Polar Biology

, Volume 31, Issue 9, pp 1059–1065 | Cite as

Lack of an HSP70 heat shock response in two Antarctic marine invertebrates

  • Melody S. ClarkEmail author
  • Keiron P. P. Fraser
  • Lloyd S. Peck
Original Paper


Members of the HSP70 gene family comprising the inducible (HSP70) genes and GRP78 (glucose-regulated protein 78 kDa) were identified in an Antarctic sea star (Odontaster validus) and an Antarctic gammarid (Paraceradocus gibber). These genes were surveyed for expression levels via Q-PCR after an acute 2-hour heat shock experiment in both animals and a time course assay in O. validus. No significant up-regulation was detected for any of the genes in either of the animals during the acute heat shock. The time course experiment in O. validus produced slightly different results with an initial down regulation in these genes at 2°C, but no significant up-regulation of the genes either at 2 or 6°C. Therefore, the classical heat shock response is absent in both species. The data is discussed in the context of the organisms’ thermal tolerance and the applicability of HSP70 to monitor thermal stress in Antarctic marine organisms.


Antarctic Climate change Biomarker Stress Heat shock proteins 


  1. Altschul SF, Madden TL, Schaffer AA, Zhang JH, Zhang Z, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389–3402PubMedCrossRefGoogle Scholar
  2. Boeckmann B, Bairoch A, Apweiler R, Blatter MC, Estreicher A, Gasteiger E, Martin MJ, Michoud K, O’Donovan C, Phan I, Pilbout S, Schneider M (2003) The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003. Nucleic Acids Res 31:365–370PubMedCrossRefGoogle Scholar
  3. Bosch TCG, Krylow SM, Bode HR, Steele RE (1988) Thermotolerance and synthesis of heat-shock proteins—these responses are present in hydra-attenuata but absent in hydra-oligactis. Proc Natl Acad Sci USA 85:7927–7931PubMedCrossRefGoogle Scholar
  4. Carpenter CM, Hofmann GE (2000) Expression of 70 kDa heat shock proteins in Antarctic and New Zealand Notothenioid fish. Comp Biochem Physiol A 125:229–238CrossRefGoogle Scholar
  5. Clark MS, Burns G (2007) Characterisation of the warm acclimated protein gene (wap65) in the Antarctic plunderfish (Harpagifer antarcticus). DNA Seq. doi: 10.1080/10425170701388586
  6. Clark MS, Fraser KPPF, Burns G, Peck LS (2007) The HSP70 heat shock response in the Antarctic fish Harpagifer antarcticus. Polar Biol 31:171–180. doi: 10.1007/s00300-007-0344-5 CrossRefGoogle Scholar
  7. Clark MS, Fraser KPPF, Peck LS (2008a) The HSP70 heat shock response in Antarctic marine molluscs. Cell Stress Chaperones 13. doi: 10.1007/s12192-008-0014-8
  8. Clark MS, Geissler P, Waller C, Fraser KPPF, Barnes DKA, Peck LS (2008b) The environmental HSP70 heat shock response in the Antarctic limpet: Nacella concinna. Cell Stress Chaperones 13. doi: 10.1007/s12192-008-0015-7
  9. Coleman CO (1989) Burrowing, grooming and feeding behaviour of Paraceradocus, an Antarctic amphipod genus (Crustacea). Polar Biol 10:43–48CrossRefGoogle Scholar
  10. Ewing B, Hillier L, Wendl MC, Green P (1998) Base-calling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res 8:175–185PubMedGoogle Scholar
  11. Feder ME, Hofmann GE (1999) Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Ann Rev Physiol 61:243–282CrossRefGoogle Scholar
  12. Fink AL (1999) Chaperone-mediated protein folding. Physiol Rev 79:425–449PubMedGoogle Scholar
  13. Fisher RA (1954) Statistical methods for research workers. Pub. Oliver and Boyd, EdinburghGoogle Scholar
  14. Gordon D, Abajian C, Green P (1998) Consed: a graphical tool for sequence finishing. Genome Res 8:195–202PubMedGoogle Scholar
  15. Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571–580PubMedCrossRefGoogle Scholar
  16. Hofmann GE, Buckley BA, Airaksinen S, Keen JE, Somero GN (2000) The Antarctic fish Trematomus bernachii lacks heat inducible heat shock protein synthesis. J Exp Biol 203:2331–2339PubMedGoogle Scholar
  17. Jin Y, deVries AL (2006) Antifreeze glycoprotein levels in Antarctic Notothenioid fishes inhabiting different thermal environments and the effect of warm acclimation. Comp Biochem Physiol B 144:290–300PubMedCrossRefGoogle Scholar
  18. LaTerza AL, Miceli C, Luporine P (2001) Divergenec between two Antarctic species of the ciliate Euplotes, E. focardii and E. nobilii, in the expression of heat-shock protein 70 genes. Mol Ecol 10:1061–1067CrossRefGoogle Scholar
  19. LaTerza AL, Miceli C, Luporine P (2004) The gene for the heat-shock protein 70 of Euplotes focardii, an Antarctic psychrophilic ciliate. Antarct Sci 16:23–28CrossRefGoogle Scholar
  20. Lowe CJ, Davison W (2005) Plasma osmolarity, glucose concentration and erythrocyte responses of two Antarctic Notothenioid fishes to acute and chronic thermal change. J Fish Biol 67:752–766CrossRefGoogle Scholar
  21. Lund SG, Caissie D, Cunjak RA, Vijayan MM, Tufts BL (2002) The effects of environmental heat stress on heat-shock mRNA and protein expression in Miramichi Atlantic salmon (Salmo salar) parr. Can J Fish Aquat Sci 59:1553–1562CrossRefGoogle Scholar
  22. McClintock JB, Pearse JS, Bosch I (1988) Population structures and energetics of the shallow water Antarctic sea star Odontaster validus in contrasting habitats. Mar Biol 99:235–246CrossRefGoogle Scholar
  23. Meredith MP, King JC (2005) Rapid climate change in the ocean west of the Antarctic Peninsula during the second half of the 20th century. Geophys Lett 32:L19604–L19609CrossRefGoogle Scholar
  24. Morimoto RI (1998) Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 12:3788–3796PubMedCrossRefGoogle Scholar
  25. Parsell DA, Lindquist S (1993) The function of heat-shock proteins in stress tolerance—degradation and reactivation of damaged proteins. Ann Rev Genet 27:437–496PubMedCrossRefGoogle Scholar
  26. Pearse J (1965) Reproductive periodicities in several contrasting populations of Odontaster validus Koehler, a common Antarctic asteroid. Antarct Res Ser 5:39–85Google Scholar
  27. Peck LS (2002) Ecophysiology of Antarctic marine ectotherms: limits to life. Polar Biol 25:31–40CrossRefGoogle Scholar
  28. Peck LS, Conway LZ (2000) The myth of metabolic cold adaptation: oxygen consumption in stenothermal Antarctic bivalve molluscs. In: Harper E, Crame AJ (eds) Evolutionary biology of the bivalvia. Geological Society of London Special Publication 177. Cambridge University Press, Cambridge, pp 441–450Google Scholar
  29. Peck LS, Prothero-Thomas E (2002) Temperature effects on the metabolism of larvae of the Antarctic starfish Odontaster validus, using a novel microrespirometry method. Mar Biol 141:271–276CrossRefGoogle Scholar
  30. Peck LS, Webb KE, Bailey DM (2004) Extreme sensitivity of biological function to temperature in Antarctic marine species. Funct Ecol 18:625–630CrossRefGoogle Scholar
  31. Peck LS, Webb KE, Miller A, Clark MS, Hill T (2008) Temperature limits to activity, feeding and metabolism in the Antarctic starfish Odontaster validus. MEPS (in press)Google Scholar
  32. Pfaffl MW (2001) A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 29:2002–2007CrossRefGoogle Scholar
  33. Pfaffl MW, Horgan GW, Dempfle L (2002) Relative expression software tool (REST©) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res 30:1–10CrossRefGoogle Scholar
  34. Place SP, Hofmann GE (2005) Constitutive expression of a stress-inducible heat shock protein gene, hsp70, in a phylogenetically distant Antarctic fish. Polar Biol 28:261–267CrossRefGoogle Scholar
  35. Place SP, Zippay ML, Hofmann GE (2004) Constitutive roles for inducible genes: evidence for the alteration in expression of the inducible hsp70 gene in Antarctic Notothenioid fishes. Am J Physiol Regul Integr Comp Physiol 287:R429–R436PubMedGoogle Scholar
  36. Podrabsky JE, Somero GN (2006) Inducible heat tolerance in Antarctic Nothothenioid fishes. Polar Biol 30:39–43CrossRefGoogle Scholar
  37. Ritossa F (1962) A new puffing pattern induced by temperature shock and DNP in Drosophila. Experimentia 18:571–573CrossRefGoogle Scholar
  38. Sorensen JG, Kristensen TN, Loeschcke V (2003) The evolutionary and ecological role of heat shock proteins. Ecol Lett 6:1025–1037CrossRefGoogle Scholar
  39. Stanwell-Smith D, Peck LS (1998) Temperature and embryonic development in relation to spawning and field occurance of larvae of three Antarctic echinoderms. Biol Bull 194:44–52CrossRefGoogle Scholar
  40. Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL-W—improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673–4680PubMedCrossRefGoogle Scholar
  41. Tomanek L, Sanford E (2003) Heat-shock protein 70 (Hsp70) as a biochemical stress indicator: an experimental field test in two congeneric intertidal gastropods (Genus: Tegula). Biol Bull 205:276–284PubMedCrossRefGoogle Scholar
  42. Wu CH, Apweiler R, Bairoch A, Natale DA, Barker WC, Boeckmann B, Ferro S, Gasteiger E, Huang H, Lopez R, Magrane M, Martin MJ, Mazumder R, O’Donovan C, Redaschi N, Suzek B (2006) The universal protein resource (UniProt): an expanding universe of protein information. Nucleic Acids Res 34:D187–D191PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  • Melody S. Clark
    • 1
    Email author
  • Keiron P. P. Fraser
    • 1
  • Lloyd S. Peck
    • 1
  1. 1.British Antarctic SurveyNatural Environment Research CouncilCambridgeUK

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