Molecular & Cellular Toxicology

, Volume 6, Issue 4, pp 384–390

Isolation of hyperthermal stress responsive genes in soft coral (Scleronephthya gracillimum)

  • Seonock Woo
  • Hye-young Jeon
  • Jongrak Lee
  • Jun-Im Song
  • Hong-Seog Park
  • Seungshic Yum
Original Paper


The extensive isolation of genes responsive to hyperthermal stress conditions in soft coral (Scleronephthya gracillimum) is described. Soft coral colonies were exposed to high seawater temperature conditions. Gene candidates whose transcript levels changed in response to hyperthermal conditions were identified by differential display polymerase chain reaction (DD-PCR). Twenty-four types of candidate genes were identified, 18 of which were upregulated in expression and 6 of which were downregulated. The genes were found to function in post-translational modification, protein turnover and chaperones (O); translation, ribosomal structure and biogenesis (J); signal transduction mechanisms (T); defense mechanisms (V); inorganic ion transport and metabolism (P); energy production and conversion (C); cytoskeleton (Z); cell cycle control, cell division and chromosome partitioning (D); lipid transport and metabolism (I); chromatin structure and dynamics (B); transcription (K); replication, recombination and repair (L); secondary metabolites biosynthesis, transport and catabolism (Q); extracellular structures (W); general function prediction (R); and finally, unknown function (S) based on KOG classification. Among these candidates, their expressional changes were confirmed by real-time quantitative PCR (qRT-PCR). These 24 isolated gene candidates were differentially expressed and therefore have great potential as molecular biomarkers for the identification of environmental stressors.


Hyperthermal stress Differentially expressed genes Real-time quantitative PCR Soft coral Scleronephthya gracillimum 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Costanza, R. et al. The value of the world’s ecosystem services and natural capital. Nature 387:253–260 (1997).CrossRefGoogle Scholar
  2. 2.
    Liang, P. & Pardee, A. B. Differential display of eukaryotic messenger RNA by means of the polymerase chain reaction. Science 257:967–971 (1992).CrossRefPubMedGoogle Scholar
  3. 3.
    Liang, P., Averboukh, L. & Pardee, A. B. Distribution and cloning of eukaryotic mRNAs by means of differential display: refinements and optimization. Nucleic Acids Res 21:3269–3275 (1993).CrossRefPubMedGoogle Scholar
  4. 4.
    Liang, P. et al. Differential display using one-base anchored oligo-dT primers. Nucleic Acids Res 22:5763–5764 (1994).CrossRefPubMedGoogle Scholar
  5. 5.
    Hwang, I. T. et al. Annealing control primer system for improving specificity of PCR amplification. Biotechniques 35:1180–1184 (2003).PubMedGoogle Scholar
  6. 6.
    Kim, Y. J. et al. Annealing control primer system for identification of differentially expressed genes on agarose gels. Biotechniques 36:424–426, 428, 430 passim (2004).PubMedGoogle Scholar
  7. 7.
    Duchen, M. R. Mitochondria and calcium: from cell signalling to cell death. J Physiol 529Pt 1:57–68 (2000).CrossRefPubMedGoogle Scholar
  8. 8.
    Pan, J. S. et al. Oxidative stress disturbs energy metabolism of mitochondria in ethanol-induced gastric mucosa injury. World J Gastroenterol 14:5857–5867 (2008).CrossRefPubMedGoogle Scholar
  9. 9.
    Chin, D. & Means, A. R. Calmodulin: a prototypical calcium sensor. Trends Cell Biol 10:322–328 (2000).CrossRefPubMedGoogle Scholar
  10. 10.
    Hoeflich, K. P. & Ikura, M. Calmodulin in action: diversity in target recognition and activation mechanisms. Cell 108:739–742 (2002).CrossRefPubMedGoogle Scholar
  11. 11.
    Moreto, J. et al. Differential involvement of H- and K-Ras in Raf-1 activation determines the role of calmodulin in MAPK signaling. Cell Signal 21:1827–1836 (2009).CrossRefPubMedGoogle Scholar
  12. 12.
    Gelebart, P., Opas, M. & Michalak, M. Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum. Int J Biochem Cell Biol 37:260–266 (2005).CrossRefPubMedGoogle Scholar
  13. 13.
    Jia, L. et al. Novel anti-oxidative role of calreticulin in protecting A549 human type II alveolar epithelial cells against hypoxic injury. Am J Physiol Cell Physiol 294:C47–55 (2008).CrossRefPubMedGoogle Scholar
  14. 14.
    Alur, M. et al. Suppressive roles of calreticulin in prostate cancer growth and metastasis. Am J Pathol 175:882–890 (2009).CrossRefPubMedGoogle Scholar
  15. 15.
    Carafoli, E. Historical review: mitochondria and calcium: ups and downs of an unusual relationship. Trends Biochem Sci 28:175–181 (2003).CrossRefPubMedGoogle Scholar
  16. 16.
    del Arco, A. & Satrustegui, J. Molecular cloning of Aralar, a new member of the mitochondrial carrier superfamily that binds calcium and is present in human muscle and brain. J Biol Chem 273:23327–23334 (1998).CrossRefPubMedGoogle Scholar
  17. 17.
    Okuda, T. et al. PQBP-1 transgenic mice show a lateonset motor neuron disease-like phenotype. Hum Mol Genet 12:711–725 (2003).CrossRefPubMedGoogle Scholar
  18. 18.
    Arosio, P. & Levi, S. Ferritin, iron homeostasis, and oxidative damage. Free Radic Biol Med 33:457–463 (2002).CrossRefPubMedGoogle Scholar
  19. 19.
    Torti, S. V. et al. The molecular cloning and characterization of murine ferritin heavy chain, a tumor necrosis factor-inducible gene. J Biol Chem 263:12638–12644 (1988).PubMedGoogle Scholar
  20. 20.
    Torti, F. M. & Torti, S. V. Regulation of ferritin genes and protein. Blood 99:3505–3516 (2002).CrossRefPubMedGoogle Scholar
  21. 21.
    Barbeito, A. G. et al. Abnormal iron metabolism and oxidative stress in mice expressing a mutant form of the ferritin light polypeptide gene. J Neurochem 109:1067–1078 (2009).CrossRefPubMedGoogle Scholar
  22. 22.
    Turner, M. W. The role of mannose-binding lectin in health and disease. Mol Immunol 40:423–429 (2003).CrossRefPubMedGoogle Scholar
  23. 23.
    Arnold, J. & Grune, T. PARP-mediated proteasome activation: a co-ordination of DNA repair and protein degradation? Bioessays 24:1060–1065 (2002).CrossRefPubMedGoogle Scholar
  24. 24.
    Simbulan-Rosenthal, C. M. et al. Transient poly(ADPribosyl) ation of nuclear proteins and role of poly(ADPribose) polymerase in the early stages of apoptosis. J Biol Chem 273:13703–13712 (1998).CrossRefPubMedGoogle Scholar
  25. 25.
    Finlin, B. S. et al. RERG is a novel ras-related, estrogen-regulated and growth-inhibitory gene in breast cancer. J Biol Chem 276:42259–42267 (2001).CrossRefPubMedGoogle Scholar
  26. 26.
    Key, M. D., Andres, D. A., Der, C. J. & Repasky, G. A. Characterization of RERG: an estrogen-regulated tumor suppressor gene. Methods Enzymol 407:513–527 (2006).CrossRefPubMedGoogle Scholar
  27. 27.
    Blobel, C. P. Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF alpha and Notch. Cell 90:589–592 (1997).CrossRefPubMedGoogle Scholar
  28. 28.
    Primakoff, P. & Myles, D. G. The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet 16:83–87 (2000).CrossRefPubMedGoogle Scholar
  29. 29.
    Woo, S. et al. Efficient isolation of intact RNA from the soft coral Scleronephthya gracillimum (Kükenthal) for gene expression analyses. Integr Biosci 9:205–209 (2005).Google Scholar
  30. 30.
    Woo, S. et al. Effects of heavy metals on antioxidants and stress-responsive gene expression in Javanese medaka (Oryzias javanicus). Comp Biochem Physiol C Toxicol Pharmacol 149:289–299 (2009).CrossRefPubMedGoogle Scholar

Copyright information

© The Korean Society of Toxicogenomics and Toxicoproteomics and Springer Netherlands 2010

Authors and Affiliations

  • Seonock Woo
    • 1
  • Hye-young Jeon
    • 1
  • Jongrak Lee
    • 2
  • Jun-Im Song
    • 3
  • Hong-Seog Park
    • 4
  • Seungshic Yum
    • 1
  1. 1.South Sea Environment Research DepartmentKorea Ocean Research and Development InstituteGeojeKorea
  2. 2.Laboratory of Marine BiodiversityIn The Sea Korea Co., Ltd.JejuKorea
  3. 3.Department of Biological Science, College of Natural SciencesEwha Womans UniversitySeoulKorea
  4. 4.Genome Research CenterKorea Research Institute of Bioscience and BiotechnologyDaejeonKorea

Personalised recommendations