Molecular cloning, characterization and gene expression of an antioxidant enzyme catalase (MrCat) from Macrobrachium rosenbergii

Fish and Shellfish Immunology

Volumn 32, Issue 5, 2012, Pages 670-682

  Arockiaraj, Jesu ^a   Easwvaran, Sarasvathi ^a   Vanaraja, Puganeshwaran ^a   Singh, Arun ^b   Othman, Rofina Yasmin ^a   Bhassu, Subha ^a  

^a UNIVERSITY OF MALAYA   (Malaysia)

^b ST XAVIER S COLLEGE AUTONOMOUS   (India)

Author keywords

Catalase; Gene expression; IHHNV; Macrobrachium rosenbergii; Protein characterization

Indexed keywords

ESCHERICHIA COLI; INFECTIOUS HYPODERMAL AND HEMATOPOIETIC NECROSIS VIRUS; MACROBRACHIUM ROSENBERGII;

EID: 84863415661     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2012.01.013     Document Type: Article

References (75)

1. Sun Y. Free radicals, antioxidant enzymes, and carcinogenesis. Free Radic Biol Med 1990, 8:583-599.
2. Sohal R.S., Orr W.C. Relationship between antioxidants, proxidants, and the aging process. Ann NY Acad Sci 1992, 663:74-84.
3. Gerhard G.S., Kauffman E.J., Grundy M.A. Molecular cloning and sequence analysis of the Danio rerio catalase gene. Comp Biochem Physiol Part B 2000, 127:447-457.
4. Barnham K.J., Masters C.L., Bush A.I. Neurodegenerative diseases and oxidative stress. Nat Rev Drug Discov 2004, 3:205-214.
5. Cantara S., Donnini S., Giachetti A., Thorpe P.E., Ziche M. Exogenous BH4/Bcl-2 peptide reverts coronary endothelial cell apoptosis induced by oxidative stress. J Vasc Res 2004, 41:202-207.
6. Droge W. Oxidative stress and aging. Adv Exp Med Biol 2003, 543:191-200.
7. Hansberg W., Aguirre J. Hyperoxidant states cause microbial cell differentiation by cell isolation from dioxygen. J Theor Biol 1990, 142:201-221.
8. 2 signaling in human alveolar macrophages. Am J Respir Cell Mol Biol 2004, 31:43-53.
9. Paris S., Wysong D., Debeaupuis J.P., Shibuya K., Philippe B., Diamond R.D., et al. Catalases of Aspergillus fumigatus. Infect Immun 2003, 71:3551-3562.
10. Fridovich I. Superoxide dismutases. Adv Enzymol Relat Areas Mol Biol 1986, 58:61-97.
11. Fridovich I. Superoxide radical and superoxide dismutase. Ann Rev Biochem 1995, 64:97-112.
12. Bauer H., Kanzok S.M., Schirmer R.H. Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin peroxidase-1 from Drosophila melanogaster. J Biol Chem 2002, 277:17457-17463.
13. Switala J., Loewen P.C. Diversity of properties among catalases. Arch Biochem Biophys 2002, 401:145-154.
14. Chance B., Sies H., Boveris A. Hydrogen peroxide metabolism in mammalian organs. Physiol Rev 1979, 59:527-605.
15. Kim B.Y., Kim H.J., Lee K.S., Seo S.J., Jin B.R. Catalase from the white-spotted flower chafer, Protaetia brevitarsis: cDNA sequence, expression, and functional characterization. Comp Biochem Physiol Part B 2008, 149:183-190.
16. Chelikani P., Fita I., Loewen P.C. Diversity of structures and properties among catalases. Cell Mol Life Sci 2004, 61:192-208.
17. Ho Y.S., Xiong Y., Ma W., Spector A., Ho D. Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury. J Biol Chem 2004, 279:32804-32812.
18. Muradian K.K., Utko N.A., Fraifeld V., Mozzhukhina T.G., Pishel I.N., Litoshenko A.Y. Superoxide dismutase, catalase and glutathione peroxidase activities in the liver of young and old mice: linear regression and correlation. Arch Gerontol Geriatr 2002, 35:205-214.
19. Igarashi T., Kono Y., Tanaka K. Molecular cloning of manganese catalase from Lactobacillus plantarum. J Biol Chem 1996, 271:29521-29524.
20. Fowler T., Rey M.W., Vaha-Vahe P., Power S.D., Berka R.M. The catR gene encoding a catalase from Aspergillus niger: primary structure and elevated expression through increased gene copy number and use of a strong promoter. Mol Microbiol 1993, 9:989-998.
21. Klotz M.G., Klassen G.R., Loewen P.C. Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol Biol Evol 1997, 14:951-958.
22. Kawasaki L., Aguirre J. Multiple catalase genes are differentially regulated in Aspergillus nidulans. J Bacteriol 2001, 183:1434-1440.
23. Diaz A., Rangel P., Montes de Oca Y., Lledias F., Hansberg W. Molecular and kinetic study of catalase-1, a durable large catalase of Neurospora crassa. Free Radic Biol Med 2001, 31:1323-1333.
24. Scherer M., Wei H., Liese R., Fischer R. Aspergillus nidulans catalase-peroxidase gene (cpeA) is transcriptionally induced during sexual development through the transcription factor StuA. Eukaryot Cell 2002, 1:725-735.
25. Michan S., Lledias F., Baldwin J.D., Natvig D.O., Hansberg W. Regulation and oxidation of two large monofunctional catalases. Free Radic Biol Med 2002, 33:521-532.
26. Varnado C.L., Hertwig K.M., Thomas R., Roberts J.K., Goodwin D.C. Properties of a novel periplasmic catalase-peroxidase from Escherichia coli O157:H7. Arch Biochem Biophys 2004, 421:166-174.
27. Hisada H., Hata Y., Kawato A., Abe Y., Akita O. Cloning and expression analysis of two catalase genes from Aspergillus oryzae. J Biosci Bioeng 2005, 99:562-568.
28. David M., Munaswamy V., Halappa R., Marigoudar S.R. Impact of sodium cyanide on catalase activity in the freshwater exotic carp, Cyprinus carpio (Linnaeus). Pestic Biochem Physiol 2008, 92:15-18.
29. Kim J., Kim S., An K.W., Choi C.Y., Lee S., Choi K. Molecular cloning of Daphnia magna catalase and its biomarker potential against oxidative stresses. Comp Biochem Physiol Part C 2010, 152:263-269.
30. Putnam C.D., Arvai A.S., Bourne Y., Tainer J.A. Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J Mol Biol 2000, 296:295-309.
31. Smith V., Brown J., Hauton C. Immunostimulation in crustaceans: does it really protect against infection?. Fish Shellfish Immunol 2003, 15:71-90.
32. Kashiwagi A., Kashiwagi K., Takase M., Hanada H., Nakamura M. Comparison of catalase in diploid and haploid Rana rugosa using heat and chemical inactivation techniques. Comp Biochem Physiol Part B 1997, 118:499-503.
33. Manduzio H., Monsinjon T., Galap C., Leboulenger F., Rocher B. Seasonal variations in antioxidant defences in blue mussels Mytilus edulis collected from a polluted area: major contributions in gills of an inducible isoform of Cu/Zn-superoxide dismutase and of glutathione S-transferase. Aqua Toxicol 2004, 7:83-93.
34. Li C., Ni D., Song L., Zhao J., Zhang H., Li L. Molecular cloning and characterization of a catalase gene from Zhikong scallop Chlamys farreri. Fish Shellfish Immunol 2008, 24:26-34.
35. Xilan Y., Gang L., Chungen W., Baoqing H., Lirong D., Pengzu P., et al. A catalase from the freshwater mussel Cristaria plicata with cloning, identification and protein characterization. Fish Shellfish Immunol 2011, 31:389-399.
36. Mackay M., Bewley G.C. The genetics of catalase in Drosophila melanogaster: isolation and characterization of acatalasemic mutants. Genetics 1989, 22:643-652.
37. Bryant D.D., Wilson G.N. Differential evolution and expression of murine peroxisomal membrane protein genes. Biochem Mol Med 1995, 55:22-30.
38. McClung C.R. Regulation of catalases in Arabidopsis. Free Radic Biol Med 1997, 23:489-496.
39. Storz G., Tartaglia L.A. OxyR: a regulator of antioxidant genes. J Nutr 1992, 122:627-630.
40. Campa-Córdova A.I., Hernández-Saaverdra N.Y., De Philippis R., Ascencio F. Generation of superoxide anion and SOD activity in hemocytes and muscle of American white shrimp (Litopenaeus vannameii) as a response to b-glucan and sulphated polysaccharide. Fish Shellfish Immunol 2002, 12:353-366.
41. Mohankumar K., Ramasamy P. White spot syndrome virus infection decreases the activity of antioxidant enzymes in Fenneropenaeus indicus. Virus Res 2006, 115:69-75.
42. Mathew S., Kumar A.K., Anandan R., Nair V.P.G., Devadasan K. Changes in tissue defence system in white spot syndrome virus (WSSV) infected Penaeus monodon. Comp Biochem Physiol Part C 2007, 145:315-320.
43. Chongsatja P.O., Bourchookarn A., Lo C.F., Thongboonkerd V., Krittanai C. Proteomic analysis of differentially expressed proteins in Penaeus vannamei hemocytes upon Taura syndrome virus infection. Proteomics 2007, 7:3592-3601.
44. Zhang Q., Li F., Zhang X., Dong B., Zhang J., Xie Y., et al. cDNA cloning, characterization and expression analysis of the antioxidant enzyme gene, catalase, of Chinese shrimp Fenneropenaeus chinensis. Fish Shellfish Immunol 2008, 24:584-591.
45. Arockiaraj J., Vanaraja P., Easwvaran S., Singh A., Alinejaid T., Othman R.Y., et al. Gene profiling and characterization of arginine kinase-1 (MrAK-1) from freshwater giant prawn (Macrobrachium rosenbergii). Fish Shellfish Immunol 2011, 31:81-89.
46. Arockiaraj J., Easwvaran S., Vanaraja P., Singh A., Othman R.Y., Bhassu S. Prophenoloxidase activating enzyme-III from giant freshwater prawn Macrobrachium rosenbergii: characterization, expression and specific enzyme activity. Mol Biol Rep 2012, 39:1377-1386.
47. Bairoch A., Bucher P., Hofmann K. The PROSITE data base, its status in 1997. Nucleic Acid Res 1997, 25:217-221.
48. Pearson W.R. Rapid and sensitive sequence comparison with FASTP and FASTA. Meth Enzymol 1990, 183:63-98.
49. Thompson J.D., Higgins D.G., Gibson T.J. Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acid Res 1994, 22:4673-4680.
50. Arnold K., Bordoli L., Kopp J., Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 2006, 22:195-201.
51. Dhar A.K., Bowers R.M., Licon K.S., Veazey G., Read B. Validation of reference genes for quantitative measurement of immune gene expression in shrimp. Mol Immunol 2009, 46:1688-1695.
52. Livak K.J., Schmittgenm T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408.
53. Sambrook J., Fritsch E.F., Maniatis T. Molecular cloning: a laboratory manual 1989, Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press, New York. 2nd ed.
54. Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of proteinedye binding. Anal Biochem 1976, 72:248-254.
55. Aebi H. Catalase in vitro. Meths Enzymol 1984, 105:121-126.
56. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the folin phenol reagent. J Biol Chem 1951, 193:265-275.
57. Bai J., Rodriguez A.M., Melendez J.A., Cederbaum A.I. Overexpression of catalase in cytosolic or mitochondrial compartment protects HepG2 cells against oxidative injury. J Biol Chem 1999, 274:26217-26224.
58. Garcia M.X., Foote C., van Es S., Devreotes P.N., Alexander S., Alexander H. Differential development expression and cell type specificity of Dictyostelium catalases and their response to oxidative stress and UV-light. Biochim Biophys Acta 2000, 1492:295-310.
59. Mousa H.M., Omer O.H., Ali B.H., Al-Wabel N., Ahmed S.M. Antioxidant levels in tissues of young and adult camels (Camelus dromedarius). J Physiol Biochem 2006, 62:213-218.
60. Ha E.M., Oh C.T., Ryu J.H., Bae Y.S., Kang S.W., Jang I.H., et al. An antioxidant system required for host protection against gut infection in Drosophila. Dev Cell 2005, 8:125-132.
61. Nordberg J., Arnér E.S.J. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 2001, 31:1287-1312.
62. Keller G.A., Krisans S., Gould S.J., Sommer J.M., Wang C.C., Schliebs W., et al. Evolutionary conservation of a microbody targeting signal that targets proteins to peroxisomes, glyoxysomes and glycosomes. J Cell Biol 1991, 114:893-904.
63. 2+ by sarcoplasmic-reticulum. Biochem J 1987, 245:739-749.
64. Ken C.F., Lin C.T., Wu J.L., Shaw J.F. Cloning and Expression of a cDNA coding for catalase from zebrafish (Danio rerio). J Agri Food Chem 2000, 48:2092-2096.
65. Tavares-Sánchez O.L., Gómez-Anduro G.A., Felipe-Ortega X., Islas-Osuna M.A., Sotelo-Mundo R.R., Barillas-Mury C., et al. Catalase from the white shrimp Penaeus (Litopenaeus) vannamei: molecular cloning and protein detection. Comp Biochem Physiol Part B 2004, 138:331-337.
66. Fita I., Silva A.M., Murthy M.R.N., Rossmann M.G. The refined structure of beef liver catalase at 2.5 å resolution. Acta Cryst 1986, B42:497-515.
67. Berthet S., Nykyri L.M., Bravo J., Mate M.J., Berthet-colominas C., Alzari P.M., et al. Crystallization and preliminary structural analysis of catalase A from Saccharomyces cerevisiae. Protein Sci 1997, 6:481-483.
68. Prohaszka Z., Fust G. Immunological aspects of heat-shock proteins-the optimum stress of life. Mol Immunol 2004, 41:29-44.
69. Dong C.W., Zhang Y.B., Zhang Q.Y., Gui J.F. Differential expression of three Paralichthys olivaceus Hsp40 genes in responses to virus infection and heat shock. Fish Shellfish Immunol 2006, 21:146-158.
70. Huang P.Y., Kang S.T., Chen W.Y., Hsu T.C., Lo C.F., Liu K.F., et al. Identification of the small heat shock protein, HSP21, of shrimp Penaeus monodon and the gene expression of HSP21 is inactivated after white spot syndrome virus (WSSV) infection. Fish Shellfish Immunol 2008, 25:250-257.
71. 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell 1994, 79:583-593.
72. Lambert C., Soudant P., Choquet G., Paillard C. Measurement of Crassostrea gigas hemocyte oxidative metabolism by flow cytometry and the inhibiting capacity of pathogenic vibrios. Fish Shellfish Immunol 2003, 15:225-240.
73. Liu C., Tseng M., 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 2007, 23:34-45.
74. Hass A., Brehum K., Kreft J., Goeble W. Cloning, characterization and expression of Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases. J Bacteriol 1991, 173:5159-5167.
75. Murthy M.R.N., Reid T.J., Sicignano A., Tanaka N., Rossmann M.G. Structure of beef liver catalase. J Mol Biol 1981, 152:465-499.