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Russian Journal of Bioorganic Chemistry

, Volume 44, Issue 4, pp 416–423 | Cite as

A New Iq-Peptide of the Kunitz Type from the Heteractis magnifica Sea Anemone Exhibits Neuroprotective Activity in a Model of Alzheimer’s Disease

  • A. N. Kvetkina
  • E. V. Leychenko
  • E. A. Yurchenko
  • E. A. Pislyagin
  • S. Peigneur
  • Y. Tytgat
  • M. P. Isaeva
  • D. L. Aminin
  • E. P. Kozlovskaya
Article

Abstract

The HMIQ3c1 recombinant peptide (6434 Da), the Kunitz-type protease inhibitor, which belonged to the new group of the IQ-peptides from the Heteractis magnifica sea anemone was prepared. The inhibitory constant of trypsin by this peptide proved to be 5.0 × 10–8 M. rHMIQ3c1 was shown to have no interaction with eight isoforms of Kv1 channels. This peptide exhibited neuroprotective activity in a concentration of 10 μM, and the peptide increased the viability of cells of the Neuro2a murine neuroblastoma by 39.4 ± 6.6% in the presence of β-amyloid. However, the peptide did not influence the viability of the cells during their incubation with 6-hydroxydofamine.

Keywords

sea anemone Kunitz-type protease inhibitors neuroprotective activity 

Abbreviation

AMPAR

the receptor that binds α-amino-3-hydrpxy-5-methyl-4-isoxazolepropionic acid

BPTI

bovine pancreatic trypsin inhibitor

Kv

potential-dependent K+-channel

NMDAR

receptor that binds N-метил-D-aspartate

TNFα

tumor necrosis factor alpha

TRPV1

Transient Receptor Potential cation channel subfamily V member 1

LPS

lipopolysaccharide

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References

  1. 1.
    Rosenthal, N., Nat. Med., 2014, vol. 20, pp. 857–869.CrossRefPubMedGoogle Scholar
  2. 2.
    Zykova, T.A., Vinokurov, L.M., Markova, L.F., Kozlovskaya, E.P., and Elyakov, G.B., Russ. J. Bioorg. Chem., 1985, vol. 11, pp. 293–301.Google Scholar
  3. 3.
    Gladkikh, I., Monastyrnaya, M., Leychenko, E., Zelepuga, E., Chausova, V., Isaeva, M., Anastyuk, S., Andreev, Y., Peigneur, S., Tytgat, J., and Kozlovkaya, E., Mar. Drugs, 2012, vol. 10, pp. 1545–1565.CrossRefPubMedPubMedCentralGoogle Scholar
  4. 4.
    Yang, W., Feng, J., Wang, B., Cao, Z., Li, W., Wu, Y., and Chen, Z., J. Biochem. Mol. Toxicol., 2014, vol. 28, pp. 76–83.CrossRefPubMedGoogle Scholar
  5. 5.
    Minagawa, S., Sugiyam, M., Ishida, M., Nagashima, Y., and Shiomi, K., Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 2008, vol. 150, pp. 240–245.Google Scholar
  6. 6.
    Minagawa, S., Ishida, M., Shimakura, K., Nagashima, Y., and Shiomi, K., Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol., 1997, vol. 118, pp. 381–386.Google Scholar
  7. 7.
    Delfin, J., Martinez, I., Antuch, W., Morera, V., Gonzalez, Y., Rodriguez, R., Marquez, M., Saroyan, A., Larionova, N., Diaz, J., Padron, G., and Chavez, M., Toxicon, 1996, vol. 34, pp. 1367–1376.CrossRefPubMedGoogle Scholar
  8. 8.
    Alonso-del-Rivero, M., Trejo, S.A., Reytor, M.L., Rodriguez-de-la-Vega, M., Delfin, J., Diaz, J., González-González, Y., Canals, F., Chavez, M.A., and Aviles, F.X., J. Biol. Chem., 2012, vol. 287, pp. 15427–15438.CrossRefPubMedPubMedCentralGoogle Scholar
  9. 9.
    Schweitz, H., Bruhn, T., Guillemare, E., Moinier, D., Lancelin, J.M., Beress, L., and Lazdunski, M., J. Biol. Chem., 1995, vol. 270, pp. 25121–25126.CrossRefPubMedGoogle Scholar
  10. 10.
    García-Fernández, R., Peigneur, S., Pons, T., Alvarez, C., González, L., Chávez, M.A., and Tytgat, J., Toxins, 2016, vol. 8, no. 110, pp. 2–17. doi 10.3390/toxins8040110Google Scholar
  11. 11.
    Bayrhuber, M., Vijayan, V., Ferber, M., Graf, R., Korukottu, J., Imperial, J., Garrett, J.E., Olivera, B.M., Terlau, H., Zweckstetter, M., and Becker, S., J. Biol. Chem., 2005, vol. 280, pp. 23766–23770.CrossRefPubMedGoogle Scholar
  12. 12.
    DePoli, P., Bacon-Baguley, T., Kendra-Franczak, S., Cederholm, M.T., and Walz, D.A., Blood, 1989, vol. 73, pp. 976–982.PubMedGoogle Scholar
  13. 13.
    Honma, T., Kawahata, S., Ishida, M., Nagai, H., Nagashima, Y., and Shiomi, K., Peptides, 2008, vol. 29, pp. 536–544.CrossRefPubMedGoogle Scholar
  14. 14.
    Andreev, Y.A., Kozlov, S.A., Koshelev, S.G., Ivanova, E.A., Monastyrnaya, M.M., Kozlovskaya, E.P., and Grishin, E.V., J. Biol. Chem., 2008, vol. 283, pp. 23914–23921.CrossRefPubMedPubMedCentralGoogle Scholar
  15. 15.
    Sokotun, I.N., Leichenko, E.V., Vakorina, T.I., Es’kov, A.A., Il’ina, A.P., Monastyrnaia, M.M., and Kozlovskaia, E.P., Russ. J. Bioorg. Chem., 2007, vol. 33, pp. 415–422.CrossRefGoogle Scholar
  16. 16.
    Sintsova, O.V., Pislyagin, E.A., Gladkikh, I.N., Monastyrnaya, M.M., Menchinskaya, E.S., Leychenko, E.V., Aminin, D.L., and Kozlovskaya, E.P., Russ. J. Bioorg. Chem., 2017, vol. 43, pp. 105–112.CrossRefGoogle Scholar
  17. 17.
    Morjen, M., Kallech-Ziri, O., Bazaa, A., Othman, H., Mabrouk, K., Zouari-Kessentini, R., Sanz, L., Calvete, J.J., Srairi-Abid, N., El Ayeb, M., Luis, J., and Marrakchi, N., Matrix Biol., 2013, vol. 32, pp. 52–62.CrossRefPubMedGoogle Scholar
  18. 18.
    Isaeva, M.P., Chausova, V.E., Zelepuga, E.A., Guzev, K.V., Tabakmakher, V.M., Monastyrnaya, M.M., and Kozlovskaya, E.P., Peptides, 2012, vol. 34, pp. 88–97.CrossRefPubMedGoogle Scholar
  19. 19.
    Sintsova, O.V., Monastyrnaya, M.M., Pislyagin, E.A., Menchinskaya, E.S., Leychenko, E.V., Aminin, D.L., and Kozlovskaya, E.P., Russ. J. Bioorg. Chem., 2015, vol. 41, pp. 590–596.CrossRefGoogle Scholar
  20. 20.
    Gladkikh, I., Monastyrnaya, M., Zelepuga, E., Sintsova, O., Tabakmakher, V., Gnedenko, O., Ivanov, A., Hua, K.-F., and Kozlovskaya, E., Mar. Drugs, 2015, vol. 13, pp. 6038–6063.CrossRefPubMedPubMedCentralGoogle Scholar
  21. 21.
    Kozlov, S.A., Andreev, Y.A., Murashev, A.N., Skobtsov, D.I., D’yachenko, I.A., and Grishin, E.V., Russ. J. Bioorg. Chem., 2009, vol. 35, pp. 711–719.CrossRefGoogle Scholar
  22. 22.
    Zelepuga, E.A., Tabakmakher, V.M., Chausova, V.E., Monastyrnaya, M.M., Isaeva, M.P., and Kozlovskaya, E.P., Russ. J. Bioorg. Chem., 2012, vol. 38, pp. 159–170.CrossRefGoogle Scholar
  23. 23.
    Monastyrnaya, M., Peigneur, S., Zelepuga, E., Sintsova, O., Gladkikh, I., Leychenko, E., Isaeva, M., Tytgat, J., and Kozlovskaya, E., Mar. Drugs, 2016, vol. 14, no. 229. doi 10.3390/md14120229Google Scholar
  24. 24.
    Tabakmakher, V.M., Sintsova, O.V., Krivoshapko, O.N., Zelepuga, E.A., Monastyrnaya, M.M., and Kozlovskaya, E.P., Dokl. Biochem. Biophys., 2015, vol. 461, pp. 80–83.CrossRefPubMedGoogle Scholar
  25. 25.
    Metrione, R.M., Schweitz, H., and Walsh, K.A., FEBS Lett., 1987, vol. 218, pp. 59–62.CrossRefPubMedGoogle Scholar
  26. 26.
    Gendeh, G.S., Young, L.C., De Medeiros, C.L.C., Jeyaseelan, K., Harvey, A.L., and Chung, M.C.M., Biochemistry, 1997, vol. 36, pp. 11461–11471.CrossRefGoogle Scholar
  27. 27.
    Wang, Y., Yap, L.L., Chua, K.L., and Khoo, H.E., Toxicon, 2008, vol. 51, pp. 1374–1382.CrossRefPubMedGoogle Scholar
  28. 28.
    Sintsova, O., Gladkikh, I., Chausova, V., Monastyrnaya, M., Anastyuk, S., Chernikov, O., Yurchenko, E., Aminin, D., Isaeva, M., Leychenko, E., and Kozlovskaya, E., J. Proteom., 2018, vol. 173, pp. 12–21.CrossRefGoogle Scholar
  29. 29.
    Anderluh, G. and Macek, P., Toxicon, 2002, vol. 40, pp. 111–124.CrossRefPubMedGoogle Scholar
  30. 30.
    Vincent, J.-P. and Lazdunski, M., Biochemistry, 1972, vol. 11, pp. 2967–2977.CrossRefPubMedGoogle Scholar
  31. 31.
    Snyder, E.M., Nong, Y., Almeida, C.G., Paul, S., Moran, T., Choi, E.Y., Nairn, A.C., Salter, M.W., Lombroso, P.J., Gouras, G.K., and Greengard, P., Nat. Neurosci., 2005, vol. 8, pp. 1051–1058.CrossRefPubMedGoogle Scholar
  32. 32.
    Shankar, G.M., Bloodgood, B.L., Townsend, M., Walsh, D.M., Selkoe, D.J., and Sabatini, B.L., J. Neurosci., 2007, vol. 27, pp. 2866–2875.CrossRefPubMedGoogle Scholar
  33. 33.
    Shankar, G.M. and Walsh, D.M., Mol. Neurodegener., 2009, vol. 4, no. 48.Google Scholar
  34. 34.
    Yamazaki, M., Chiba, K., and Satoh, K., J. Health Sci, 2008, vol. 54, pp. 638–644. doi.org/doi 10.1186/1750-1326-4-48CrossRefGoogle Scholar
  35. 35.
    Soto-Otero, R., Méndez-Álvarez, E., Hermida-Ameijeiras, A., Munoz-Patino, A.M., and Labandeira-Garcia, J.L., J. Neurochem., 2000, vol. 74, pp. 1605–1612.CrossRefPubMedGoogle Scholar
  36. 36.
    Small, G., Liston, E., and Jarvik, L., West. J. Med., 1981, vol. 135, pp. 469–470.PubMedPubMedCentralGoogle Scholar
  37. 37.
    Kreft, A., Martone, R., and Porte, A., J. Med. Chem., 2009, vol. 52, pp. 6169–6188.CrossRefPubMedGoogle Scholar
  38. 38.
    Georgievska, B., Sandin, J., Doherty, J., Mortberg, A., Neelissen, J., Andersson, A., Gruber, S., Nilsson, Y., Schott, P., Arvidsson, P.I., Hellberg, S., Osswald, G., Berg, S., Falting, J., and Bhat, R.V., J. Neurochem., 2013, vol. 125, pp. 446–456.CrossRefPubMedGoogle Scholar
  39. 39.
  40. 40.
    Tamura, K., Stecher, G., Peterson, D., Filipski, A., and Kumar, S., Mol. Biol. Evol., 2013, vol. 30, pp. 2725–2729.CrossRefPubMedPubMedCentralGoogle Scholar
  41. 41.
    Felsenstein, J., Evolution, 1985, vol. 39, pp. 783–791.CrossRefPubMedGoogle Scholar
  42. 42.
    Andreev, Y.A., Kozlov, S.A., Vassilevski, A.A., and Grishin, E.V., Anal. Biochem., 2010, vol. 407, pp. 144–146.CrossRefPubMedGoogle Scholar
  43. 43.
    Dixon, M., Biochem. J., 1953, vol. 55, pp. 170–171.CrossRefPubMedPubMedCentralGoogle Scholar
  44. 44.
    Castaneda, O., Sotolongo, V., Amor, A.M., Stocklin, R., Anderson, A.J., Harvey, A.L., Engstrom, A., Wernstedt, C., and Karlsson, E., Toxicon, 1995, vol. 33, pp. 603–613.CrossRefPubMedGoogle Scholar
  45. 45.
    Carmichael, J., Degraff, W.G., Gazdar, A.F., Minna, J.D., and Mitchell, J.B., Am. Assoc. Cancer Res., 1987, vol. 47, pp. 936–942.Google Scholar

Copyright information

© Pleiades Publishing, Ltd. 2018

Authors and Affiliations

  • A. N. Kvetkina
    • 1
  • E. V. Leychenko
    • 1
    • 2
  • E. A. Yurchenko
    • 1
  • E. A. Pislyagin
    • 1
  • S. Peigneur
    • 3
  • Y. Tytgat
    • 3
  • M. P. Isaeva
    • 1
    • 2
  • D. L. Aminin
    • 1
  • E. P. Kozlovskaya
    • 1
  1. 1.Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern BranchRussian Academy of SciencesVladivostokRussia
  2. 2.School of Natural SciencesFar Eastern Federal UniversityVladivostokRussia
  3. 3.Catholic University of LeuvenLeuvenBelgium

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