NR  Vol.3 No.4 , December 2012
Tissue-Specific Isoenzyme Variations in Tilapia Fish, Oreochromis niloticus
ABSTRACT
Native polyacrylamide gel electrophoresis have been used to analyze malate dehydrogenase (MDH), acid phosphatase (Acph) and peroxidase (Px) isoenzymes in different tissues (liver, kidney, muscle and heart) of the tilapia fish, Oreo- chromis niloticus in order to study the tissue specificity of these isoenzymes. Three, two and one fractions have been recorded respectively for the three isoenzymes in different studied tissues. The MDH-1 and MDH-2 have been ex- pressed only in muscle and heart while MDH-3 has been expressed in all studied tissues. The percentage amount of MDH in general varied significantly between muscle and different studied tissues. With respect to acid phosphatase, the percentage amount of the total enzyme showed significant difference between liver and muscle and that this variation may be due to higher gene activity in liver. Peroxidase isoenzyme was recorded in liver and heart only with significant increase in liver. The kidney was the least among the studied tissues in showing gene expression for the studied isoenzymes and therefore, liver, heart and muscle tissues are better applicable in studying the isoenzymatic profiles for fish physiology and systematics.

Cite this paper
M. AL-Harbi and S. Amer, "Tissue-Specific Isoenzyme Variations in Tilapia Fish, Oreochromis niloticus," Natural Resources, Vol. 3 No. 4, 2012, pp. 201-205. doi: 10.4236/nr.2012.34027.
References
[1]   R. Trewavas, “Tilapiine Fishes of the Genera Sarotherodon, Oreochromis and Danakilia, ? Comstock Publishing Associates, London, 1983.

[2]   S.-F. Li, Y. Zhao, W.-J. Fan, W.-Q. Cai and Y.-F. Xu, “Possible Genetic Reproductive Isolation between Two Tilapiine Genera and Species: Oreochromis niloticus and Sarotherodon melanotheron, ?Zoological Research, Vol. 32, No. 5, 2011, pp. 521-527.

[3]   R. S. V. Pullin, A. E. Eknath, T. Gjedrum, M. M. Tayamen, J. M. Macaranas and T. A. Abella, “The Genetic Improvement of Farmed Tilapias (GIFT) Project, the Story So Far,? NAGA. ICLARM Quarterly, Vol. 14, No. 2, 1991, pp. 7-9.

[4]   S.-F. Li, J.-L. Zhao, M. Dey and R. Dunham, “Isozyme Variation of Nile Tilapia Oreochromis niloticus in China,? Asian Fisheries Science, Vol. 14, 2001, pp. 411-416.

[5]   Y. Mo, C. D. Young and R. W. Gracy, “Isolation and Characterization of Tissue-Specific Isozymes of Glucosephosphate Isomerase from Catfish and Conger,? Journal of Biological Chemistry, Vol. 250, No. 17, 1975, pp. 6747-6755.

[6]   S. E. Fisher and G. S. Whitt, “Evolution of Isozyme Loci and Their Differential Tissue Expression. Creatine Kinase as a Model System,? Journal of Molecular Evolution, Vol. 12, No. 1, 1978, pp. 25-55. doi:10.1007/BF01732544

[7]   J. F. Leslie and P. J. Pontier, “Linkage Conservation of Homologous Esterase Loci in Fish (Cyprinodontoidei: Poeciliidae),? Biochemical Genetics, Vol. 18, No. 1-2, 1980, pp. 103-105. doi:10.1007/BF00504363

[8]   W. J. Berg and D. G. Buth, “Glucose Dehydrogenase in Teleosts: Tissue Distribution and Proposed Function,? Comparative Biochemistry and Physiology, Vol. 77, No. 2, 1984, pp. 285-288.

[9]   R. W. Holt and W. S. Leibel, “Coexpression of Distinct Eye- and Liver-Specific LDH Isozymes in Cichlid Fish,? Journal of Experimental Zoology, Vol. 244, No. 2, 1987, pp. 337-343. doi:10.1002/jez.1402440219

[10]   F. Basaglia, “Interspecific Gene Differences and Phylogeny of the Sparidae Family (Perciformes, Teleostei), Estimated from Electrophoretic Data on Enzymatic Tissue-Expression,? Comparative Biochemistry and Physiology, B, Vol. 99, No. 3, 1991, pp. 495-508. doi:10.1016/0305-0491(91)90329-C

[11]   D. Xia, T. Wu and H. Wang, “Differential Gene Expression for Lactate Dehydrogenase of Mandarian Fish (Sinaperca chuatsi),? Aquaculture, Vol. 108, No. 3-4, 1992, pp. 207-214. doi:10.1016/0044-8486(92)90107-V

[12]   M. Seimiya, T. Kusakabe and N. Suzuki, “Primary Structure and Differential Gene Expression of Three Membrane Forms of Guanylyl Cyclase Found in the Eye of the Teleost Oryzias latipes, ?Journal of Biological Chemistry, Vol. 272, 1997, pp. 23407-23417. doi:10.1074/jbc.272.37.23407

[13]   R. Shahjahan, A. Karim, R. A. Begum, M. S. Alam and A. Begum, “Tissue Specific Esterase Isozyme Banding Pattern in Nile Tilapia (Oreochromis niloticus), ?University Journal of Zoology, Vol. 27, 2008, pp. 1-5.

[14]   C. R. Goward and D. J. Nicholls, “Malate Dehydrogenase: A Model for Structure, Evolution, and Catalysis,? Protein Science, Vol. 3, No. 10, 1994, pp. 1883-1888. doi:10.1002/pro.5560031027

[15]   R. Mishra and S. P. Shukla, “Endosulfan Negatively Modulates-Mitochondrial Malate Dehydrogenase from the Freshwater Catfish, Clarias batrachus,? Ecotoxicology and Environmental Safety, Vol. 56, No. 3, 2003, pp. 425-433. doi:10.1016/S0147-6513(03)00006-X

[16]   A. Chaudhuri and G. Krishna, “Tissue Specifisty and Degree of Polymorphism of Five Enzyme Systems of L. rohita, from River Yamuna,? Fish Genetics and Biodiversity Conservation, Vol. 5, 1998, pp. 358-360.

[17]   S. Fujimoto, Y. Urata, T. Nakagawa and A. Ohara, “Characterization of Intermediate Molecular Weight Acid Phosphatase from Bovin Kidney Cortex, ?Journal of Biochemistry, Vol. 96, No. 4, 1984, pp. 1079-1088.

[18]   J. Shan, “Dissertation on: Transcriptional Regulation of the Human Prostatic Acid Phosphatase Gene,? University of Oulu, Oulu, 2002, p. 15.

[19]   A. Rodriguez, M. A. Esteban and J. Meseguer, “Phagocytosis and Peroxidase Release by Seabream (Sparus aurata L.) Leukocytes in Response to Yeast Cells, ? The Anatomical Record Part A: Discoveries in Molecular, Cellular, and Evolutionary Biology, Vol. 272, No. 1, 2003, pp. 415-423. doi:10.1002/ar.a.10048

[20]   I. M. Soares-da-Silva, J. Ribeiro, C. Valongo, R. Pinto, M. Vilanova, R. Bleher and J. Machad, “Cytometric, Morphologic and Enzymatic Characterization of Haemocytes in Anodonta cygnea,? Comparative Biochemistry and Physiology A: Molecular & Integrative Physiology, Vol. 132, No. 3, 2002, pp. 541-553. doi:10.1016/S1095-6433(02)00039-9

[21]   T. Holmblad and K. Soderhall, “Cell Adhesion Molecules and Antioxidative Enzymes in a Crustacean, Possible Role in Immunity,? Aquaculture, Vol. 172, No. 1-2, 1999, pp. 111-123. doi:10.1016/S0044-8486(98)00446-3

[22]   S. C. Gamble, P. S. Goldfarb, C. Porte and D. R. Livingstone, “Glutathione Peroxidase and Other Antioxidant Enzyme Function in Marine Invertebrates (Mytifus edulis, Pecten maximus, Carcinus maenas and Asterias rubens),? Marine Environmental Research, Vol. 39, No. 1-4, 1995, pp. 191-195. doi:10.1016/0141-1136(94)00031-J

[23]   T. S. Galloway and M. H. Depledge, “Immunotoxicology in Invertebrates: Measurement and Ecotoxicological Review,? Ecotoxicology, Vol. 10, No. 1, 2001, pp. 5-23. doi:10.1023/A:1008939520263

[24]   M. D’Ischa, A. Napolitano and G. Prota, “Peroxidase as an Alternative to Tyrosinase in the Oxidative Polymerization of 5,6-Dihydroxyindoles tomelanin(s), ?Biochimica et Biophysica Acta, Vol. 1073, No. 2, 1991, pp. 423-430. doi:10.1016/0304-4165(91)90152-7

[25]   H. Stegemann, A. M. R. Afify and K. R. F. Hussein, “Cultivar Identification of Dates (Phoenix dactylifera) by Protein Patterns,? Second International Symposium of Biochemical Approaches to Identification of Cultivars, Braunschweing, West Germany, 1985, p. 44.

[26]   J. F. Jonathan and N. F. Wendell, “Visualization and Interpretation of Plant Isozymes,? In: D. E. Soltis and P. S. Soltis, Ed., Isozymes in Plant Biology, Champan and Hall, London, 1990, pp. 5-45.

[27]   J. F. Wendel and N. F. Weeden, “Visualization and Interpretation of Plant Isozymes,? In: D. E. Soltis and P. S. Soltis, Eds., Isozymes in Plant Biology, Dioscorides Press, Portland, 1989, pp. 5-45. doi:10.1007/978-94-009-1840-5_2

[28]   W. H. Heldt, “A Leaf Cell Consists of Several Metabolic Compartments,? Plant Biochemistry and Molecular Biology, Institute of Plant Biochemistry, Gottingen with the Collaboration of Fiona, 1997.

[29]   W. Allendorff and F. M. Utter, “Population Genetics,? In: W. S. Hoaran and D. J. Randalal, Eds., Fish Physiology, Academic Press, New York, 1978, pp. 407-454.

[30]   A. Siddiqua, A. Saeed, R. Naz, M. Sherazi, S. Abbas and A. Saeed, “Purification and Biochemical Properties of Acid Phosphatase from Rohu Fish Liver,? International Journal of Agriculture and Biology, Vol. 14, No. 2, 2012, pp. 223-228.

[31]   E. A. Dyrynda, R. K. Pipe, G. R. Burt and N. A. Ratcliffe, “Modulations in the immune Defenses of Mussels (Mytilus edulis) from Contaminated Sites in the UK,? Aquatic Toxicology, Vol. 42, No. 3, 1998, pp. 169-185. doi:10.1016/S0166-445X(97)00095-7

[32]   L. D. Mydlarz and C. D. Harvel, “Peroxidase Activity and Inducibility in the Sea Fan Coral Exposed to a Fungal Pathogen,? Comparative Biochemistry and Physiology A: Molecular and Integrative Physiology, Vol. 146, No. 1, 2007, pp. 54-62. doi:10.1016/j.cbpa.2006.09.005

[33]   A. J. Nappi and B. M. Christensen, “Melanogenesis and Associated Cytotoxic Reactions: Applications to Insect Innate Immunity, ?Insect Biochemistry and Molecular Biology, Vol. 35, No. 5, 2005, pp. 443-459. doi:10.1016/j.ibmb.2005.01.014

[34]   G. P. Bolwell, D. R. Davies, C. Gerrish, C.-K. Auh, T. M. Murphy, “Comparative Biochemistry of the Oxidative Burst Produced by Rose and French Bean Cells Reveals Two Distinct Mechanisms, ?Plant Physiology, Vol. 116, No. 4, 1998, pp. 1379-1385. doi:10.1104/pp.116.4.1379

[35]   P. R. Laud and J. W. Campbell, “Genetic Basis for Tissue Isozyme of Glutamine Synthetase in Elasmobranchs,? Journal of Molecular Evolution, Vol. 39, No. 1, 1994, pp. 93-100. doi:10.1007/BF00178254

[36]   T. H. Yang and G. N. Somero, “Activity of Lactate Dehydrogenase but Not Its Concentration of Messenger RNA Increases with Body Size in Barred Sand Bass, Paralabrax nebulifer (Teleostei),? The Biological Bulletin, Vol. 19, No. 2, 1996, pp. 155-158.

 
 
Top