Biochemistry (Moscow)

, Volume 76, Issue 3, pp 332–338 | Cite as

Amino acid sequences of two immune-dominant epitopes of recoverin are involved in Ca2+/recoverin-dependent inhibition of phosphorylation of rhodopsin

  • I. I. SeninEmail author
  • N. K. Tikhomirova
  • V. A. Churumova
  • I. I. Grigoriev
  • T. A. Kolpakova
  • D. V. Zinchenko
  • P. P. Philippov
  • E. Yu. Zernii


Antibodies AB60–72 and AB80–92 against two immune-dominant epitopes of photoreceptor Ca2+-binding protein recoverin, 60-DPKAYAQHVFRSF-72 and 80-LDFKEYVIALHMT-92, which can be exposed in a Ca2+-dependent manner, were obtained. The presence of AB60–72 or AB80–92 results in a slight increase in Ca2+-affinity of recoverin and does not affect significantly a Ca2+-myristoyl switch mechanism of the protein. However in the presence of AB60–72 or AB80–92 recoverin loses its ability to interact with rhodopsin kinase and consequently to perform a function of Ca2+-sensitive inhibitor of rhodopsin phosphorylation in photoreceptor cells.

Key words

Ca2+-dependent antibodies Ca2+-myristoyl switch cancer associated retinopathy recoverin 


AB60–72 and AB80–92

antibodies against peptide fragments of recoverin 60-DPKAYAQHVFRSF-72 and 80-LDFKEYVIALHMT-92, respectively


cancer associated retinopathy




phenylmethylsulfonyl fluoride


rod outer segment


trichloroacetic acid


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  1. 1.
    Dizhoor, A. M., Ray, S., Kumar, S., Niemi, G., Spencer, M., Brolley, D., Walsh, K. A., Philipov, P. P., Hurley, J. B., and Stryer, L. (1991) Science, 251, 915–918.PubMedCrossRefGoogle Scholar
  2. 2.
    Ames, J. B., Ishima, R., Tanaka, T., Gordon, J. I., Stryer, L., and Ikura, M. (1997) Nature, 389, 198–202.PubMedCrossRefGoogle Scholar
  3. 3.
    Dizhoor, A. M., Ericsson, L. H., Johnson, R. S., Kumar, S., Olshevskaya, E., Zozulya, S., Neubert, T. A., Stryer, L., Hurley, J. B., and Walsh, K. A. (1992) J. Biol. Chem., 267, 16033–16036.PubMedGoogle Scholar
  4. 4.
    Tanaka, T., Ames, J. B., Harvey, T. S., Stryer, L., and Ikura, M. (1995) Nature, 376, 444–447.PubMedCrossRefGoogle Scholar
  5. 5.
    Zozulya, S., and Stryer, L. (1992) Proc. Natl. Acad. Sci. USA, 89, 11569–11573.PubMedCrossRefGoogle Scholar
  6. 6.
    Ames, J. B., Levay, K., Wingard, J. N., Lusin, J. D., and Slepak, V. Z. (2006) J. Biol. Chem., 281, 37237–37245.PubMedCrossRefGoogle Scholar
  7. 7.
    Kawamura, S. (1993) Nature, 362, 855–857.PubMedCrossRefGoogle Scholar
  8. 8.
    Senin, I. I., Zargarov, A. A., Alekseev, A. M., Gorodovikova, E. N., Lipkin, V. M., and Philippov, P. P. (1995) FEBS Lett., 376, 87–90.PubMedCrossRefGoogle Scholar
  9. 9.
    Kuhn, H., and Wilden, U. (1987) J. Recept. Res., 7, 283–298.PubMedGoogle Scholar
  10. 10.
    Makino, C. L., Dodd, R. L., Chen, J., Burns, M. E., Roca, A., Simon, M. I., and Baylor, D. A. (2004) J. Gen. Physiol., 123, 729–741.PubMedCrossRefGoogle Scholar
  11. 11.
    Kennedy, M. J., Dunn, F. A., and Hurley, J. B. (2004) Neuron, 41, 915–928.PubMedCrossRefGoogle Scholar
  12. 12.
    Polans, A. S., Buczylko, J., Crabb, J., and Palczewski, K. (1991) J. Cell. Biol., 112, 981–989.PubMedCrossRefGoogle Scholar
  13. 13.
    Polans, A. S., Witkowska, D., Haley, T. L., Amundson, D., Baizer, L., and Adamus, G. (1995) Proc. Natl. Acad. Sci. USA, 92, 9176–9180.PubMedCrossRefGoogle Scholar
  14. 14.
    Bazhin, A. V., Schadendorf, D., Willner, N., De Smet, C., Heinzelmann, A., Tikhomirova, N. K., Umansky, U., Philippov, P. P., and Eichmuller, S. B. (2007) Int. J. Cancer, 120, 1268–1276.PubMedCrossRefGoogle Scholar
  15. 15.
    Adamus, G. (2009) Autoimmun. Rev., 8, 410–414.PubMedCrossRefGoogle Scholar
  16. 16.
    Kobayashi, M., Ikezoe, T., Uemura, Y., Ueno, H., and Taguchi, H. (2007) Lung Cancer, 57, 399–403.PubMedCrossRefGoogle Scholar
  17. 17.
    Ahn, J., Kim, J., Kim, J., Yu, Y., Park, K., Kim, D., and Kim, K.-W. (2008) Invest. Ophthalmol. Vis. Sci., 49, 4753.PubMedCrossRefGoogle Scholar
  18. 18.
    Adamus, G., Guy, J., Schmied, J. L., Arendt, A., and Hargrave, P. A. (1993) Invest. Ophthalmol. Vis. Sci., 34, 2626.PubMedGoogle Scholar
  19. 19.
    Adamus, G., and Amundson, D. (1996) J. Neurosci. Res., 45, 863–872.PubMedCrossRefGoogle Scholar
  20. 20.
    Tikhomirova, N. K., Goncharskaya, M. A., and Senin, I. I. (2004) Biochemistry (Moscow), 69, 1360–1364.PubMedGoogle Scholar
  21. 21.
    Kuhn, H., and Dreyer, W. J. (1972) FEBS Lett., 20, 1–6.PubMedCrossRefGoogle Scholar
  22. 22.
    Shichi, H., and Somers, R. L. (1978) J. Biol. Chem., 253, 7040–7046.PubMedGoogle Scholar
  23. 23.
    Senin, I. I., Fischer, T., Komolov, K. E., Zinchenko, D. V., Philippov, P. P., and Koch, K.-W. (2002) J. Biol. Chem., 277, 50365–50372.PubMedCrossRefGoogle Scholar
  24. 24.
    Senin, I. I., Dean, K. R., Zargarov, A. A., Akhtar, M., and Philippov, P. P. (1997) Biochem. J., 321, 551–555.PubMedGoogle Scholar
  25. 25.
    Tikhomirova, N. K. (1990) Biochem. Int., 22, 31–36.PubMedCrossRefGoogle Scholar
  26. 26.
    Ames, J. B., Porumb, T., Tanaka, T., Ikura, M., and Stryer, L. (1995) J. Biol. Chem., 270, 4526–4533.PubMedCrossRefGoogle Scholar
  27. 27.
    Gorodovikova, E. N., Senin, I. I., and Philippov, P. P. (1994) FEBS Lett., 353, 171–172.PubMedCrossRefGoogle Scholar
  28. 28.
    Sanada, K., Shimizu, F., Kameyama, K., Haga, K., Haga, T., and Fukada, Y. (1996) FEBS Lett., 384, 227–230.PubMedCrossRefGoogle Scholar
  29. 29.
    Towbin, H., Staehelin, T., and Gordon, J. (1979) Proc. Natl. Acad. Sci. USA, 76, 4350–4354.PubMedCrossRefGoogle Scholar
  30. 30.
    Laemmli, U. K. (1979) Nature (London), 227, 680–685.CrossRefGoogle Scholar
  31. 31.
    Bradford, M. (1976) Anal. Biochem., 72, 248–254.PubMedCrossRefGoogle Scholar
  32. 32.
    Ohguro, H., and Nakazawa, M. (2002) Adv. Exp. Med. Biol., 514, 109–124.PubMedGoogle Scholar
  33. 33.
    Senin, I. I., Bosch, L., Ramon, E., Zernii, E. Y., Manyosa, J., Philippov, P. P., and Garriga, P. (2006) Biochem. Biophys. Res. Commun., 349, 345–352.PubMedCrossRefGoogle Scholar

Copyright information

© Pleiades Publishing, Ltd. 2011

Authors and Affiliations

  • I. I. Senin
    • 1
    Email author
  • N. K. Tikhomirova
    • 1
  • V. A. Churumova
    • 1
  • I. I. Grigoriev
    • 1
  • T. A. Kolpakova
    • 1
  • D. V. Zinchenko
    • 2
  • P. P. Philippov
    • 1
  • E. Yu. Zernii
    • 1
  1. 1.Department of Cell Signaling, Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia
  2. 2.Laboratory of Protein ChemistryPushchino Branch of the Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryPushchino, Moscow RegionRussia

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