The proteomic study on cellular responses of the testes of zebrafish (Danio rerio) exposed to microcystin-RR

Proteomics

Volumn 12, Issue 2, 2012, Pages 300-312

  Zhao, Sujuan ^a   Xie, Ping ^a   Li, Guangyu ^a,b   Jun, Chen ^a   Cai, Yan ^a   Xiong, Qian ^a   Zhao, Yanyan ^a  

^a INSTITUTE OF HYDROBIOLOGY   (China)

^b HUAZHONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

2 DE; Animal proteomics; MC RR; Reproductive toxicity; Testis; Ultrastructure

Indexed keywords

CALCIUM ION; MICROCYSTIN RR;

ANIMAL EXPERIMENT; ARTICLE; BIOLOGICAL FUNCTIONS; CALCIUM BINDING; CELL JUNCTION; CONTROLLED STUDY; CYTOSKELETON; GLYCOLYSIS; MALE; MALE GENITAL SYSTEM; METABOLISM; MITOCHONDRION; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEOMICS; TESTIS DISEASE; ULTRASTRUCTURE; ZEBRA FISH;

ANIMALS; GLYCOLYSIS; INJECTIONS, INTRAPERITONEAL; INTERMEDIATE FILAMENT PROTEINS; LETHAL DOSE 50; MALE; MICROCYSTINS; MICROSCOPY, ELECTRON, TRANSMISSION; MITOCHONDRIA; OXIDATIVE STRESS; PROTEOME; PROTEOMICS; TESTIS; TUBULIN; ZEBRAFISH; ZEBRAFISH PROTEINS;

ANIMALIA; DANIO RERIO;

EID: 84862917943     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100214     Document Type: Article

References (63)

1. Chorus, I., Bartram, J., Toxic Cyanobacteria in Water - A Guide To Their Public Health Consequences, Monitoring and Management. E&FN Spon, London 1999, p. 416.
2. Dietrich, D., Hoeger, S., Guidance values for microcystins in water and cyanobacterial supplement products (blue-green algal supplements): a reasonable or misguided approach. Toxicol. Appl. Pharm. 2005, 203, 273-289.
3. Ross, C., Santiago-Vazquez, L., Paul, V., Toxin release in response to oxidative stress and programmed cell death in the cyanobacterium Microcystis aeruginosa. Aquat. Toxicol. 2006, 78, 66-73.
4. MacKintosh, C., Beattie, K. A., Klumpp, S., Cohen, P., Codd, G. A., Cyanobacterial microcystin-LR is a potent and specific inhibitor of protein phosphatases 1 and 2A from both mammals and higher plants. FEBS Lett. 1990, 264, 187-192.
5. Wiegand, C., Pflugmacher, S., Ecotoxicological effects of selected cyanobacterial secondary metabolites: A short review. Toxicol. Appl. Pharmacol. 2005, 203, 201-218.
6. Ding, W. X., Ong, C. N., Role of oxidative stress and mitochondrial changes in cyanobacteria-induced apoptosis and hepatotoxicity. FEMS Microbiol. Lett. 2003, 2, 1-7.
7. Li, X. Y., Chung, I. K., Kim, J. I., Lee, J. A., Oral exposure to Microcystis increases activity-augmented antioxidant enzymes in the liver of loach (Misgurnus mizolepis) and has no effect on lipid peroxidation. Comp. Biochem. Physiol. C: Toxicol. Pharmacol. 2005, 141, 292-296.
8. Li, X. Y., Wang, J., Liang, J. B., Liu, Y. D., Toxicity of microcystins in the isolated hepatocytes of common carp (Cyprinus carpio L.). Ecotoxicol. Environ. Saf. 2007, 67, 447-451.
9. Zimba, P. V., Khoo, L., Gaunt, P. S., Brittain, S. et al., Confirmation of catfish, Ictalurus punctatus (Rafinesque) mortality from Microcystis toxins. J. Fish Dis. 2001, 24, 41-47.
10. Xie, L., Xie, P., Ozawa, K., Honma, T. et al., Dynamics of microcystin- LR and -RR in the phytoplanktivorous silver carp in a subchronic toxicity experiment. Environ. Pollut. 2004, 127, 431-439.
11. El Ghazali, I., Saqrane, S., Carvalho, A. P., Ouahid, Y. et al., Compensatory growth induced in zebrafish larvae after pre-exposure to a Microcystis aeruginosa natural bloom extract containing microcystins. Int. J. Mol. Sci. 2009, 10, 133-146.
12. Anderson, R. J., Luu, H. A., Chen, D. Z. X., Holmes, C. F. B. et al., Chemical and biological evidence links microcystins to salmon "netpen liver disease". Toxicon 1993, 31, 1315-1323.
13. Xie, L., Xie, P., Guo, L. G., Li, L. et al., Organ distribution and bioaccumulation of microcystins in freshwater fishes with different trophic levels from the eutrophic Lake Chaohu, China. Environ. Toxicol. 2005, 20, 292-300.
14. Xie, L., Yokoyama, A., Nakamura, K., Park, H., Accumulation of microcystins in various organs of the freshwater snail Sinotaia histrica and three fishes in a temperate lake, the eutrophic Lake Suwa, Japan. Toxicon 2007, 49, 646-652.
15. Chen, J., Xie, P., Zhang, D., Lei, H., In situ studies on the distribution patterns and dynamics of microcystins in a biomanipulation fish - bighead carp (Aristichthys nobilis). Environ. Pollut. 2007, 147, 150-157.
16. Malbrouck, C., Trausch, G., Devos, P., Kestemont, P., Hepatic accumulation and effects of microcystin-LR on juvenile goldfish Carassius auratus L. Comp. Biochem. Physiol. C: Pharmacol. Toxicol. 2003, 135, 39-48.
17. Fischer, W. J., Dietrich, D. R., Pathological and biological characterization of microcystin-induced hepatopancreas and kidney damage in carp (Cyprinus carpio). Toxicol. Appl. Pharmacol. 2000, 164, 73-81.
18. Best, J. H., Eddy, F. B., Codd, G. A., Effects of purified microcystin- LR and cell extracts of Microcystis strains PCC 7813 and CYA 43 on cardiac function in brown trout (Salmo trutta) alevine. Fish Physiol. Biochem. 2001, 24, 171-178.
19. Funari, E., Testai, E., Human health risk assessment related to cyanotoxins exposure. Crit. Rev. Toxicol. 2008, 38, 97-125.
20. Li, Y., Sheng, J., Sha, J., Han, X., The toxic effects of microcystin- LR on the reproductive system of male rats in vivo and in vitro. Reprod. Toxicol. 2008, 26, 239-245.
21. Ding, X. S., Li, X. Y., Duan, H. Y., Chung, I. K. et al., Toxic effects of Microcystis cell extracts on the reproductive system of male mice. Toxicon 2006, 48, 973-979.
22. Xiong, Q., Xie, P., Li, Y., Hao, L. et al., Involvement of Fas/FasL system in apoptotic signaling in testicular germ cells of male Wistar rats injected i.v. with microcystins. Toxicon 2009, 54, 1-7.
23. Merrick, B. A., Toxicoproteomics in liver injury and inflammation. Ann. NY Acad. Sci. 2006, 1076, 707-717.
24. Wang, M. H., Chan, L. L., Si, M. Z., Hong, H. S. et al., Proteomic analysis of hepatic tissue of zebrafish (Danio rerio) experimentally exposed to chronic microcystin-LR. Toxicol. Sci. 2010, 113, 60-69.
25. Wang, M. H., Wang, D. Z., Lin, L., Hong, H. S., Protein profiles in zebrafish (Danio rerio) brains exposed to chronic microcystin-LR. Chemosphere 2010, 81, 716-724.
26. Wang, Q., Xie, P., Chen, J., Liang, G. D., Distribution of microcystins in various organs (Heart, Liver, Intestine, Gonad, Brain, Kidney and Lung) of Wistar rat via intravenous injection. Toxicon 2008, 52, 721-727.
27. Gad, S. C., Weil, C. S., Statistics and Experimental Design for Toxicologists. Telford Press, NJ 1988, p. 435.
28. Bayer, W. F., Fridovich, J. L., Assaying for superoxide dismutase activity: some large consequences of minor changes in conditions. Anal. Biochem. 1987, 161, 559-566.
29. Habig, W. H., Pabst, M. J., Jakoby, W. B., Glutathine-S-transferases: the first enzymatic step in mercapturic acid formation. Biol. Chem. 1974, 249, 7130-7139.
30. Habig, W. H., Jakoby, W. B., Assays for differentiation of glutathione S-transferases. Methods Enzymol. 1981, 77, 398-405.
31. Drotar, A., Phelps, P., Fall, R., Evidence for glutathione peroxidase activities in cultured plant cells. Plant Sci. 1985, 42, 35-40.
32. Griffith, O., Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Anal. Biochem. 1980, 106, 207-212.
33. Ohkawa, H., Ohishi, N., Yagi, K., Assay for lipid peroxides in animal tissues bythiobarbituric acid reaction. Anal. Biochem. 1979, 95, 351-358.
34. Tay, T. L., Lin, Q., Seow, T. K., Tan, K. H. et al., Proteomic analysis of protein profiles during early development of the zebrafish, Danio rerio. Proteomics 2006, 6, 3176-3188.
35. Li, G.Y., Chen, J., Xie, P., Jiang, Y., Wu, L.Y. et al., Protein expression profiling in the zebrafish (Danio rerio) embryos exposed to the microcystin-LR. Proteomics 2011, 11, 2003-2018.
36. Liu, Y., Xie, P., Qiu, T., Li, H. Y. et al., Microcystin extracts induce ultrastructural damage and biochemical disturbance in male rabbit testis. Environ. Toxicol. 2010, 25, 9-17.
37. Wickstrom, M. L., Khan, S. A., Haschek, W. M., Wyman, J. F. et al., Alterations in microtubules, intermediate filaments, and microfilaments induced by microcystin-LR in cultured cells. Toxicol. Pathol. 1995, 23, 326-337.
38. Howard, J., Hyman, A. A., Dynamics and mechanics of the microtubule plus end. Nature 2003, 422, 753-758.
39. Westermann, S., Weber, K., Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell. Biol. 2003, 4, 938-947.
40. Fu, W. Y., Yu, Y. N., Xu, L. H., Identification of temporal differentially expressed protein responses to microcystin in human amniotic epithelial cells. Chem. Res. Toxicol. 2009, 22, 41-51.
41. Ding, W. X., Shen, H. M., Ong, C. N., Microcystic cyanobacteria extract induces cytoskeletal disruption and intracellular glutathione alteration in hepatocytes. Environ. Health Perspect. 2000, 108, 605-609.
42. Batista, T., de Sousa, G., Suput, J. S., Rahmani, R. et al., Microcystin-lr causes the collapse of actin filaments in primary human hepatocytes. Aquat. Toxicol. 2003, 65, 85-91.
43. Fourest-Lieuvin, A., Peris, L., Gache, V., Garcia-Saez, I. et al., Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin- dependent kinase cdk1. Mol. Biol. Cell 2006, 1, 1041-1050.
44. Toivola, D. M., Goldman, R. D., Garrod, D. R., Eriksson, J. E., Protein phosphatases maintain the organization and structure interactions of hepatic keratin intermediate filaments. J. Cell Sci. 1997, 110, 23-33.
45. Winston, G. W., Di Giulio, R. T., Prooxidant and antioxidant mechanisms in aquatic organisms. Aquat. Toxicol. 1991, 19, 137-161.
46. Sies, H., Strategies of antioxidant defense. Eur. J. Biochem. 1993, 215, 213-219.
47. Chen, T., Cui, J., Liang, Y., Xin, X. B. et al., Identification of human liver mitochondrial aldehyde dehydrogenase as a potential target for microcystin-LR. Toxicology 2006, 220, 71-80.
48. Marchitti, S. A., Deitrich, R. A., Vasiliou, V., Neurotoxicity and metabolism of the catecholamine-derived 3, 4-dihydroxyphenylacetaldehyde and 3, 4- dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase. Pharmacol. Rev. 2007, 59, 125-150.
49. Wright, R. M., McManaman, J. L., Repine, J. E., Alcohol-induced breast cancer: A proposed mechanism. Free Radical. Bio. Med. 1999, 26, 348-354.
50. Lindahl, R., Aldehyde dehydrogenases and their role in carcinogensis. Crit. Rev. Biochem. Mol. Biol. 1992, 27, 283-335.
51. O'Brien, P. J., Siraki, A. G., Shangari, N., Aldehyde sources, metabolism, molecular toxicity mechanisms, and possible effects on human health. Crit. Rev. Toxicol. 2005, 35, 609-662.
52. Chopra, D., Wilkoff, L. J., Activity of retinoids against benzo(a)pyrene-induced hyperplasia in mouse prostate organ cultures. Eur. J. Cancer 1979, 15, 1417-1423.
53. Mongan, N. P., Gudas, L. J., Diverse actions of retinoid receptors in cancer prevention and treatment. Differentiation 2007, 75, 853-870.
54. Kim, H., Lapointe, J., Kaygusuz, G., Ong, D. E. et al., The retinoic acid synthesis gene ALDH1a2 is a candidate tumor suppressor in prostate cancer. Cancer Res. 2005, 65, 8118-8124.
55. Hanke, G. T., Satomi, Y., Shinmura, K., Takao, T., Hase, T., A screen for potential ferredoxin electron transfer partners uncovers new, redox dependent interactions. Biochim. Biophys. Acta 2010, 1814, 366-374.
56. Peng, J., Graham, J., Kenneth, W., Stress proteins as biomarkers of oxidative stress: effects of antioxidant supplements. Free Radical. Bio. Med. 2000, 28, 1598-1606.
57. Goldfarb, S., Kashlan, O., Watkins, J., Suaud, L. et al., Differential effects of Hsc70 and Hsp70 on the intracellular trafficking and functional expression of epithelial sodium channels. Proc. Natl. Acad. Sci. USA 2006, 103, 5817-5822.
58. Dowling, V. A., Sheehan, D., Proteomics as a route to identification of toxicity targets in environmental toxicology. Proteomics 2006, 6, 5597-5604.
59. Mezhoud, K., Bauchet, A. L., Château-Joubert, S., Praseuth, D. et al., Proteomic and phosphoproteomic analysis of cellular responses in medaka fish (Oryzias latipes) following oral gavage with microcystin-LR. Toxicon 2008, 51, 1431-1439.
60. Watanabe, D., Yamada, K., Nishina, Y., Tajima, Y. et al., Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development. J. Biol. Chem. 1994, 269, 7744-7749.
61. Murphy, M. P., How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417, 1-13.
62. Ciechanover, A., Brundin, P., The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 2003, 40, 427-446.
63. Grune, T., Reinheckel, T., Davies, K. J. A., Degradation of oxidized proteins in mammalian cells. FASEB J. 1997, 11, 526-534.