Identification of some proteins of blood and tissue fluid in the fish with enciphered genome

Comparative and Ontogenic Biochemistry

Abstract

Applying proteomics methods, ependymins, vitellogenins, immunoglobulins and albumin-like proteins (ALP) were identified in the blood and tissue fluid of pacific redfin, scorpaena, sterlet and two ray species. For all proteins, except ALP, identification by tandem MALDI mass- spectrometry was successful. The reconstruction of amino acid fragments sequences was performed using databases of fish proteins with sequenced genome and that of mammals. The problems with ALP identification are associated with high level of their structural variety and absence of resemblance with mammalian proteins.

Key words

fish proteins blood tissue fluids MALDI 

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References

  1. 1.
    Andreeva, A.M., Chalov, Yu.P., and Ryabtseva, I.P., Peculiarities of Distribution of Plasma Proteins between Specialized Compartments of Inner Medium in the Carp Cyprinus carpio, Zh. Evol. Biokhim. Fiziol., 2007, vol. 43, pp. 501–504.PubMedGoogle Scholar
  2. 2.
    Laemmli, U.K., Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage, Nature (Gr. Brit.), 1970, vol. 227, no. 4, pp. 680–685.CrossRefGoogle Scholar
  3. 3.
    Andreeva, A.M., Structural and Functional Organization of Fish Blood Proteins, Nova Science Publisher: N.Y. 2012, 188 p.Google Scholar
  4. 4.
    Goufman, E.I., Moshkovskii, S.A., Tikhonova, O.V., Lokhov, P.G., Zgoda, V.G., Serebryakova, M.V., Toropygin, I.Yu., Vlasova, M.A., Archakov, A.I., Safarova, M.P., and Makarov, O.V., Two-Dimensional Electrophoretic Proteome Study of Serum Thermostable Fraction from Patients with Various Tumor Conditions, Biokhimiya, 2006, vol. 71, pp. 445–453.Google Scholar
  5. 5.
    Shashoua, V.E., Brain Protein Metabolism and the Acquisition of New Patterns of Behavior, Proc. Natl. Acad. Sci. USA, 1977, vol. 74, pp. 1743–1747.PubMedCrossRefGoogle Scholar
  6. 6.
    Sterrer, S., Konigstorfer, A., and Hoffmann, W., Biosynthesis and Expression of Ependymin Homologous Sequences in Zebrafish Brain, Neurosci., 1990, vol. 37, pp. 277–284.CrossRefGoogle Scholar
  7. 7.
    Tang, S.J., Sun, K.H., Sun, G.H., Lin, G., Lin, W.W., and Chuang, M.J., Cold-Induced Ependymin Expression in Zebrafish and Carp Brain: Implications for Cold Acclimation, FEBS Lett., 1999, vol. 459, pp. 95–99.PubMedCrossRefGoogle Scholar
  8. 8.
    Apostolopoulos, J., Sparrow, R.L., McLeod, J.L., Collier, F.M., Darcy, P.K., Slater, H.R., Ngu, C., Gregorio-King, C.C., and Kirkland, M.A., Identification and Characterization of a Novel Family of Mammalian Ependymin-Related Proteins (MERPs) in Hematopoietic, Nonhematopoietic, and Malignant Tissues, DNA Cell Biol., 2001, vol. 20, pp. 625–635.PubMedCrossRefGoogle Scholar
  9. 9.
    Nimmrich, I., Erdmann, S., Melchers, U., Chtarbova, S., Finke, U., Hentsch, S., Hoffmann, I., Oertel, M., Hoffmann, W., and Muller, O., The Novel Ependymin Related Gene UCC1 Is Highly Expressed in Colorectal Tumor Cells, Cancer Lett., 2001, vol. 165, pp. 71–79.PubMedCrossRefGoogle Scholar
  10. 10.
    Suárez-Castillo, E.C., Medina-Ortíz, W.E., Roig-López, J.L., and García-Arrarás, J.E., Ependymin, a Gene Involved in Regeneration and Neuroplasticity in Vertebrates, Is Overexpressed during Regeneration in the Echinoderm Holothuria glaberrima, Gene, 2004, vol. 334, pp. 133–143.PubMedCrossRefGoogle Scholar
  11. 11.
    Suarez-Castillo, E.C. and Garcia-Arraras, J.E., Molecular Evolution of the Ependymin Protein Family: a Necessary Update, BMC Evol Biol., 2007, vol. 7, p. 23. Doi: 10.1186/1471-2148-7-23.PubMedCentralPubMedCrossRefGoogle Scholar
  12. 12.
    Andreeva, A.M., Participation of Yolk Proteins in Regulation of Germ Genes Expression from Intergeneric F1 Hybrids of Bream Roach and Blue Bream, IJMBF, 2011, vol. 17, no. 1/2, pp. 159–180.Google Scholar
  13. 13.
    Johanning, K.M. and Specker, J.L., Characterization of Yolk Proteins during Oocyte Development of Tilapia, Oreochromis mossambicus, Comp. Biochem. Physiol., 1995, vol. 112 B, pp. 177–189.CrossRefGoogle Scholar
  14. 14.
    Matsubara, T., Ohkubo, N., Andoh, T., Sullivan, C.V., and Hara, A., Two Forms of Vitellogenin, Yielding Two Distinct Lipovitellins, Play Different Roles during Oocyte Maturation and Early Development of Barfin Flounder, Verasper moseri, a Marine Teleost Spawning Pelagic Eggs, Devol. Biol., 1999, vol. 213, no. 1, pp. 18–32.Google Scholar
  15. 15.
    Finn, R.N., Fyhn, H.J., Noriberg, B., Munholand, J., and Reith, M., Oocyte Hydration as a Key Feature in the Adaptive Evolution of Teleost Fishes to Seawater, Proc. 6th Int. Symp. Reprod. Physiol. Fish., 2000, pp. 289–291.Google Scholar
  16. 16.
    Andreeva, A.M., Serum Gamma-Globulins of the Fishes, J. Ichthyol., 2001, vol. 41, no. 6, pp. 464–470. Original Russian text is published in Voprosy Ikhtiology, 2001, vol. 41, no. 4, pp. 550-556.Google Scholar
  17. 17.
    Alabyev, B.Y., Najakshin, A.M., Denisov, S.G., Mechetina, L.V., and Taranin, A.V., The Diversity of Expressed IgL Genes in Chondrostean Acipenser ruthenus: Implications for the Evolution of IgL Types, Unpublished, NCBI, 1999, ACCESS CAB37327.Google Scholar
  18. 18.
    Andreeva, A.M. and Dmitrieva, A.E., Organization of Heavy Chains of Scorpaena Scorpaena porcus L., Intern. Conf. “Problems of Immunology, Pathology and Health Protection of Fish”, 2011, Borok, pp. 81–85.Google Scholar
  19. 19.
    Andreeva, A.M., Mechanisms of the Plurality of Scorpaena porcus L. Serum Albumin, OJMS, 2011, vol. 1 (2), pp. 31–35. DOI: 10.4236/ ojms.2011.12003.CrossRefGoogle Scholar
  20. 20.
    Zorin, N.A., Zhabin, S.G., Lykova, O.F., Zorina, V.N., Belogorlova, T.I., and Chirikova, T.S., Comparative Investigation of Physicochemical and Antigenic Properties of Human and Animal Albumin, Zh. Evol. Biokhim. Fiziol., 1994, vol. 30, pp. 505–511.PubMedGoogle Scholar
  21. 21.
    Chikhachev, A.S., Complex Investigations of the Causes of Protein Polymorphism in Fish, Ekologicheskaya fiziologiya i biokhimiya ryb (Ecological Physiology and Biochemistry of Fish), Kiev, Naukova Dumka, 1982, p. 4, pp. 33-35.Google Scholar
  22. 22.
    Filosa, M.F., Adam, I., Robson, P., Heinig, J.A., Smith, K., Keeley, F.W., and Youson, J.H., Partial Clone of the Gene for AS Protein of the Lamprey Petromyzon marinus, a Member of the Albumin Supergene Family Whose Expression Is Restricted to the Larval and Metamorphic Phases of the Life Cycle, J. Exp. Zool., 1998, vol. 282,no. 3, pp. 301–309.PubMedCrossRefGoogle Scholar
  23. 23.
    Danis, M.H., Filosa, M.F., and Youson, J.H., An Albumin-Like Protein in the Serum of Non- Parasitic Brook Lamprey (Lampetra appendix) Is Restricted to Preadult Phases of the Life Cycle in Contrast to the Parasitic Species Petromyzon marinus, Comp. Biochem. Physiol. Part B. Biochem. Mol. Biol., 2000, vol. 127, no. 2, pp. 251–260.CrossRefGoogle Scholar
  24. 24.
    Metcalf, V., Brennan, St., and Georg, P., Using Serum Albumin to Inter Vertebrate Phylogenies, Applied Bioinformatics, 2003, vol. 2,no. 3, pp. 97–107.Google Scholar
  25. 25.
    Metcalf, V.J., George, P.M., and Brennan, S.O., Lungfish Albumin is More Similar to Tetrapod Than to Teleost Albumins: Purification and Characterization of Albumin from Australian Lungfish, Neocaratodus forsteri, Comp. Biochem. Physiol. Part B. Biochem. Mol. Biol., 2007, vol. 147,no. 3, pp. 428–437.CrossRefGoogle Scholar

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© Pleiades Publishing, Ltd. 2013

Authors and Affiliations

  1. 1.Papanin Institute of Biology of Inland WatersRussian Academy of Sciences, Yaroslavskaya oblastBorokRussia

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