A new heat shock protein 70 gene (HSC70) and its expression profiles in response to cadmium stress and after different post-moulting times in Exopalaemon carinicauda (Holthuis, 1950) (Decapoda, Palaemonidae)

in Crustaceana
Restricted Access
Get Access to Full Text
Rent on DeepDyve

Have an Access Token?

Enter your access token to activate and access content online.

Please login and go to your personal user account to enter your access token.


Have Institutional Access?

Access content through your institution. Any other coaching guidance?


In this study, the full-length cDNA sequence (GenBank accession number AGF80339.1) encoding a novel heat shock protein HSP70 family member (Heat shock cognate 70, EcHSC70) was cloned from the ridgetail white prawn, Exopalaemon carinicauda (Holthuis, 1950) [currently also as: Palaemon carinicauda Holthuis, 1950]. EcHSC70 full-length cDNA consists of 2452 bp, containing an open reading frame (ORF) of 1935 bp, and it encodes a 650-amino-acid protein with a theoretical size of about 71 kDa and a predicted isoelectric point of 5.32. Phylogenetic analysis showed that EcHSC70 can be categorized together with the known HSP70 family members reported in other crustaceans. Tissue-expression analysis revealed that EcHSC70 was constitutively expressed in all of the tested tissues, with a significantly increased expression in the gill post-moulting. Moreover, the relative mRNA level of EcHSC70 tended to increase in the early stages of post-moulting (from 0 to 5 min), suggesting that EcHSC70 might take part in the recovery of E. carinicauda after moulting. In addition, under different levels of cadmium stress, EcHSC70 tended to be significantly expressed only after 24 h of cadmium exposure, and was more inducible by low concentrations of cadmium, as opposed to high concentrations.

A new heat shock protein 70 gene (HSC70) and its expression profiles in response to cadmium stress and after different post-moulting times in Exopalaemon carinicauda (Holthuis, 1950) (Decapoda, Palaemonidae)

in Crustaceana



BoutetI.TanguyA.RousseauS.AuffretM.MoragaD.2003. Molecular identification and expression of heat shock cognate 70 (hsc70) and heat shock protein 70 (hsp70) genes in the Pacific oyster Crassostrea gigas. Cell Stress & Chaperones8: 76-85.

BukauB.DeuerlingE.PfundC.CraigE. A.2000. Getting newly synthesized proteins into shape. Cell101: 119-122.

BukauB.HorwichA. L.1998. The Hsp70 and Hsp60 chaperone machines. Cell92: 351-366.

CarlosA. G.DanielaB.SeleneZ.2002. Heat shock cognate protein 70 is involved in rotavirus cell entry. Journal of Virology76: 4096-4102.

CesarJ. R. O.YangJ.2007. Expression patterns of ubiquitin, heat shock protein 70, α-actin and β-actin over the molt cycle in the abdominal muscle of marine shrimp Litopenaeus vannamei. Molecular Reproduction and Development74: 554-559.

ChuangK. H.HoS. H.SongY. L.2007. Cloning and expression analysis of heat shock cognate 70 gene promoter in tiger shrimp (Penaeus monodon). Gene405: 10-18.

Clavero-SalasA.Sotelo-MundoR. R.Gollas-GalvanN.Hernandez-LopezJ.Peregrino-UriarteA. B.Muhlia-AlmazanA.Yepiz-PlascenciaG.2007. Transcriptome analysis of gills from the white shrimp Litopenaeus vannamei infected with white spot syndrome virus. Fish Shellfish Immunology23: 459-472.

DeanR. J.ShimmieldT. M.BlackK. D.2007. Copper, zinc and cadmium in marine cage fish farm sediments: an extensive survey. Environmental Pollution145: 84-95.

FederM. E.HofmannG. E.1999. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annual Review of Physiology61: 243-282.

GeorgopoulosC.WelchW. J.1993. Role of the major heat shock proteins as molecular chaperones. Annual Review of Cell Biology9: 601-634.

GilbertL. I.GrangerN. A.RoeR. M.2000. The juvenile hormones: historical facts and speculations on future research directions. Insect Biochemistry and Molecular Biology30: 617-644.

GuntherE.WalterL.1994. Genetic aspects of the hsp70 multi-family in vertebrates. Experientia50: 987-1001.

HartlF. U.1996. Molecular chaperones in cellular protein folding. Nature381: 571-579.

HolthuisL. B.1950. The Decapoda of the Siboga Expedition. Part X. The Palaemonidae collected by the Siboga and Snellius expeditions with remarks on other species. I. Subfamily Palaemoninae. Siboga Expeditie Monographie 39a9: 1-268.

HolthuisL. B.1980. FAO species catalogue. Shrimps and prawns of the world: an annotated catalogue of species of interest to fisheries. FAO Fisheries Synopsis 125: 1-271. (FAORome).

HubermanA.2000. Shrimp endocrinology: a review. Aquaculture191: 191-208.

JiangX.GuanX.YaoL.ZhangH.JinX.HanY.2015. Effects of single and joint subacute exposure of copper and cadmium on heat shock proteins in common carp (Cyprinus carpio). Biological Trace Elements Research169: 374-381.

JiaoC.WangZ.LiF.ZhangC.XiangJ.2004. Cloning, sequencing and expression analysis of cDNA encoding a constitutive heat shock protein 70 (HSC70) in Fenneropenaeus chinensis. Chinese Science Bulletin49: 2385-2393.

Karouna-RenierN. K.ZehrJ. P.2003. Short-term exposures to chronically toxic copper concentrations induce HSP70 proteins in midge larvae (Chironomus tentans). The Science of the Total Environment312: 267-272.

KregelK. C.2002. Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. Journal of Applied Physiology92: 2177-2186.

LarkinM. A.BlackshieldsG.BrownN. P.ChennaR.McgettiganP. A.McwilliamH.ValentinF.WallaceI. M.WilmA.LopezR.ThompsonJ. D.GibsonT. J.HigginsD. G.2007. Clustal W and Clustal X version 2.0. Bioinformatics23: 2947-2948.

LewisS.DonkinM. E.DepledgeM. H.2001. Hsp70 expression in Enteromorpha intestinalis (Chlorophyta) exposed to environmental stressors. Aquatic Toxicology51: 277-291.

LiangJ. P.LiJ.LiuP.LiJ.ChenP.2012. Research progress of biological characteristics and artificial breeding of ridgetail white prawn, Exopalaemon carinicauda. Chinese Agricultural Science Bulletin28: 109-116.

LindquistS.CraigE. A.1988. The heat-shock proteins. Annual Review of Genetics22: 631-677.

LoW. Y.LiuK. F.LiaoI. C.SongY. L.2004. Cloning and molecular characterization of heat shock cognate 70 from tiger shrimp (Penaeus monodon). Cell Stress & Chaperones9: 332-343.

LuanW.LiF.ZhangJ.WenR.LiY.XiangJ.2010. Identification of a novel inducible cytosolic Hsp70 gene in Chinese shrimp Fenneropenaeus chinensis and comparison of its expression with the cognate Hsc70 under different stresses. Cell Stress & Chaperones15: 83-93.

MoseleyP. L.1997. Heat shock proteins and heat adaptation of the whole organism. Journal of Applied Physiology83: 1413-1417.

MulthoffG.2007. Heat shock protein 70 (Hsp70): membrane location, export and immunological relevance. Methods43: 229-237.

ParsellD. A.LindquistS.1993. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annual Review of Genetics27: 437-496.

QianZ.LiuX.WangL.WangX.LiY.XiangJ.WangP.2012. Gene expression profiles of four heat shock proteins in response to different acute stresses in shrimp, Litopenaeus vannamei. Comparative Biochemistry and Physiology Part C156: 211-220.

QianZ.MiX.WangX.HeS.LiuY.HouF.LiuQ.LiuX.2013. cDNA cloning and expression analysis of myostatin/GDF11 in shrimp, Litopenaeus vannamei. Comparative Biochemistry and Physiology Part A165: 30-39.

RanfordJ. C.HendersonB.2002. Chaperonins in disease: mechanisms, models, and treatments. Journal of Clinical Pathology: Molecular Pathology55: 209-213.

RiddifordL. M.HirumaK.ZhouX.NelsonC. A.2003. Insights into the molecular basis of the hormonal control of molting and metamorphosis from Manduca sexta and Drosophila melanogaster. Insect Biochemistry and Molecular Biology33: 1327-1338.

SchmittgenT. D.LivakK. J.2008. Analyzing real-time PCR data by the comparative CT method. Nature Protocols3: 1101-1108.

TempletonD. M.LiuY.2010. Multiple roles of cadmium in cell death and survival. Chemico-Biological Interaction188: 267-275.

WebsterS. G.KellerR.1986. Purification, characterization and amino acid composition of the putative moult-inhibiting hormone (MIH) of Carcinus maenas (Crustacea, Decapoda). Journal of Comparative Physiology Part B156: 611-624.

WhiteleyN. M.El-HajA. J.1997. Regulation of muscle gene expression over the moult in Crustacea. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology117: 323-331.

WiteskaM.JezierskaB.ChaberJ.1995. The influence of cadmium on common carp embryos and larvae. Aquaculture129: 129-132.

XuW.XieJ.ShiH.LiC.2010. Hematodinium infections in cultured ridgetail white prawns, Exopalaemon carinicauda, in eastern China. Aquaculture300: 25-31.

ZhangJ.WangJ.GuiT.SunZ.XiangJ.2014. A copper-induced metallothionein gene from Exopalaemon carinicauda and its response to heavy metal ions. International Journal of Biological Macromolecules70: 246-250.

ZhengW. W.YangD. T.WangJ. X.SongQ. S.GilbertL. I.ZhaoX. F.2010. Hsc70 binds to ultraspiracle resulting in the upregulation of 20-hydroxyecdsone-responsive genes in Helicoverpa armigera. Molecular and Cellular Endocrinology315: 282-291.


  • View in gallery

    Full-length cDNA sequence and deduced amino-acid sequence of EcHSC70 in Exopalaemon carinicauda (Holthuis, 1950). The initiation codon (ATG) and the stop codon (TAG) are boxed. The poly(A) signal (AATAAA) is indicated by a wavy underlining.

  • View in gallery

    Phylogenetic tree constructed with the neighbour-joining method showing the relationship of the Exopalaemon carinicauda (Holthuis, 1950) EcHSC70 amino-acid sequence with other HS70 family members from various species. Robustness was tested by 1000 bootstrap replications; the numbers at the forks indicate the bootstrap.

  • View in gallery

    Expression profiles of EcHSC70 in different tissues of Exopalaemon carinicauda (Holthuis, 1950). Tissue types are indicated in the abscissa. Each bar represents the mean ± SD (n=3). The reference gene is the 18S rRNA. Column bars with asterisks indicate values that are significantly different from the tissue of muscle (P<0.05).

  • View in gallery

    Expression profiles of EcHSC70 of Exopalaemon carinicauda (Holthuis, 1950) in response to Cd2+ stress.

  • View in gallery

    Discrepancy in the expression of EcHSC70 in Exopalaemon carinicauda (Holthuis, 1950) in different tissues at post-moulting. Each bar represents the mean ± SD (n=3). The reference gene is the 18S rRNA. Column bars with asterisk in gill indicate values that are significantly different from other tissues (P<0.05).

  • View in gallery

    Expression profiles of EcHSC70 in Exopalaemon carinicauda (Holthuis, 1950) at different times after post-moulting. Each bar represents the mean ± SD (n=3). The reference gene is the 18S rRNA. Columns with an asterisk indicate values that are significantly different from the control (P<0.05).


Content Metrics

Content Metrics

All Time Past Year Past 30 Days
Abstract Views 19 19 7
Full Text Views 80 80 50
PDF Downloads 4 4 2
EPUB Downloads 0 0 0