Skip to main content
Log in

Intracellular protein degradation in the development of the atlantic salmon Salmo salar L.

  • Published:
Russian Journal of Bioorganic Chemistry Aims and scope Submit manuscript

Abstract

Through the example of the Atlantic salmon Salmo salar L. we provide here the quick details on the universal and specific features of the proteolytic apparatus in the skeletal muscles of fish. Among the numerous muscle tissue proteases, the most comprehensively studied are those which determine the protein degradation levels in the efficiently growing and developing muscles of the salmon juveniles and by this way regulate the protein accumulation rates in muscles and the overall growth processes in the organism, namely, the lysosomal cathepsins B and D and calcium-dependent proteases (calpains). We have detected the age-related differences in the activity of the intracellullar proteases in salmon muscles, which suggest the important role of the proteolysis regulation in growth and the specific role for the certain proteolytic enzymes. For example, we have obtained data indicating the negative correlation between the cathepsin D and calpains activity levels in muscle tissue and the weight gain rate in the salmon of different age groups. The detected positive correlation between the cathepsin B activity and the morphometric indices in juvenile fish is apparently indicative of the key role of this enzyme in the metabolism of proteins of the predominantly nonmyofibrillar nature.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

AMC:

aminomethyl coumarine

CatB, CatD:

cathepsins B and D

DTT:

dithiotreitol

Na-EDTA:

sodium ethyl-enediaminetetraacetic acid

PMSF:

phenylmethylsulfonyl fluoride

SDS:

sodium dodecyl sulfate

TCA:

trichloroacetic acid

References

  1. Bond, J.S. and Butler, P.E., Annu. Rev. Biochem., 1987, vol. 56, pp. 333–364.

    Article  CAS  PubMed  Google Scholar 

  2. Nemova, N.N., Vnutrikletochnye proteoliticheskie fermenty u ryb (Intracellular Proteolytic Enzymes in Fish), Petrozavodsk: KarNTs RAN, 1996.

    Google Scholar 

  3. Goll, D.E., Thompson, V.F., Li, H., Wei, W., and Cong, J., Physiol. Rev., 2003, vol. 83, no. 3, pp. 731–801.

    Article  CAS  PubMed  Google Scholar 

  4. Turk, V., Stoka, V., Vasiljeva, O., Renko, M., Sun, T., Turk, B., and Turk, D., Biochim. Biophys. Acta, 2012, vol. 1824, pp. 68–88.

    Article  CAS  PubMed  Google Scholar 

  5. Rock, K.L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., and Goldberg, A.L., Cell, 1994, vol. 78, pp. 761–771.

    Article  CAS  PubMed  Google Scholar 

  6. Dayton, W.R., Goll, D.E., Stromer, M.H., Reville, W.J., Zeece, M.G., and Robson, R.M., in Proteases and Biological Control, Reich, E., Rifkin, D.B., and Shaw, E, Eds., New York: Cold Spring Harbor Lab., 1975, pp. 551–577.

  7. Huang, J. and Forsberg, N.E., Proc. Natl. Acad. Sci. U.S.A., 1998, vol. 95, pp. 12100–12105.

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  8. Goll, D.E., Neti, G., Mares, S.W., and Thompson, V.F., J. Anim. Sci., 2008, vol. 86, pp. E19–E35.

    Article  CAS  PubMed  Google Scholar 

  9. Busconi, L., Folco, E.J., Studdert, C., and Sanchez, J.J., Comp. Biochem. Physiol., B, 1992, vol. 102, pp. 303–309.

    CAS  PubMed  Google Scholar 

  10. Seiliez, I., Dias, K., and Cleveland, B.M., Am. J. Physiol. Regul. Integr. Comp. Physiol., 2014, vol. 307, pp. R1330–R1337.

  11. Koodziejska, I. and Smorski, Z.E., J. Food Biochem., 1996, vol. 20, pp. 349–363.

    Article  Google Scholar 

  12. Verrez-Bagnis, V., Ladrat, C., Noelle, J., and Fleurence, J., J. Sci. Food Agric., 2002, vol. 82, pp. 1256–1262.

    Article  CAS  Google Scholar 

  13. Mommsen, T.P., Comp. Biochem. Physiol. B, 2004, vol. 139, no. 3, pp. 383–400.

    Article  PubMed  Google Scholar 

  14. Salem, M., Kenney, B., Rexroad, C., and Yao, J., Comp. Biochem. Physiol. D, 2006, vol. 1, pp. 227–237.

    Google Scholar 

  15. Seiliez, I., Gabillard, J.C., Riflade M., Sadoul, B., Dias, K., Averous, J., Tesseraud, S., Skiba, S., and Panserat, S., Autophagy, 2012, vol. 8, pp. 364–375.

    Article  CAS  PubMed  Google Scholar 

  16. Purintrapiban, J., Wang, M.C., and Forsberg, N.E., Comp. Biochem. Physiol., vol. 136, pp. 393–401.

  17. Mommsen, T.P., Comp. Biochem. Physiol., vol. 129, pp. 207–219.

  18. Johnston, I.A., Bower, N.I., and Macqueen, D.J., J. Exp. Biol, 2011, vol. 214, pp. 1617–1628.

    Article  CAS  PubMed  Google Scholar 

  19. Salem, M., Silverstein, J., Rexroad, C.E., and Yao, J., BMC Genomics, 2007, vol. 8, p. 328.

    Article  PubMed Central  PubMed  Google Scholar 

  20. Overturf, K. and Gaylord, T.G., Comp. Biochem. Physiol., vol. 152, pp. 150–160.

  21. Cleveland, B.M. and Burr, G.S., Aquaculture, 2011, vol. 319, pp. 194–204.

    Article  CAS  Google Scholar 

  22. Cleveland, B.M. and Weber, G.M., Gen. Comp. Endocrinol., 2011, vol. 174, pp. 132–142.

    Article  CAS  PubMed  Google Scholar 

  23. Nemova, N.N., Sidorov, V.S., and Ripatti, P.O., Vopr. Ikhtiol., 1980, vol. 20, no. 1, pp. 180–182.

    CAS  Google Scholar 

  24. Salmerón, C., García de la Serrana, D., Jiménez-Amilburu, V., Fontanillas, R., Navarro, I., Johnston, I.A., Gutiérrez, J., and Capilla, E., PLoS ONE, 2013, vol. 8, no. 9, p. e75349.

    Article  PubMed Central  PubMed  Google Scholar 

  25. Nemova, N.N., Kaivarainen, E.I., and Bondareva, L.A., Vestnik Mosk. Univ. Ser. 2: Khim., 2000, vol. 41, suppl. 6, pp. 106–108.

    Google Scholar 

  26. Salem, M., Kenney, P.B., Killefer, J., and Nath, J., J. Muscle Foods, 2004, vol. 15, pp. 245–255.

    Article  CAS  Google Scholar 

  27. Bahuaud, D., Gaarder, M., Veiseth-Kent, E., and Thomassen, M., Aquaculture, 2010, vol. 310, pp. 213–220.

    Article  CAS  Google Scholar 

  28. Gaarder, M., Thomassen, M.S., and Veiseth-Kent, E., Food Chem., 2011, vol. 125, pp. 1091–1096.

    Article  CAS  Google Scholar 

  29. Lysenko, L.A., Kantserova, N.P., Ushakova, N.V., and Nemova, N.N., Russ. J. Bioorg. Chem, 2012, vol. 38, pp. 282–290.

    Article  CAS  Google Scholar 

  30. Muramoto, M., Yamamoto, Y., and Seki, N., Bull. Jpn. Soc. Sci. Fish., 1989, vol. 55, pp. 917–923.

    Article  CAS  Google Scholar 

  31. Salem, M., Yao, J., Rexroad, C., Kenney, B., Semmens, K., Killefer, J., and Nath, J., Comp. Biochem. Physiol. B, 2005, vol. 141, pp. 488–497.

    Article  PubMed  Google Scholar 

  32. Chéret, R., Delbarre-Ladrat, C., de Lamballerie-Anton, M., and Verrez-Bagnis, V., Food Chem., 2007, vol. 101, pp. 1474–1479.

    Article  Google Scholar 

  33. Yamashita, M. and Konagaya, S., Comp. Biochem. Physiol. B, 1992, vol. 103, no. 4, pp. 999–1003.

    Google Scholar 

  34. Liu, H., Yin, L., Zhang, N., Li, S., and Ma, C., Food Chem., 2008, vol. 110, no. 2, pp. 310–318.

    Article  CAS  PubMed  Google Scholar 

  35. Wang, P.A., Stenvik, J., Larsen, R., Maehre, H., and Olsen, R.L., Comp. Biochem. Physiol. B, 2007, vol. 147, no. 3, pp. 504–511.

    Article  PubMed  Google Scholar 

  36. Churova, M.V., Meshcheryakova, O.V., Veselov, A.E., and Nemova, N.N., Russ. J. Dev. Biol., 2015, no. 5 (in press).

    Google Scholar 

  37. Ladrat, C., Chaplet, M., Verrez-Bagnis, V., Noel, J., and Fleurence, J., Comp. Biochem. Physiol. B, vol. 125, pp. 83–95.

  38. Cottin, P., Brustis, J.J., Poussard, S., Elamrani, N., Broncard, S., and Ducastaing, A., Acta, 1994, vol. 1223, no. 2, pp. 170–178.

    CAS  Google Scholar 

  39. Fukuda, M., Sako, H., Shigeta, T., and Shibata, R., Mar. Biol., 2001, vol. 138, no. 1, pp. 47–55.

    Article  CAS  Google Scholar 

  40. Shustov, Yu.A., Baryshev, I.A., and Belyakova, E.N., Biol. Vnutr. Vod, 2012, no. 3, pp. 66–70.

    Google Scholar 

  41. Anson, M.L., J. Gen. Physiol., 1938, vol. 22, pp. 79–89.

    Article  PubMed Central  CAS  PubMed  Google Scholar 

  42. Enns, D.L. and Belcastro, A.N., Can. J. Physiol. Pharmacol., 2006, vol. 84, pp. 601–609.

    Article  CAS  PubMed  Google Scholar 

  43. Bradford, M.M., Anal. Biochem., 1976, vol. 72, pp. 248–254.

    Article  CAS  PubMed  Google Scholar 

  44. Arthur, J.S.C. and Mykles, D.L., Calpain. Methods and Protocols, Elce, J.S., Ed., New Jersey: Humana Press, 2000, pp. 109–116.

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to L. A. Lysenko.

Additional information

Original Russian Text © L.A. Lysenko, N.P. Kantserova, M.Yu. Krupnova, A.E. Veselov, N.N. Nemova, 2015, published in Bioorganicheskaya Khimiya, 2015, Vol. 41, No. 6, pp. 717–724.

The article has been adapted from the report presented at the VIIth All-Russian symposium “Proteins and Peptides”, Novosibirsk, 12–17 July, 2015.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Lysenko, L.A., Kantserova, N.P., Krupnova, M.Y. et al. Intracellular protein degradation in the development of the atlantic salmon Salmo salar L.. Russ J Bioorg Chem 41, 645–651 (2015). https://doi.org/10.1134/S1068162015060096

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1134/S1068162015060096

Keywords

Navigation