Identification of differentially expressed genes in the hydrothermal vent shrimp Rimicaris exoculata exposed to heat stress

Marine Genomics

Volumn 3, Issue 2, 2010, Pages 71-78

  Cottin, Delphine ^a   Shillito, Bruce ^a   Chertemps, Thomas ^b   Tanguy, Arnaud ^a,c   Léger, Nelly ^a   Ravaux, Juliette ^a  

^a SORBONNE UNIVERSITÉ   (France)

^b INRA Institut National de la Recherche Agronomique   (France)

^c STATION BIOLOGIQUE DE ROSCOFF   (France)

Author keywords

Heat stress; Hydrothermal vent; Real time PCR; Rimicaris exoculata; Suppression subtractive hybridization

Indexed keywords

CELL SURFACE RECEPTOR; COMPLEMENTARY DNA; HEMOCYANIN; HISTONE; LECTIN; MANNOSE BINDING LECTIN; MANNOSE RECEPTOR; METALLOPROTEINASE; PRIMER DNA;

ANIMAL; ARTICLE; ATLANTIC OCEAN; BIOLOGY; DECAPODA (CRUSTACEA); DNA SEQUENCE; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; GENETICS; HEAT; HYDROTHERMAL VENT; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYSIOLOGICAL STRESS; PHYSIOLOGY; REAL TIME POLYMERASE CHAIN REACTION;

ANIMALS; ATLANTIC OCEAN; BASE SEQUENCE; COMPUTATIONAL BIOLOGY; DECAPODA (CRUSTACEA); DNA PRIMERS; DNA, COMPLEMENTARY; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; HEMOCYANIN; HISTONES; HOT TEMPERATURE; HYDROTHERMAL VENTS; LECTINS, C-TYPE; MANNOSE-BINDING LECTINS; METALLOPROTEASES; MOLECULAR SEQUENCE DATA; REAL-TIME POLYMERASE CHAIN REACTION; RECEPTORS, CELL SURFACE; SEQUENCE ANALYSIS, DNA; STRESS, PHYSIOLOGICAL;

ANIMALIA; DECAPODA (CRUSTACEA); RIMICARIS EXOCULATA;

EID: 77957794348     PISSN: 18747787     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.margen.2010.05.002     Document Type: Article

References (48)

1. Andersen C.L., Jensen J.L., Orntoft T.F. Normalization of real-time quantitative reverse transcription-PCR data: a model-based variance estimation approach to identify genes suited for normalization, applied to bladder and colon cancer data sets. Cancer Res. 2004, 64(15):5245-5250.
2. Boutet I., Jollivet D., Shillito B., Moraga D., Tanguy A. Molecular identification of differentially regulated genes in the hydrothermal-vent species Bathymodiolus thermophilus and Paralvinella pandorae in response to temperature. BMC Genomics 2009, 10:222.
3. Boutet I., Tanguy A., Le Guen D., Piccino P., Hourdez S., Legendre P., Jollivet D. Global depression in gene expression as a response to rapid thermal changes in vent mussels. Proc. R. Soc. B 2009, 276:3071-3079.
4. Buckley B.A., Gracey A.Y., Somero G.N. The cellular response to heat stress in the goby: a cDNA microarray and protein-level analysis. J. Exp. Biol. 2006, 209:2660-2677.
5. Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92:351-366.
6. Cairo G., Tacchini L., Pogliaghi G., Anzon E., Tomasi A., Bernelli-Zazzera A. Induction of ferritin synthesis by oxidative stress. J. Biol. Chem. 1995, 270(2):700-703.
7. Chevaldonné P., Desbruyères D., Le Haitre M. Time-series of temperature from three deep-sea hydrothermal vent sites. Deep-Sea Res. 1991, 38:1417-1430.
8. Clark M.S., Fraser K.P.P., Peck L.S. Antarctic marine molluscs do have an HSP70 heat shock response. Cell Stress Chaperones 2008, 13:39-49.
9. Clarke A. Costs and consequences of evolutionary temperature adaptation. Trends Ecol. Evol. 2003, 18(11):573-581.
10. Cottin D., Ravaux J., Léger N., Halary S., Toullec J.-Y., Sarradin P.-M., Gaill F., Shillito B. Thermal biology of the deep-sea vent annelid Paralvinella grasslei: in vivo studies. J. Exp. Biol. 2008, 211:2196-2204.
11. De La Vega E., Degnan B.M., Hall M.R., Wilson K.J. Differential expression of immune-related genes and transposable elements in black tiger shrimp (Penaeus monodon) exposed to a range of environmental stressors. Fish Shellfish Immunol. 2007, 23:1072-1088.
12. Desbruyères D., Biscoito M., Caprais J.C., Colaço A., Comtet T., Crassous P., Fouquet Y., Khripounoff A., Le Bris N., Olu K., Riso R., Sarradin P.-M., Segonzac M., Vangriesheim A. Variations in the deep-sea hydrothermal vent communities on the Mid-Atlantic Ridge near the Azores plateau. Deep-Sea Res. 2001, 48:1325-1346.
13. Diatchenko L., Lau Y.F.C., Campbell A.P., Chenchik A., Moqadam F., Huang B., Lukyanov K., Gurshaya N., Sverdlov E.D., Siebert P.D. Suppression subtractive hybridization: a method for generating differentially regulated or tissue-specific cDNA probes and libraries. Proc. Nat. Acad. Sci. U. S. A. 1996, 93:6025-6030.
14. Feder M.E., Hofmann G.E. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol. 1999, 61:243-282.
15. Hansen B.H., Altin D.A., Nordtug T., Olsen A.J. Suppression subtractive hybridization library prepared from the copepod Calanus finmarchicus exposed to a sublethal mixture of environmental stressors. Comp. Biochem. Physiol. D 2007, 2:250-256.
16. Heise K., Puntarulo S., Nikinmaa M., Abele D., Pörtner H.O. Oxidative stress during stressful heat exposure and recovery in the North sea eelpout Zoarces viviparus L. J. Exp. Biol. 2006, 209:353-363.
17. Hochachka P.W., Somero G.N. Biochemical Adaptation 2002, Oxford University Press, New York.
18. Hofmann G.E., Somero G.N. Protein ubiquitination and stress protein synthesis in Mytilus trossulus occurs during recovery from tidal emersion. Mol. Mar. Biol. Biotechnol. 1996, 5:175-184.
19. Kahari V.M., Saarialho-Kere U. Matrix metalloproteinase in skin. Exp. Dermatol. 1997, 6:199-213.
20. Keller M., Sommer A.M., Pörtner H.O., Abele D. Seasonality of energetic functioning and production of reactive oxygen species by lugworm (Arenicola marina) mitochondria exposed to acute temperature changes. J. Exp. Biol. 2004, 207:2529-2538.
21. Larade K., Storey K.B. Accumulation and translation of ferritin heavy chain transcripts following anoxia exposure in a marine invertebrate. J. Exp. Biol. 2004, 207:1353-1360.
22. Le Bris N., Zbinden M., Gaill F. Processes controlling the physico-chemical micro-environments associated with Pompeii worms. Deep-Sea Res. I 2005, 52:1071-1083.
23. Mayer M.P., Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 2005, 62:670-684.
24. Meistertzheim A.L., Tanguy A., Moraga D., Thébault M.T. Identification of differentially expressed genes of the Pacific oyster Crassostrea gigas to prolonged thermal stress. FEBS J. 2007, 274:6392-6402.
25. Ojima N., Yamashita M., Watabe S. Quantitative mRNA expression profiling of heat-shock protein families in rainbow trout cells. Biochem. Biophys. Res. Commun. 2005, 329:51-57.
26. Parihar M.S., Javeri T., Hemnani T., Dubey A.K., Prakash P. Responses of superoxide dismutase, glutathione peroxidase and reduced glutathione antioxidant defenses in gills of the freshwater catfish (Heteropneustes fossilis) to short-term elevated temperature. J. Theor. Biol. 1997, 22:151-156.
27. Park C.H., Lee M.J., Ahn J., Kim S., Kim H.H., Kim K.H., Eun H.C., Chung J.H. Heat shock-induced matrix metalloproteinase (MMP)-1 and (MMP)-3 are mediated through ERK and JNK activation and via an autocrine interleukin-6 loop. J. Investig. Dermatol. 2004, 123:1012-1019.
28. Parsell D.A., Lindquist S. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 1993, 27:437-496.
29. Pfaffl M.W., Tichopad A., Prgomet C., Neuvians T.P. Determination of stable housekeeping genes, differentially regulated target genes and sample integrity: BestKeeper-Excel-based tool using pair-wise correlations. Biotechnol. Lett. 2004, 26(6):509-515.
30. Pörtner H.O. Climate variations and the physiological basis of temperature dependent biogeography: systemic to molecular hierarchy of thermal tolerance in animals. Comp. Biochem. Physiol. A 2002, 132:739-761.
31. Ravaux J., Gaill F., Le Bris N., Sarradin P.-M., Jollivet D., Shillito B. Heat shock response and temperature resistance in the deep-sea vent shrimp Rimicaris exoculata. J. Exp. Biol. 2003, 206:2345-2354.
32. Ravaux J., Toullec J.-Y., Léger N., Lopez P., Gaill F., Shillito B. First hsp70 from two hydrothermal vent shrimps, Mirocaris fortunata and Rimicaris exoculta: characterization and sequence analysis. Gene 2007, 386:162-172.
33. Ravaux J., Cottin D., Chertemps T., Hamel G., Shillito B. Hydrothermal shrimps display low expression of heat-inducible hsp70 gene in nature. Mar. Ecol. Prog. Ser. 2009, 396:153-156.
34. Sanders B.M. Stress proteins in aquatic organisms: an environmental perspective. Crit. Rev. Toxicol. 1993, 23:49-75.
35. Schmidt C., Vuillemin R., Le Gall C., Gaill F., Le Bris N. Geochemical energy sources for microbial primary production in the environment of hydrothermal vent shrimps. Mar. Chem. 2008, 108:18-31.
36. Shillito B., Le Bris N., Hourdez S., Ravaux J., Cottin D., Caprais J.-C., Jollivet D., Gaill F. Temperature resistance studies on the deep-sea vent shrimp Mirocaris fortunata. J. Exp. Biol. 2006, 209:945-955.
37. Simon P. Q-gene: processing quantitative real-time RT-PCR data. Bioinformatics 2003, 19:1439-1440.
38. Somero G.N. Proteins and temperature. Ann. Rev. Physiol. 1995, 57:43-68.
39. Sørensen J.G., Kristensen T.N., Loeschcke V. The evolutionary and ecological role of heat shock proteins. Ecol. Lett. 2003, 6:1025-1037.
40. Teranishi K.S., Stillman J.H. A cDNA microarray analysis of the response to heat stress in hepatopancreas tissue of the porcelain crab Petrolisthes cinctipes. Comp. Biochem. Physiol. D 2007, 2:53-62.
41. Tomanek L., Sanford E. Heat shock protein 70 (HSP70) as a biochemical stress indicator: an experimental field test in two congeneric intertidal gastropods (genus: Tegula). Biol. Bull. 2003, 205:276-284.
42. Ursic D., Culbertson M.R. Is yeast TCP1 a chaperonin?. Nature 1992, 356:392.
43. Vandesompele J., De Preter K., Pattyn F., Poppe B., Van Roy N., De Paepe A., Speleman F. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiples internal control genes. Genome Biol. 2002, 3(7). RESEARCH0034.
44. Vazquez J., Pauli D., Tissières A. Transcriptional regulation in Drosophila during heat shock: a nuclear run-on analysis. Chromosoma 1993, 102:233-238.
45. Whitesell L., Lindquist S. HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 2005, 5:761-772.
46. Woessner J.F. Role of matrix proteases in processing enamel protein. Connect. Tissue Res. 1998, 39:69-73.
47. Xu J., Wu S., Zhang X. Novel function of QM protein of shrimp (Penaeus japonicus) in regulation of phenol oxidase activity by interaction with hemocyanin. Cell. Physiol. Biochem. 2008, 21:473-480.
48. Zhao R., Houry W.A. Hsp90: a chaperone for protein folding and gene regulation. Biochem. Cell. Biol. 2005, 83:703-710.