A thioredoxin response to the WSSV challenge on the Chinese white shrimp, Fenneropenaeus chinensis

Comparative Biochemistry and Physiology - C Toxicology and Pharmacology

Volumn 151, Issue 1, 2010, Pages 92-98

  Ren, Qian ^a   Zhang, Ran Ran ^a   Zhao, Xiao Fan ^a   Wang, Jin Xing ^a  

^a SHANDONG UNIVERSITY   (China)

Author keywords

Innate immunity; Shrimp; TRX; White spot syndrome virus (WSSV)

Indexed keywords

MESSENGER RNA; THIOREDOXIN;

3' UNTRANSLATED REGION; 5' UNTRANSLATED REGION; ARTICLE; BLOOD CELL; DOWN REGULATION; FEMALE; FENNEROPENAEUS CHINENSIS; GENE EXPRESSION; GENE SEQUENCE; GILL; HEART; HEPATOPANCREAS; INNATE IMMUNITY; INTESTINE; MALE; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; SHRIMP; STOMACH; WESTERN BLOTTING; WHITE SPOT SYNDROME VIRUS;

DECAPODA (CRUSTACEA); FENNEROPENAEUS CHINENSIS; SHRIMP WHITE SPOT SYNDROME VIRUS;

EID: 71649112581     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2009.08.012     Document Type: Article

References (54)

1. Aispuro-Hernandez E., Garcia-Orozco K.D., Muhlia-Almazan A., Del-Toro-Sanchez L., Robles-Sanchez R.M., Hernandez J., Gonzalez-Aguilar G., Yepiz-Plascencia G., and Sotelo-Mundo R.R. Shrimp thioredoxin is a potent antioxidant protein. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 148 (2008) 94-99
2. Akerman S.E., and Müller S. 2-Cys peroxiredoxin PfTrx-Px1 is involved in the antioxidant defence of Plasmodium falciparum. Mol. Biochem. Parasitol. 130 (2003) 75-81
3. Alday-Sanz V., Roque A., and Turnbull J.F. Clearing mechanisms of Vibrio vulnificus biotype I in the black tiger shrimp Penaeus monodon. Dis. Aquat. Org. 48 (2002) 91-99
4. Andersen J.F., Sanders D.A., Gasdaska J.R., Weichsel A., Powis G., and Montfort W.R. Human Thioredoxin Homodimers: Regulation by pH, Role of Aspartate 60, and Crystal Structure of the Aspartate 60→Asparagine Mutant. Biochemistry 36 (1997) 13979-13988
5. Arnold K., Bordoli L., Kopp J., and Schwede T. The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22 (2006) 195-201
6. Aruoma O.I. Free radicals, oxidative tress, and antioxidants in human health and disease. J. Amer. Oil Chem. Soc. 75 (1998) 199-212
7. Bacano Maningas M.B., Koyama T., Kondo H., Hirono I., and Aoki T. A peroxiredoxin from kuruma shrimp, Marsupenaeus japonicus, inhibited by peptidoglycan. Dev. Comp. Immunol. 32 (2008) 198-203
8. Bianchini A., and Monserrat J.M. Effects of methyl parathion on Chasmagnathus granulatus hepatopancreas: protective role of sesamol. Ecotoxicol. Environ. Saf. 67 (2007) 100-108
9. Bjornstedt M., Xue J., Huang W., Akesson B., and Holmgren A. The thioredoxin and glutaredoxin systems are efficient electron donors to human plasma glutathione peroxidase. J. Biol. Chem. 269 (1994) 29382-29384
10. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
11. Contreras-Vergara C.A., Harris-Valle C., Sotelo-Mundo R.R., and Yepiz-Plascencia G. A mu-class glutathione S-transferase from the marine shrimp Litopenaeus vannamei: molecular cloning and active-site structural modeling. J. Biochem. Mol. Toxicol. 18 (2004) 245-252
12. Du X.J., Zhao X.F., and Wang J.X. Molecular cloning and characterization of a lipopolysaccharide and beta-1,3-glucan binding protein from fleshy prawn (Fenneropenaeus chinensis). Mol. Immunol. 44 (2007) 1085-1094
13. Gómez-Anduro G.A., Barillas-Mury C.V., Peregrino-Uriarte A.B., Gupta L., Gollas-Galván T., Hernández-López J., and Yepiz-Plascencia G. The cytosolic manganese superoxide dismutase from the shrimp Litopenaeus vannamei: molecular cloning and expression. Dev. Comp. Immunol 30 (2006) 893-900
14. Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis 18 (1997) 2714-2723
15. Gutteridge J.M., and Halliwell B. Free radicals and antioxidants in the year 2000. A historical look to the future. Ann. N. Y. Acad. Sci. 899 (2000) 136-147
16. Hirota K., Matsui M., Iwata S., Nishiyama A., Mori K., and Yodoi J. AP-1transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 3633-3638
17. Hirota K., Nakamura H., Masutani H., and Yodoi J. Thioredoxin superfamily and thioredoxin-inducing agents. Ann. N. Y. Acad. Sci. 957 (2002) 189-199
18. Holmgren A. Thioredoxin. Annu. Rev. Biochem. 54 (1985) 237-271
19. Holmgren A., Johansson C., Berndt C., Lonn M.E., Hudemann C., and Lillig C.H. Thiol redox control via thioredoxin and glutaredoxin systems. Biochem. Soc. Trans. 33 (2005) 1375-1377
20. Kang C.J., Wang J.X., Zhao X.F., Yang X.M., Shao H.L., and Xiang J.H. Molecular cloning and expression analysis of Ch-penaeidin, an antimicrobial peptide from Chinese shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol. 16 (2004) 513-525
21. Kanzok S.M., Fechner A., Bauer H., Ulschmid J.K., Muller H.M., Botella-Munoz J., Schneuwly S., Schirmer R., and Becker K. Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science 291 (2001) 643-646
22. Kondo N., Ishii Y., Son A., Sakakura-Nishiyama J., Kwon Y.W., Tanito M., Nishinaka Y., Matsuo Y., Nakayama T., Taniguchi M., and Yodoi J. Cysteine-dependent immune regulation by TRX and MIF/GIF family proteins. Immunol. Lett. 29 (2004) 143-147
23. Kong C.W., Tsai K., Chin J.H., Chan W.L., and Hong C.Y. Magnolol attenuates peroxidative damage and improves survival of rats with sepsis. Shock 13 (2000) 24-28
24. Kumar S., Nei M., Dudley J., and Tamura K. MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences. Brief Bioinformatics 9 (2008) 299-306
25. Laemmli U.K. Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 227 (1970) 680-685
26. Li D.X., Du X.J., Zhao X.F., and Wang J.X. Cloning and expression analysis of an o-methyltransferase (OMT) gene from Chinese shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol 21 (2006) 284-292
27. Lillig C.H., and Holmgren A. Thioredoxin and related molecules-from biology to health and disease. Antioxid. Redox Signal 9 (2007) 25-47
28. Liu C.H., Tseng M.C., and Cheng W. Identification and cloning of the antioxidant enzyme, glutathione peroxidase, of white shrimp, Litopenaeus vannamei, and its expression following Vibrio alginolyticus infection. Fish Shellfish Immunol. 23 (2007) 34-45
29. Livak K.J., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25 (2001) 402-408
30. Masutani H., Ueda S., and Yodoi J. The thioredoxin system in retroviral infection and apoptosis. Cell Death Differ. 12 (2005) 991-998
31. Mates J.M., Perez-Gomez C., and Nunez de Castro I. Antioxidant enzymes and human diseases. Clin. Biochem. 32 (1999) 595-603
32. McEligot A.J., Yang S., and Meyskens F.L. Redox regulation by intrinsic species and extrinsic nutrients in normal and cancer cells. Annu. Rev. Nutr. 25 (2005) 261-295
33. Mohankumar K., and Ramasamy P. White spot syndrome virus infection decreases the activity of antioxidant enzymes in Fenneropenaeus indicus. Virus Res 115 (2006) 69-75
34. Moriarty-Craige S.E., and Jones D.P. Extracellular thiols and thiol/disulfide redox in metabolism. Annu. Rev. Nutr. 24 (2004) 481-509
35. Mu C., Zhao J., Wang L., Song L., Song X., Zhang H., Qiu L., Gai Y., and Cui Z. A thioredoxin with antioxidant activity identified from Eriocheir sinensis. Fish Shellfish Immunol. 26 (2009) 716-723
36. Nakamura H., Nakamura K., and Yodoi J. Redox regulation of cellular activation. Annu. Rev. Immunol. 15 (1997) 351-369
37. Powis G., and Montfort W.R. Properties and biological activities of thioredoxins. Annu. Rev. Pharmacol. Toxicol. 41 (2001) 261-295
38. Ren Q., Sun R.R., Zhao X.F., and Wang J.X. A selenium-dependent glutathione peroxidase (Se-GPx) and two glutathione S-transferases (GSTs) from Chinese shrimp (Fenneropenaeus chinensis). Comp. Biochem. Physiol. C Toxicol. Pharmacol. 149 (2009) 613-623
39. Ren Q., Xu Z.L., Wang X.W., Zhao X.F., and Wang J.X. Clip domain serine protease and its homolog respond to Vibrio challenge in Chinese white shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol. 26 (2009) 787-798
40. Saitoh M., Nishitoh H., Fujii M., Takeda K., Tobiume K., Sawada Y., Kawabata M., Miyazono K., and Ichijo H. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J. 17 (1998) 2596-2606
41. Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Research 31 (2003) 3381-3385
42. Segal A. How neutrophils kill microbes. Annu. Rev. Immunol. 23 (2005) 197-223
43. Sen C.K., and Packer L. Antioxidant and redox regulation of gene transcription. FASEB J. 10 (1996) 709-720
44. Shi X.Z., Zhao X.F., and Wang J.X. Molecular cloning and expression analysis of chymotrypsin-like serine protease from the Chinese shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol. 25 (2008) 589-597
45. Tanaka T., Hosoi F., Yamaguchi-lwai Y., Nakamura H., Masutani H., Ueda S., Nishiyama A., Takeda A., Wada H., Spyrou G., and Yodoi J. Thioredoxin-2 (TRX2) is an essential gene regulating mitochondria-dependent apoptosis. EMBO J. 21 (2002) 1695-17063
46. Tavares-Sanchez O.L., Gomez-Anduro G.A., Felipe-Ortega X., Islas-Osuna M.A., Sotelo-Mundo R.R., Barillas-Mury C., and Yepiz-Plascencia G. Catalase from the white shrimp Penaeus (Litopenaeus) vannamei: molecular cloning and protein detection. Comp. Biochem. Physiol. B 138 (2004) 331-337
47. Van Wormhoudt A., and Sellos D. Cloning and sequencing analysis of three amylase cDNAs in the shrimp Penaeus vannamei (Crustacea decapoda): evolutionary aspects. J. Mol. Evol. 42 (1996) 543-551
48. Wahl M.C., Irmler A., Hecker B., Schirmer R.H., and Becker K. Comparative structural analysis of oxidized and reduced thioredoxin from Drosophila melanogaster. J. Mol. Biol. 345 (2005) 1119-1130
49. Wang S., Zhao X.F., and Wang J.X. Molecular cloning and characterization of the translationally controlled tumor protein from Fenneropenaeus chinensis. Mol. Biol. Rep. 36 (2008) 1683-1693
50. Watson W.H., Yang X., Choi Y.E., Jones D.P., and Kehrer J.P. Thioredoxin and its role in toxicology. Toxicol. Sci. 78 (2004) 3-14
51. Yu B.P. Cellular defenses against damage from reactive oxygen species. Physiol. Rev. 74 (1994) 139-162
52. Zhang Q., Li F., Zhang J., Wang B., Gao H., Huang B., Jiang H., and Xiang J. Molecular cloning, expression of a peroxiredoxin gene in Chinese shrimp Fenneropenaeus chinensis and the antioxidant activity of its recombinant protein. Mol. Immunol. 44 (2007) 3501-3509
53. Zhang Q., Li F., Zhang X., Dong B., Zhang J., Xie Y., and Xiang J. cDNA cloning, characterization and expression analysis of the antioxidant enzyme gene, catalase, of Chinese shrimp Fenneropenaeus chinensis. Fish Shellfish Immunol. 24 (2008) 584-591
54. Zhao X.F., An X.M., Wang J.X., Du X.J., Sueda S., and Kondo H. Expression of the Helicoverpa cathepsin B-like proteinase during embryonic development. Arch. Insect Biochem. Physiol. 58 (2005) 39-46