

FOLLOWUS
1. Key Laboratory of Experimental Marine Biology Institute of Oceanology Chinese Academy of Sciences
2. Graduate School of Chinese Academy of Sciences
3. College of Life Sciences Nankai University
网络首发:2010-03-20,
纸质出版:2010
Scan QR Code
Proteomic analysis of acute responses to copper sulfate stress in larvae of the brine shrimp, Artemia sinica[J]. 海洋湖沼学报(英文), 2010,28(2):224-232.
Zhou, Q., Wu, C., Dong, B. et al. Proteomic analysis of acute responses to copper sulfate stress in larvae of the brine shrimp, Artemia sinica, ., Chin. J. Ocean. Limnol. 28, 224–232 (2010). https://doi.org/10.1007/s00343-010-9232-x
Proteomic analysis of acute responses to copper sulfate stress in larvae of the brine shrimp, Artemia sinica[J]. 海洋湖沼学报(英文), 2010,28(2):224-232. DOI: 10.1007/s00343-010-9232-x.
Zhou, Q., Wu, C., Dong, B. et al. Proteomic analysis of acute responses to copper sulfate stress in larvae of the brine shrimp, Artemia sinica, ., Chin. J. Ocean. Limnol. 28, 224–232 (2010). https://doi.org/10.1007/s00343-010-9232-x DOI:
Proteomics was used to reveal the differential protein expression profiles of acute responses to copper sulfate exposure in larvae of Artemia sinica. Fourteen differentially displayed protein spots were detected and seven of them were identified. Three spots were up-expressed and identified: actin
heat shock protein 70
and chaperone subunit 1; three down-regulated proteins were identified: arginine kinase
elongation factor-2
and glycine-rich protein; and a newly expressed protein was identified as peroxiredoxin. The study indicates the involvement of all the differentially expressed proteins in the early responses of protein expression
and in the survival of A. sinica in the presence of copper and other heavy metals; the findings improve understanding of the organism’s adaptive responses and resistance.
Aust S D, Morehouse L A, Thomas C E. 1985. Role of metals in oxygen radical reactions. J. Free Radic. Biol. Med., 1: 3–25.
Barahona M V, Sanchez-Fortun S. 1999. Toxicity of carbamates to the brine shrimp Artemia salina and the effect of atropine, BW284c51, iso-OMPA and 2-PAM on carbaryl toxicity. Environ. Pollut., 104: 469–476.
Bauer H, Kanzok S M, Schirmer R H. 2002. Thioredoxin-2 but not Thioredoxin-1 is a substrate of Thioredoxin Peroxidase-1 from Drosophila melanogaster. J. Biol. Chem., 277: 17 457–17 463.
Blackstock W P, Weir M P. 1999. Proteomics: quantitative and physical mapping of cellular proteins. Trends Biotechnol., 17: 121–127.
Bradford M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72: 248–254.
Brix K V, Cardwell R D, Adams W J. 2003. Chronic toxicity of arsenic to the Great Salt Lake brine shrimp, Artemia franciscana. Ecotox. Environ. Safe, 54: 169–175.
Browne R A. 1991. Taxonomy and population genetics of Artemia. In: Browne R A, Sorgeloos P, Trotman, C N A Eds. Artemia Biology. CRC Press, Boca Raton. p. 221–235
Bryk R, Griffin P, Nathan C. 2000. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 407: 211–215.
Cai Y N. 1990. A Redescription of the brine shrimp (Artemia sinica). The Wasmann J. Biol., 47(1–2): 105–110.
Marco S, Carrascossa J L, Valpuesta J M. 1994. Reversible interaction of beta-actin along the channel of the TCP-1 cytoplasmic chaperonin. Biophys. J., 67: 364–368.
Dumas C, Camonis J. 1993. Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle. J. Biol. Chem., 268: 21 599–21 605.
Ellington W R. 1989. Phosphocreatine represents a thermodynamic and functional improvement over other muscle phosphagens. J. Exp. Biol., 143: 143–177.
Feder M E, Hofmann G E. 1999. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol., 61: 243–282.
Fountoulakis M. 2001. Proteomics: Current technologies and applications in neurological disorders and toxicology. Amino Acids, 21: 363–381.
Fujii J, Ikeda Y. 2002. Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein. Redox Rep. 7: 123–130.
Gaetke L M, Chow C K. 2003. Copper toxicity, oxidative stress, and antioxidant nutrients. Toxicology, 189: 147–163.
Garcia-Rodriguez S, Arguelles S, Llopis R, Murillo M L, Machado A, Carreras O, Ayala A. 2003. Effect of prenatal exposure to ethanol on hepatic elongation factor-2 and proteome in 21 d old rats: protective effect of folic acid. Free Radic. Bio. Med., 425: 428–437.
Gething M J, Sambrook J. 1992. Protein folding in the cell. Nature, 355: 33–45.
Halliwell B, Gutteridge J M C. 1984. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J., 219: 1–14.
Hartl F U. 1996. Molecular chaperones in cellular protein folding. Nature, 381: 571–580.
Henkle-Duhrsen K, Kampkotter A. 2001. Antioxidant enzyme families in parasitic nematodes. Mol. Biochem. Parasitol., 114: 129–142.
Herman I M. 1993. Actin isoforms. Curr. Opin. Cell Biol., 5: 48–55.
Kim Y K, Yoo W I, Lee S H, Lee M Y. 2005. Proteomic Analysis of Cadmium-Induced Protein Profile Alterations from Marine Alga Nannochloropsis oculata. Ecotoxicology, 14: 589–596.
Kotlyar S, Weihrauch D, Paulsen R S, Towle D W. 2000. Expression of arginine kinase enzymatic activity and mRNA in gills of the euryhaline crabs Carcinus maenas and Callinectes sapidus. J. Exp. Biol., 20: 2 395–2 404.
Kubota H, Hynes G, Carne A, Ashworth A, Willison K. 1994. Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin. Curr. Biol., 4: 89–99.
Mayer M P, Bukau B. 1998. Hsp70 chaperone systems: diversity of cellular functions and mechanism of action. Biol. Chem., 379: 261–268.
Nunes B S, Carvalho F D, Guilhermino L M, Van Stappen G. 2006. Use of the genus Artemia in ecotoxicity testing. Environ. Pollut., 144: 453–462.
Pandey A, Mann M. 2000. Proteomics to study genes and genomes. Nature 405, 837–846.
Radyuk S N, Sohal R S, Orr W C. 2003. Thioredoxin peroxidases can foster cytoprotection or cell death in response to different stressors: over-and under-expression of thioredoxin peroxidase in Drosophila cells. Biochem. J., 371: 743–752.
Righetti P G, Castagna A, Antonucci F, Piubelli C, Cecconi D, Campostrini N, Rustichelli C, Antonioli P, Zanusso G, Monaco S. 2005. Proteome analysis in the clinical chemistry laboratory: Myth or reality? Clin. Chim. Acta, 357: 123–139.
Sachetto-Martins G, Franco L O, de Oliveira D E. 2000. Plant glycine-rich proteins: a family or just proteins with a common motif? Biochim. Biophys. Acta, 1 492: 1–14.
Sarabia R, Del Ramo J, Varo I, Díaz-Mayans J, Torreblanca A. 2002. Comparing the acute response to cadmium toxicity of nauplii from different populations of Artemia. Environ. Toxicol. and Chem., 21: 437–444.
Sarabia R, Torreblanca A, Del Ramo J J, Daz-Mayans J. 1998. Effects of low mercury concentration exposure on hatching, growth and survival in the Artemia strain La Mata parthenogenetic diploid. Comp. Biochem. Phys. A, 120: 93–97.
Shanmuganathan A, Avery S V, Willetts S A, Houghton J E. 2004. Copper-induced oxidative stress in Saccharomyces cerevisiae targets enzymes of the glycolytic pathway. FEBS Lett., 556: 253–259.
Shepard J L, Olsson B, Tedengren M, Bradley B P. 2000. Protein expression signatures identified in Mytilus edulis exposed to PCBs, copper and salinity stress. Mar. Environ. Res., 50: 337–340.
Shevchenko A, Jensen O N, Podtelejnikov A V, Sagliocco F, Wilm M, Vorm O, Mortensen P, Shevchenko A, Boucherie H, Mann M. 1996. Linking genome and proteome by mass spectrometry: Large-scale identification of yeast proteins from two dimensional gels. Proc. Natl. Acad. Sci. USA., 25: 14 440–14 445.
Shrader E A, Henry T R, Greeley M S, Bradley B P. 2003. Proteomics in Zebrafish Exposed to Endocrine Disrupting Chemicals. Ecotoxicology, 14: 485–488.
Silvestre F, Dierick J F, Dumont V, Dieu M, Raes M, Devos P. 2005. Differential protein expression profiles in anterior gills of Eriocheir sinensis during acclimation to cadmium. Aquat. Toxicol., 76: 46–58.
Spiess C, Meyer A S, Reissmann S, Frydman J. 2004. Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. TRENDS Cell Biol., 14: 598–604.
Uriu-Adams J Y, Keen C L, 2005. Copper, oxidative stress, and human health. Keen Mol. Med., 26: 268–298.
Victoria Barahona M, Sanchez-Fortun S. 2007. Protective effect induced by atropine, carbamates, and 2-pyridine aldoxime methoiodide Artemia salina larvae exposed to fonofos and phosphamidon. Ecotoxicol Environ. Safe, 66: 65–73.
Wang S B, Chen F, Sommerfeld M, Hu Q. 2004. Proteomic analysis of molecular response to oxidative stress by the green alga Haematococcus pluvialis (Chlorophyceae). Planta, 220: 17–29.
Warner A H. 1989. Cell and Molecular Biology of Artemia Development. Plenum. New York.
Wood Z A, Schroder E, Robin Harris J, Poole L B. 2003. Structure, mechanism and regulation of peroxiredoxins. Trends biochem. Sci., 28: 32–40.
Yu B P. 1994. Cellular defenses against damage from reactive oxygen species. Physiol. Rev., 74: 139–162.
0
浏览量
3
Downloads
15
CSCD
关联资源
相关文章
相关作者
相关机构

京公网安备11010802024621