Fisheries and Aquatic Sciences

The Korean Society of Fisheries and Aquatic Science (한국수산과학회)
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Genomic Organization, Tissue Distribution and Developmental Expression of Glyceraldehyde 3-Phosphate Dehydrogenase Isoforms in Mud Loach Misgurnus mizolepis

  • Lee, Sang Yoon (Department of Marine Bio-Materials and Aquaculture, Pukyong National University) ;
  • Kim, Dong Soo (Department of Marine Bio-Materials and Aquaculture, Pukyong National University) ;
  • Nam, Yoon Kwon (Department of Marine Bio-Materials and Aquaculture, Pukyong National University)
  • Received : 2013.07.11
  • Accepted : 2013.09.17
  • Published : 2013.12.30
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Abstract

The genomic organization, tissue distribution, and developmental expression of two paralogous GAPDH isoforms were characterized in the mud loach Misgurnus mizolepis (Cypriniformes). The mud loach gapdh isoform genes (mlgapdh-1 and mlgapdh-2) had different exon-intron organizations: 12 exons in mlgapdh-1 (spanning to 4.88 kb) and 11 in mlgapdh-2 (11.78 kb), including a non-translated exon 1 in each isoform. Southern blot hybridization suggested that the mud loach might possess the two copies of mlgapdh-1 and a single copy of mlgapdh-2. The mlgapdh-1 transcript levels are high in tissues requiring high energy flow, such as skeletal muscle and heart, whereas mlgapdh-2 is expressed abundantly in the brain. Both isoforms are differentially regulated during embryonic and larval development, during which their expression is upregulated with the progress of development. Lipopolysaccharide challenge preferentially induced mlgapdh-2 transcripts in the liver. Therefore, the two isoforms have diversified functionally; mlgapdh-1 is associated more closely with energy metabolism, while mlgapdh-2 is related more to stress/immune responses, in the mud loach.

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References

  1. Bannerman DD and Goldblum SE. 2003. Mechanisms of bacterial lipopolysaccharide- induced endothelial apoptosis. Am J Physiol Lung Cell Mol Physiol 284, L899-L914. http://dx.doi.org/10.1152/ajplung.00338.2002.
  2. Booth NJ and Bilodeau-Bourgeois AL. 2009. Proteomic analysis of head kidney tissue from high and low susceptibility families of channel catfish following challenge with Edwardsiella ictaluri. Fish Shellfish Immunol 26, 193-196. http://dx.doi.org/10.1016/j.fsi.2008.03.003.
  3. Bunch DO, Welch JE, Magyar PL, Eddy EM and O'Brien DA. 1998. Glyceraldehyde 3-phosphate dehydrogenase-S protein distribution during mouse spermatogenesis. Biol Reprod 58, 834-841. http://dx.doi.org/10.1095/biolreprod58.3.834.
  4. Cho YS, Lee SY, Kim KH and Nam YK. 2008. Differential modulations of two glyceraldehyde 3-phosphate dehydrogenase mRNAs in response to bacterial and viral challenges in a marine teleost Oplegnathus fasciatus (Perciformes). Fish Shellfish Immunol 25, 472-476. http://dx.doi.org/10.1016/j.fsi.2008.07.007.
  5. Cho YS, Kim DS and Nam YK. 2011. Isoform-specific response of two GAPDH paralogs during bacterial challenge and metal exposure in mud loach (Misgurnus mizolepis; Cypriniformes) kidney and spleen. J Fish Pathol 24, 269-278. http://dx.doi.org/10.7847/ jfp.2011.24.3.269.
  6. Dang W and Sun L. 2011. Determination of internal controls for quantitative real time RT-PCR analysis of the effect of Edwardsiella tarda infection on gene expression in turbot (Scophthalmus maximus). Fish Shellfish Immunol 30, 720-728. http://dx.doi.org/10.1016/j.fsi.2010.12.028.
  7. DeLeo FR. 2004. Modulation of phagocyte apoptosis by bacterial pathogens. Apoptosis 9, 399-413. http://dx.doi.org/10.1023/B:APPT.0000031448.64969.fa.
  8. Gao LY and Kwaik YA. 2000. The modulation of host cell apoptosis by intracellular bacterial pathogens. Trends Microbiol 8, 306-313. http://dx.doi.org/10.1016/S0966-842X(00)01784-4.
  9. Garcia-Meunier P, Etienne-Julan M, Fort P, Piechaczyk M and Bonhomme F. 1993. Concerted evolution in the GAPDH family of retrotransposed pseudogenes. Mamm Genome 4, 695-703. http://dx.doi.org/10.1007/BF00357792.
  10. Kim DS, Jo JY and Lee TY. 1994. Induction of triploidy in mud loach (Misgurnus mizolepis) and its effect on gonad development and growth. Aquaculture 120, 263-270. http://dx.doi.org/10.1016/0044-8486(94)90083-3.
  11. Kim KY and Nam YK. 2008. Evolutionary history of two paralogous glyceraldehyde 3-phosphate dehydrogenase genes in teleosts. J Fish Sci Technol 11, 177-181. http://dx.doi.org/10.5657/ fas.2008.11.3.177.
  12. Kim YU, Park YS and Kim DS. 1987. Development of eggs, larvae and juveniles of loach, Misgurnus mizolepis Gunther. Bull Korean Fish Soc 20, 16-23.
  13. Li T, Hu J, Thomas JA and Li L. 2005. Differential induction of apoptosis by LPS and taxol in monocytic cells. Mol Immunol 42, 1049-1055. http://dx.doi.org/10.1016/j.molimm.2004.09.032.
  14. Liu YJ, Zheng D, Balasubramanian S, Carriero N, Khurana E, Robilotto R and Gerstein MB. 2009. Comprehensive analysis of the pseudogenes of glycolytic enzymes in vertebrates: the anomalously high number of GAPDH pseudogenes highlights a recent burst of retrotrans-positional activity. BMC Genomics 10, 480. http://dx.doi.org/10.1186/1471-2164-10-480.
  15. MacKenzie S, Iliev D, Liarte C, Koskinen H, Planas JV, Goetz FW, Molsa H, Krasnov A and Tort L. 2006a. Transcriptional analysis of LPS-stimulated activation of trout (Oncorhynchus mykiss) monocyte/macrophage cells in primary culture treated with cortisol. Mol Immunol 43, 1340-1348. http://dx.doi.org/10.1016/j.molimm.2005.09.005.
  16. MacKenzie S, Montserrat N, Mas M, Acerete L, Tort L, Krasnov A, Goetz FW and Planas JV. 2006b. Bacterial lipopolysaccharide induces apoptosis in the trout ovary. Reprod Biol Endocrinol 4, 46. http://dx.doi.org/10.1186/1477-7827-4-46.
  17. Manchado M, Infante C, Asensio E and Canavate JP. 2007. Differential gene expression and dependence on thyroid hormones of two glyceraldehyde-3-phosphate dehydrogenases in the flatfish Senegalese sole (Solea senegalensis Kaup). Gene 400, 1-8. http://dx.doi.org/10.1016/j.gene.2007.05.008.
  18. Mezquita J, Pau M and Mezquita C. 1998. Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase expressed in adult chicken testis. J Cell Biochem 71, 127-139. http://dx.doi.org/10.1002/(SICI)1097-4644(19981001)71:1<127::AID-JCB13>3.0.CO;2-K.
  19. Miki K, Qu W, Goulding EH, Willis WD, Bunch DO, Strader LF, Perreault SD, Eddy EM and O'Brien DA. 2004. Glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme, is required for sperm motility and male fertility. Proc Natl Acad Sci U S A 101, 16501-16506. http://dx.doi.org/10.1073/pnas.0407708101.
  20. Mitter K, Kotoulas G Magoulas A, Mulero V, Sepulcre P, Figueras A, Novoa B and Sarropoulou E. 2009. Evaluation of candidate reference genes for QPCR during ontogenesis and of immune-relevant tissues of European seabass (Dicentrarchus labrax). Comp Biochem Physiol B Biochem Mol Biol 153, 340-347. http://dx.doi.org/10.1016/j.cbpb.2009.04.009.
  21. Mommens M, Fernandes JM, Bizuayehu TT, Bolla SL, Johnston IA and Babiak I. 2010. Maternal gene expression in Atlantic halibut (Hippoglossus hippoglossus L.) and its relation to egg quality. BMC Res Notes 3, 138. http://dx.doi.org/10.1186/1756-0500-3-138.
  22. Nam YK, Cho YS, Lee SY, Kim BS and Kim DS. 2011. Molecular characterization of hepcidin gene from mud loach (Misgurnus mizolepis; Cypriniformes). Fish Shellfish Immunol 31, 1251-1258. http://dx.doi.org/10.1016/j.fsi.2011.09.007.
  23. Sarropoulou E, Nousdili D, Kotoulas G and Magoulas A. 2011. Functional divergences of GAPDH isoforms during early development in two perciform fish species. Mar Biotechnol 13, 1115-1124. http://dx.doi.org/10.1007/s10126-011-9375-6.
  24. Schmittgen TD and Livak KJ. 2008. Analyzing real-time PCR data by the comparative CT method. Nat Protoc 3, 1101-1108. http://dx.doi.org/10.1038/nprot.2008.73.
  25. Sirover MA. 2005. New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. J Cell Biochem 95, 45-52. http://dx.doi.org/10.1002/jcb.20399.
  26. Tang R, Dodd A, Lai D, McNabb WC and Love DR. 2007. Validation of zebrafish (Danio rerio) reference genes for quantitative real-time RT-PCR normalization. Acta Biochim Biophys Sin 39, 384-390. http://dx.doi.org/10.1111/j.1745-7270.2007.00283.x.
  27. Tristan C, Shahani N, Sedlak TW and Sawa A. 2011. The diverse functions of GAPDH: views from different subcellular compartments. Cell Signal 23, 317-323. http://dx.doi.org/10.1016/j.cellsig.2010.08.003.
  28. Welch JE, Barbee RR, Magyar PL, Bunch DO and O'Brien DA. 2006. Expression of the spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase (GAPDS) in rat testis. Mol Reprod Dev 73, 1052-1060. http://dx.doi.org/10.1002/mrd.20235.
  29. Welch JE, Brown PL, O'Brien DA, Magyar PL, Bunch DO, Mori C and Eddy EM. 2000. Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells. J Androl 21, 328-338.
  30. Xiang LX, Peng B, Dong WR, Yang ZF and Shao JZ. 2008. Lipopolysaccharide induces apoptosis in Carassius auratus lymphocytes, a possible role in pathogenesis of bacterial infection in fish. Dev Comp Immunol 32, 992-1001. http://dx.doi.org/10.1016/j.dci.2008.01.009.
  31. Xie W, Shao N, Ma X, Ling B, Wei Y, Ding Q, Yang G, Liu N, Wang H and Chen K. 2006. Bacterial endotoxin lipopolysaccharide induces up-regulation of glyceraldehyde-3-phosphate dehydrogenase in rat liver and lungs. Life Sci 79, 1820-1827. http://dx.doi.org/10.1016/j.lfs.2006.06.018.