Anal. Cal., 95 (2009) 721.CrossRefGoogle Scholar
  39. 39.
    G. Feuer, F. Molnár, E. Pettkó and F. B. Straub, Hung. Acta Physiol., 1 (1948) 150.Google Scholar
  40. 40.
    J. A. Spudich and S. Watt, J. Biol. Chem., 246 (1971) 4866.Google Scholar
  41. 41.
    T. W. HoukJr. and K. Ue, Anal. Biochem., 62 (1974) 66.CrossRefGoogle Scholar
  42. 42.
    H. Strzelecka-Golaszewska, J. Moraczewska, S. Y. Khaitlina and M. Mossakowska, Eur. J. Biochem., 211 (1993) 731.CrossRefGoogle Scholar
  43. 43.
    A. Cooper, M. A. Nutley and A. Wadood, Protein-Ligand Interactions: Hydrodynamics and Calorimetry, S. E. Harding and B. Z. Chowdhury, Eds, Oxford University Press, Oxford 2001, p. 287.Google Scholar
  44. 44.
    D. Lőrinczy, F. Könczöl, B. Gaszner and J. Belágyi, Thermochim. Acta, 322 (1998) 95.CrossRefGoogle Scholar

Copyright information

© Akadémiai Kiadó, Budapest, Hungary 2009

Authors and Affiliations

  • Réka Dudás
    • 1
  • Tünde Kupi
    • 1
  • Andrea Vig
    • 1
  • J. Orbán
    • 1
  • D. Lőrinczy
    • 1
    Email author
  1. 1.Department of BiophysicsUniversity of Pécs, Medical SchoolPécsHungary

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