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Apr 22, 2024
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May 5, 2024
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Abstract

Claudins multigene family encode proteins which forms main structures of tight junction among epithelial cells. In intestinal epithelium claudin proteins are proposed to have roles in ion balances regulation and forming barrier against pathogenic invasion. This work was done in order to identify claudin encoding genes in common carp (Cyprinus carpio), one of the most important cultured fish in freshwater aquaculture. Sample of RNA was isolated from the fish and transcribed into cDNA. Carp claudin genes were amplified, cloned, and sequenced. Carp claudin 1 and 2 were amplified with primers designed based on relevant known claudin genes in fish. On the basis of carp ESTs, other six carp claudin genes were amplified by using appropriate primers. Phylogenetic and sequence analysis confirmed that the eight identified genes are claudin genes and could be designated as carp claudin 1, 2, 3b, 3c, 7, 11, 23, and 30, respectively. This finding could be used to develop further study of carp claudin especially roles of claudin during pathogen infection and strategy to modulate its expression in order to protect diseases in carp aquaculture.

Keywords

Claudin; Cyprinus carpio; Intestinal barrier

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Copyright (c) 2014 Aquacultura Indonesiana

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This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Author Biographies

Hamdan Syakuri, Jenderal Soedirman University, Purwokerto, Indonesia

Department of Fisheries and Marine Science, Faculty of Science and Technology,

Dieter Steinhagen, University of Veterinary Medicine Hanover, Bünteweg 17, D-30559 Hanover, Germany

Fish Diseases Research Unit, Center of Infectious Diseases

References

  1. Adamek, M., H. Syakuri, S. Harris, KŁ. Rakus, G. Brogden, M. Matras, I. Irnazarow, and D. Steinhagen. 2013. Cyprinid herpesvirus 3 infection disrupts the skin barrier of common carp (Cyprinus carpio L.). Veterinary Microbiology, 162: 456–470
  2. Alexandre, M.D., B.G. Jeansonne, R.H. Renegar, R.Tatum, and Y.H. Chen. 2007. The first extracellular domain of claudin-7 affects paracellular Cl permeability. Biochemical and Biophysical Research Communications,357 (1): 87-91.
  3. Altschul, S.F., W. Gish, W. Miller, E.W. Myers, and D.J. Lipman. 1990. Basic local alignment search tool. J. Mol. Biol., 215 (3):403-10.
  4. Angelow, S., R. Ahlstrom, and A.S. Yu. 2008.Biology of claudins. Am J. Physiol. Renal.Physiol., 295 (4): F867-76.
  5. Anisimova, M. and O. Gascuel. 2006. Approximate likelihood-ratio test for branches: A fast,accurate, and powerful alternative. Syst. Biol.,55 (4): 539-52.
  6. Bagherie-Lachidan, M., S.I. Wright, and S.P. Kelly. 2008. Claudin-3 tight junction proteins in Tetraodon nigroviridis: cloning, tissue-specific expression, and a role in hydromineral balance. American Journal of Physiology - Regulatory, Integrative and Comparative Physiology, 294 (5): R1638- R1647.
  7. Berkes, J., V.K. Viswanathan, S.D. Savkovic, and G. Hecht. 2003. Intestinal epithelial responses to enteric pathogens: effects on the tight junction barrier, ion transport, and inflammation. Gut, 52 (3): 439-451.
  8. Chasiotis, H. and S.P. Kelly. 2011. Effect of cortisol on permeability and tight junction protein transcript abundance in primary cultured gill epithelia from stenohaline goldfish and euryhaline trout. General and Comparative Endocrinology, 172 (3): 494-504.
  9. Colegio, O.R., C. Van Itallie, C. Rahner, and J.M. Anderson. 2003.Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am J. Physiol. Cell. Physiol., 284 (6): C1346-54.
  10. Dereeper, A., V. Guignon, G. Blanc, S. Audic, S. Buffet, F. Chevenet, J.F. Dufayard, S. Guindon, V. Lefort, M. Lescot, J.M. Claverie, and O. Gascuel. 2008.Phylogeny.fr: robust phylogenetic analysis for the non-specialist. Nucleic Acids Res., 36 (Web Server issue): W465-9.
  11. Dereeper, A., S. Audic, J.M. Claverie, and G. Blanc. 2010. BLAST-EXPLORER helps you building datasets for phylogenetic analysis.BMC Evol. Biol., 10: 8.
  12. Edgar, R.C. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res., 32 (5): 1792-7.
  13. Gasteiger, E., A. Gattiker, C. Hoogland, I. Ivanyi,R.D. Appel, and A. Bairoch. 2003.ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res., 31 (13): 3784–3788.
  14. Groschwitz, K.R. and S.P. Hogan. 2009. Intestinal barrier function: Molecular regulation and disease pathogenesis. Journal of Allergy and Clinical Immunology, 124 (1): 3-20.
  15. Guindon, S. and O. Gascuel. 2003. A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol., 52 (5): 696-704.
  16. Guttman, J.A. and B.B. Finlay. 2009. Tight junctions as targets of infectious agents. Biochimica et Biophysica Acta (BBA) – Biomembranes, 1788 (4): 832-841.
  17. Hirokawa, T., S. Boon-Chieng, and S. Mitaku. 1998.
  18. SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics, 14 (4): 378-379.
  19. Kollmar, R., S.K. Nakamura, J.A. Kappler, and A.J. Hudspeth. 2001. Expression and phylogeny of claudins in vertebrate primordia. Proceedings of the National Academy of Sciences of the United States of America, 98(18): 10196-10201.
  20. Lal-Nag, M. and P. Morin. 2009. The claudins. Genome Biology, 10 (8): 235.
  21. Larkin, M.A., G. Blackshields, N.P. Brown, R. Chenna, P.A. McGettigan, H. McWilliam, F. Valentin, I.M. Wallace, A. Wilm, R. Lopez, J.D. Thompson, T.J. Gibson, and D.G. Higgins. 2007. Clustal W and Clustal X version 2.0. Bioinformatics, 23 (21): 2947-2948.
  22. Loh, Y.H., A. Christoffels, S. Brenner, W. Hunziker, and B. Venkatesh. 2004. Extensive expansion of the claudin gene family in the teleost fish, Fugu rubripes. Genome Research, 14 (7): 1248-1257.
  23. Mitaku, S. and T. Hirokawa. 1999. Physicochemical
  24. factors for discriminating between soluble and membrane proteins: hydrophobicity of helical segments and protein length. Protein Engineering, 12 (11) : 953-957.
  25. Mitaku, S., T. Hirokawa, and T. Tsuji. 2002. Amphiphilicity index of polar amino acids as an aid in the characterization of amino acid preference at membrane–water interfaces. Bioinformatics, 18 (4): 608-616.
  26. Morita, K., M. Furuse, K. Fujimoto, and S. Tsukita.1999. Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proceedings of the National Academy of Sciences of the United States of America, 96(2): 511-516.
  27. Pagni, M., V. Ioannidis, L. Cerutti, M. Zahn-Zabal, C. V. Jongeneel, and L. Falquet. 2004. MyHits: a new interactive resource for protein annotation and domain identification.Nucleic Acids Res., 32 (Web Server issue):W332-5.
  28. Pagni, M., V. Ioannidis, L. Cerutti, M. Zahn-Zabal, C.V. Jongeneel, J. Hau, O. Martin, D. Kuznetsov, and L. Falquet. 2007. MyHits: improvements to an interactive resource for analyzing protein sequences. Nucleic Acids Res., 35 (Web Server issue): W433-7.
  29. Prasad, S., R. Mingrino, K. Kaukinen, K.L. Hayes, R.M. Powell, T.T. MacDonald, and J.E.Collins. 2005.Inflammatory processes have differential effects on claudins 2, 3 and 4 in colonic epithelial cells. Lab. Invest., 85 (9):1139-1162.
  30. Rozen, S. and H. Skaletsky. 1999. Primer3 on the WWW for general users and for biologist programmers. Bioinformatics Methods and Protocols, 132: 365-386.
  31. Sandbichler, A.M., M. Egg, T. Schwerte, and B. Pelster. 2011. Claudin 28b and F-actin are involved in rainbow trout gill pavement cell tight junction remodeling under osmotic stress. J. Exp. Biol., 214 (Pt 9): 1473-87.
  32. Schulzke, J.D., S. Ploeger, M. Amasheh, A. Fromm, S. Zeissig, H. Troeger, J. Richter, C.Bojarski, M. Schumann, and M. Fromm. 2009. Epithelial tight junctions in intestinal inflammation. Ann. N.Y. Acad. Sci., 1165:294-300.
  33. Syakuri, H., M. Adamek, G. Brogden, K.Å. Rakus, M. Matras, I. Irnazarow, and D. Steinhagen. 2013. Intestinal barrier of carp (Cyprinus carpio L.) during a cyprinid herpesvirus 3-infection: Molecular identification and regulation of the mRNA expression of claudin encoding genes. Fish &Shellfish Immunology, 34 (1): 305-314.
  34. Syakuri, H., V. Jung-Schroers, M. Adamek, G.Brogden, I. Irnazarow, and D. Steinhagen.2014. Beta-glucan feeding differentiated the regulation of mRNA expression of claudin genes and prevented an intestinal inflammatory response post Aeromonas hydrophila intubation in common carp,Cyprinus carpio L. Journal of Fish Diseases,37: 149–156
  35. Tipsmark, C.K., P. Kiilerich, T.O. Nilsen, L.O.E.Ebbesson, S.O. Stefansson, and S.S. Madsen. 2008a.Branchial expression patterns of claudin isoforms in Atlantic salmon during seawater acclimation and smoltification. American Journal of Physiology - Regulatory, Integrative and Comparative Physiology, 294 (5): R1563-R1574.
  36. Tipsmark, C.K., J.A. Luckenbach, S.S. Madsen, P.Kiilerich, and R.J. Borski. 2008b.Osmoregulation and expression of ion transport proteins and putative claudins in the gill of southern Flounder (Paralichthys lethostigma). Comparative Biochemistry and Physiology - Part A: Molecular & Integrative Physiology, 150 (3): 265-273.
  37. Turner, J.R. 2009. Intestinal mucosal barrier function in health and disease. Nat. Rev. Immunol., 9(11): 799-809.
  38. Van Itallie, C.M. and J.M. Anderson. 2004. The molecular physiology of tight junction pores. Physiology (Bethesda), 19: 331-8.
  39. Van Itallie, C.M. and J.M. Anderson. 2006. Claudins and epithelial paracellular transport.Annu. Rev. Physiol., 68: 403-29.
  40. Wen, H., D.D. Watry, M.C. Marcondes, and H.S.Fox. 2004. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol.Cell. Biol., 24 (19): 8408-17.