Browse > Article
http://dx.doi.org/10.7847/jfp.2011.24.3.269

Isoform-specific response of two GAPDH paralogs during bacterial challenge and metal exposure in mud loach (Misgurnus mizolepis: Cypriniformes) kidney and spleen  

Cho, Young-Sun (Institute of Marine Living Modified Organisms, Pukyong National University)
Kim, Dong-Soo (Institute of Marine Living Modified Organisms, Pukyong National University)
Nam, Yoon-Kwon (Institute of Marine Living Modified Organisms, Pukyong National University)
Publication Information
Journal of fish pathology / v.24, no.3, 2011 , pp. 269-278 More about this Journal
Abstract
Gene expression of two glyceraldehyde-3-phosphate dehydrogenase (GAPDH) paralogs was examined during Edwardsiella tarda challenge and heavy metal exposures in mud loach (Misgurnus mizolepis; Cypriniformes) kidney and spleen. Transcription of the two mud loach GAPDH paralogs (mlGAPDH-1 and mlGAPDH-2) was significantly modulated by these stimulatory challenges in an isoform-dependent manner. Based on the real-time RT-PCR analysis, the mlGAPDH-2 transcripts were more preferentially induced by E. tarda challenge, whereas the mlGAPDH-1 transcripts were proven to show more inducibility in response to heavy metal exposure using Cd, Cu, Mn and Zn at $5{\mu}M$. Their isoform-specific response patterns were closely in accordance with the TF binding profiles in promoter and intron-1 of the two mlGAPDH isoforms, in which the mlGAPDH-2 has more binding sites for immune-related transcription factors than mlGAPDH-1 while the mlGAPDH-1 possesses exclusively metal responsive elements in its intron. Collectively, the mlGAPDHs are potentially involved in cellular pathways independent of glycolysis and the two GAPDH paralogs might undergo functional diversification or subfunctionalization at least at the transcription level.
Keywords
Bacterial challenge; GAPDH isoforms; Heavy metals; Misgurnus mizolepis;
Citations & Related Records
Times Cited By KSCI : 2  (Citation Analysis)
연도 인용수 순위
1 Tang, R., Dodd, A., Lai, D., McNabb, W.C. and Love, D.R.: Validation of zebrafish (Danio rerio) reference genes for quantitative real-time RT-PCR normalization. Acta Biochim. Biophys. Sin., 39:384-390, 2007.   DOI   ScienceOn
2 Valavanidis. A., Vlahogianni, T., Dassenakis, M. and Scoullos, M.: Molecular biomarkers of oxidative stress in aquatic organisms in relation to toxic environmental pollutants. Ecotoxicol. Environ. Saf., 64:178-189, 2006.   DOI   ScienceOn
3 Welch, J.E., Barbee, R.R., Magyar, P.L., Bunch, D.O. and O'Brien, D.A.: Expression of the spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase (GAPDS) in rat testis. Mol. Reprod. Dev., 73:1052-1060, 2006.   DOI   ScienceOn
4 Welch, J.E., Brown, P.L., O'Brien, D.A., Magyar, P.L., Bunch, D.O., Mori, C. and Eddy, E.M.: Human glyceraldehyde 3-phosphate dehydrogenase-2 gene is expressed specifically in spermatogenic cells. J. Androl., 21:328-338, 2000.
5 Li, T., Hu, J., Thomas, J.A. and Li, L.: Differential induction of apoptosis by LPS and taxol in monocytic cells. Mol. Immunol., 42:1049-1055, 2005.   DOI   ScienceOn
6 Manchado, M., Infante, C., Asensio, E. and Canavate, J.P.: 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, 2007.   DOI   ScienceOn
7 Mazzola, J.L. and Sirover, M.A.: Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function. Biochim. Biophys. Acta. Gen. Subj., 1622:50-56, 2003.   DOI   ScienceOn
8 Mezquita, J., Pau, M. and Mezquita, C.: Several novel transcripts of glyceraldehyde-3-phosphate dehydrogenase expressed in adult chicken testis. J. Cell. Biochem., 71:127-139, 1998.   DOI   ScienceOn
9 Mitter, K., Kotoulas, G., Magoulas, A., Mulero, V., Sepulcre, P., Figueras, A., Novoa, B. and Sarropoulou, E.: Evaluation of candidate reference genes for QPCR during ontogenesis and of immune-relevant tissues of European seabass (Dicentrarchus labrax). Comp. Biochem. Physiol. Biochem., 153B:340-347, 2009.
10 Murray, P.J.: The JAK-STAT signaling pathway: Input and output integration. J. Immunol., 178:2623-2629, 2007.   DOI
11 Rebl, A., Goldammer, T. and Seyfert, H.M.: Toll-like receptor signaling in bony fish. Vet. Immunol. Immunopathol., 134:139-150, 2010.   DOI   ScienceOn
12 Cho, Y.S., Lee, S.Y., Kim, K.H. and Nam, Y.K.: 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, 2008.   DOI   ScienceOn
13 Bannerman, D.D. and Goldblum, S.E.: Mechanisms of bacterial lipopolysaccharide-induced endothelial apoptosis. Am. J. Physiol. Lung Cell Mol. Physiol., 284:L899-L914, 2003.
14 Bols, N.C., Brubacher, J.L., Ganassin, R.C. and Lee, L.E.J.: Ecotoxicology and innate immunity in fish. Dev. Comp. Immunol., 25:853-873, 2001.   DOI   ScienceOn
15 Booth, N.J. and Bilodeau-Bourgeois, A.L.: 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, 2009.   DOI   ScienceOn
16 Cho, Y.S., Lee, S.Y., Kim, K.Y. and Nam, Y.K.: Two metallothionein genes from mud loach Misgurnus mizolepis (Teleostei; Cypriniformes): Gene structure, genomic organization, and mRNA expression analysis. Comp. Biochem. Physiol., 153B:317-326, 2009.
17 Singh, R. and Green, M.R.: Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science, 259:365-368, 1993.   DOI
18 Robbins, A.R., Ward, R.D. and Oliver, C.: A mutation in glyceraldehyde 3-phosphate dehydrogenase alters endocytosis in CHO cells. J. Cell Biol., 130:1093-1104, 1995.   DOI   ScienceOn
19 Schmittgen, T.D. and Livak, K.J.: Analyzing real-time PCR data by the comparative CT method. Nat. Protoc., 3:1101-1108, 2008.   DOI   ScienceOn
20 Sehgal, P.B.: Paradigm shifts in the cell biology of STAT signaling. Semin. Cell Dev. Biol., 19:329-340, 2008.   DOI   ScienceOn
21 Sirover, M.A.: New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. J. Cell. Biochem., 95:45-52, 2005.   DOI   ScienceOn
22 Kim, K.Y. and Nam, Y.K.: Evolutionary history of two paralogous glyceraldehyde 3-phosphate dehydrogenase genes in teleosts. J. Fish. Sci. Technol., 11:177-181, 2008.
23 Dang, W. and Sun, L.: 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, 2011.   DOI   ScienceOn
24 Demarse, N.A., Ponnusamy, S., Spicer, E.K., Apohan, E., Baatz, J.E., Ogretmen, B. and Davies, C.: Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation. J. Mol. Biol., 394:789-803, 2009.   DOI   ScienceOn
25 Ishitani, R., Tajima, H., Takata, H., Tsuchiya, K., Kuwae, T., Yamada, M., Takahashi, H., Tatton, N.A. and Katsube, N.: Proapoptotic protein glyceraldehyde-3- phosphate dehydrogenase: a possible site of action of antiapoptotic drugs. Prog. Neuro-Psychopharmacol. Biol. Psychiatry, 27:291-301, 2003.   DOI   ScienceOn
26 Lee, S.Y., Stoliar, O. and Nam, Y.K.: Transcriptional alteration of two metallothionein isoforms in mud loach (Misgurnus mizolepis) fry during acute heavy metal exposure. Fish. Aquat. Sci., 13:112-117, 2010.
27 Azam, S., Jouvet, N., Jilani, A., Vongsamphanh, R., Yang, X., Yang, S. and Ramotar, D.: Human glyceraldehyde-3-phosphate dehydrogenase plays a direct role in reactivating oxidized forms of the DNA repair enzyme APE1. J. Biol. Chem., 283:30632-30641, 2008.   DOI   ScienceOn
28 Andrews, G.K.: Regulation of metallothionein gene expression by oxidative stress and metal irons. Biochem. Pharmacol., 59:95-104, 2000.   DOI   ScienceOn