Cloning of bovine peroxiredoxins - Gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 136, Issue 4, 2003, Pages 943-955

  Leyens, Gregory ^a   Donnay, Isabelle ^a   Knoops, Bernard ^a  

^a UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

Author keywords

Antioxidant enzymes; Bovine; Cloning; Comparison; Expression; Mammals; Peroxiredoxin; Thioredoxin peroxidases

Indexed keywords

CYSTEINE; PEROXIREDOXIN; VALINE;

AMINO ACID SEQUENCE; ANIMAL TISSUE; BASAL METABOLIC RATE; CONFERENCE PAPER; GENE EXPRESSION PROFILING; GENE SEQUENCE; GENETIC CONSERVATION; GENETIC SIMILARITY; GENETIC VARIABILITY; MAMMAL CELL; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; ORTHOLOGY; PRIORITY JOURNAL; PROTEIN MOTIF; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SPECIES COMPARISON;

BOS; BOS TAURUS; BOVINAE; HOMO; HOMO SAPIENS; MAMMALIA; MUS; MUS MUSCULUS; MUSCULUS; PRIMATES; RATTUS; RATTUS NORVEGICUS;

EID: 0345528189     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1096-4959(03)00290-2     Document Type: Conference Paper

References (74)

1. Akiba S., Dodia C., Chen X., Fisher A.B. Characterization of acidic Ca(2+)-independent phospholipase A2 of bovine lung. Comp. Biochem. Physiol. B. Biochem. Mol. Biol. 120:(2):1998;393-404.
2. Anahory T., Dechaud H., Bennes R., Marin P., Lamb N.J., Laoudj D. Identification of new proteins in follicular fluid of mature human follicles. Electrophoresis. 23:(7-8):2002;1197-1202.
3. Araki M., Nanri H., Ejima K., et al. Antioxidant function of the mitochondrial protein SP-22 in the cardiovascular system. J. Biol. Chem. 274:(4):1999;2271-2278.
4. Bryk R., Griffin P., Nathan C. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature. 407:2000;211-215.
5. Butterfield L.H., Merino A., Golub S.H., Shau H. From cytoprotection to tumor suppression: the multifactorial role of peroxiredoxins. Antioxid. Redox Signal. 1:(4):1999;385-402.
6. Chae H.Z., Kim H.J., Kang S.W., Rhee S.G. Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res. Clin. Pract. 45:(2-3):1999;101-112.
7. Chae H.Z., Chung S.J., Rhee S.G. Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269:(44):1994;27670-27678.
8. Chae H.Z., Kim I.H., Kim K., Rhee S.G. Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae. J. Biol. Chem. 268:(22):1993;16815-16821.
9. Choi H.J., Kang S.W., Yang C.H., Rhee S.G., Ryu S.E. Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution. Nat. Struct. Biol. 5:(5):1998;400-406.
10. Cismowski M.J., Narula S.S., Armitage I.M., Chernaik M.L., Huang P.C. Mutation of invariant cysteines of mammalian metallothionein alters metal binding capacity, cadmium resistance, and 113Cd NMR spectrum. J. Biol. Chem. 266:(36):1991;24390-24397.
11. Declercq J.P., Evrard C., Clippe A., Vander Stricht D., Bernard A., Knoops B. Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. J. Mol. Biol. 311:2001;751-759.
12. Emanuelsson O., Nielsen H., Brunak S., von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300:(4):2000;1005-1016.
13. Engels W.R. Contributing software to the internet: the Amplify program. Trends Biochem. Sci. 18:1993;448-450.
14. Fisher A.B., Dodia C. Role of phospholipase A2 enzymes in degradation of dipalmitoylphosphatidylcholine by granular pneumocytes. J. Lipid. Res. 37:(5):1996;1057-1064.
15. Fisher A.B., Dodia C., Manevich Y., Chen J.W., Feinstein S.I. Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase. J. Biol. Chem. 274:(30):1999;21326-21334.
16. Frank S., Munz B., Werner S. The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene. Oncogene. 14:(18):1997;915-921.
17. Fujii J., Ikeda Y. Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein. Redox Rep. 7:(3):2002;123-130.
18. Fujii T., Fujii J., Taniguchi N. Augmented expression of peroxiredoxin VI in rat lung and kidney after birth implies an antioxidative role. Eur. J. Biochem. 268:(2):2001;218-225.
19. Haridas V., Ni J., Meager A., et al. TRANK, a novel cytokine that activates NF-kappa B and c-Jun N-terminal kinase. J. Immunol. 161:(1):1998;1-6.
20. Harris J.R., Schroder E., Isupov M.N., et al. Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography. Biochim. Biophys. Acta. 1547:(2):2001;221-234.
21. Haslekas, C., Viken, M.K., Grini, P.E., Nygaard, V., Nordgard, S.H., Meza, T.J., Aalen, R.B., 2003. Seed 1-cysteine peroxiredoxin antioxidants are not involved in dormancy, but contribute to inhibition of germination during stress. Plant Physiol, in press.
22. Hofmann B., Hecht H.J., Flohe L. Peroxiredoxins. Biol. Chem. 383:(3-4):2002;347-364.
23. Horling F., Lamkemeyer P., Konig J., et al. Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis. Plant Physiol. 131:2003;317-325.
24. Iakoubova O.A., Pacella L.A., Her H., Beier D.R. LTW4 protein on mouse chromosome 1 is a member of a family of antioxidant proteins. Genomics. 42:(3):1997;474-478.
25. Ichimiya S., Davis J.G., O'Rourke D.M., Katsumata M., Greene M.I. Murine thioredoxin peroxidase delays neuronal apoptosis and is expressed in areas of the brain most susceptible to hypoxic and ischemic injury. DNA Cell Biol. 16:(3):1997;311-321.
26. Ishii T., Kawane T., Taketani S., Bannai S. Inhibition of the thiol-specific antioxidant activity of rat liver MSP23 protein by hemin. Biochem. Biophys. Res. Commun. 216:(3):1995;970-975.
27. Ishii T., Yamada M., Sato H., et al. Cloning and characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein. J. Biol. Chem. 268:(25):1993;18633-18636.
28. Iwahara S., Satoh H., Song D.X., et al. Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol. Biochemistry. 34:(41):1995;13398-13406.
29. Jin D.Y., Chae H.Z., Rhee S.G., Jeang K.T. Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation. J. Biol. Chem. 272:(49):1997;30952-30961.
30. Jung H., Kim T., Chae H.Z., Kim K.T., Ha H. Regulation of macrophage migration inhibitory factor and thiol-specific antioxidant protein PAG by direct interaction. J. Biol. Chem. 276:(18):2001;15504-15510.
31. Kang S.W., Baines I.C., Rhee S.G. Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J. Biol. Chem. 273:(11):1998;6303-6311.
32. Kang S.W., Chae H.Z., Seo M.S., Kim K., Baines I.C., Rhee S.G. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J. Biol. Chem. 273:(11):1998;6297-6302.
33. Kawai S., Takeshita S., Okazaki M., Kikuno R., Kudo A., Amann E. Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells. J. Biochem. (Tokyo). 115:(4):1994;641-643.
34. Kim T.S., Dodia C., Chen X., et al. Cloning and expression of rat lung acidic Ca(2+)-independent PLA2 and its organ distribution. Am. J. Physiol. 274:(5 Pt 1):1998;L750-L761.
35. Knoops B., Clippe A., Bogard C., et al. Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family. J. Biol. Chem. 274:(43):1999;30451-30458.
36. Kropotov A., Sedova V., Ivanov V., et al. A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro. Eur. J. Biochem. 260:(2):1999;336-346.
37. Lee T.H., Kim S.U., Yu S.L., et al. Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice. Blood. 101:2003;5033-5038.
38. Lee S.P., Hwang Y.S., Kim Y.J., et al. Cyclophilin A binds to peroxiredoxins and activates its peroxidase activity. J. Biol. Chem. 276:(32):2001;29826-29832.
39. Lee T.H., Yu S.L., Kim S.U., et al. Characterization of the murine gene encoding 1-Cys peroxiredoxin and identification of highly homologous genes. Gene. 234:(2):1999;337-344.
40. Lim Y.S., Cha M.K., Kim H.K., et al. Removals of hydrogen peroxide and hydroxyl radical by thiol-specific antioxidant protein as a possible role in vivo. Biochem. Biophys. Res. Commun. 192:(1):1993;273-280.
41. Matsumoto A., Okado A., Fujii T., et al. Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member. FEBS Lett. 443:(3):1999;246-250.
42. Mitsumoto A., Takanezawa Y., Okawa K., Iwamatsu A., Nakagawa Y. Variants of peroxiredoxins expression in response to hydroperoxide stress. Free Radic. Biol. Med. 30:(6):2001;625-635.
43. Munz B., Frank S., Hubner G., Olsen E., Werner S. A novel type of glutathione peroxidase: expression and regulation during wound repair. Biochem. J. 326:(Pt 2):1997;579-585.
44. Neumann C.A., Krause D.S., Carman C.V., et al. Essential role for the peroxiredoxin PRDX1 in erythrocyte antioxidant defence and tumour suppression. Nature. 424:2003;556-561.
45. Oberley T.D., Verwiebe E., Zhong W., Kang S.W., Rhee S.G. Localization of the thioredoxin system in normal rat kidney. Free Radic. Biol. Med. 30:(4):2001;412-424.
46. Okado-Matsumoto A., Matsumoto A., Fujii J., Taniguchi N. Peroxiredoxin IV is a secretable protein with heparin-binding properties under reduced conditions. J. Biochem. (Tokyo). 127:(3):2000;493-501.
47. Palmiter R.D., Findley S.D., Whitmore T.E., Durnam D.M. MT-III, a brain-specific member of the metallothionein gene family. Proc. Natl. Acad. Sci. USA. 89:(14):1992;6333-6337.
48. Peshenko I.V., Shichi H. Oxidation of active center cysteine of bovine 1-Cys peroxiredoxin to the cysteine sulfenic acid form by peroxide and peroxynitrite. Free Radic. Biol. Med. 31:2001;292-303.
49. Peshenko I.V., Novoselov V.I., Evdokimov V.A., et al. Novel 28-kDa secretory protein from rat olfactory epithelium. FEBS Lett. 381:(1-2):1996;12- 14.
50. Power J.H., Nicholas T.E. Immunohistochemical localization and characterization of a rat Clara cell 26-kDa protein (CC26) with similarities to glutathione peroxidase and phospholipase A2. Exp. Lung Res. 25:(5):1999;379-392.
51. Prosperi M.T., Ferbus D., Karczinski I., Goubin G. A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins. J. Biol. Chem. 268:(15):1993;11050-11056.
52. Roise D., Schatz G. Mitochondrial presequences. J. Biol. Chem. 263:(10):1988;4509-4511.
53. Rossjohn J., McKinstry W.J., Oakley A.J., et al. Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site. Structure. 6:(3):1998;309-322.
54. Sasagawa I., Matsuki S., Suzuki Y., et al. Possible involvement of the membrane-bound form of peroxiredoxin 4 in acrosome formation during spermiogenesis of rats. Eur. J. Biochem. 268:(10):2001;3053-3061.
55. Schmidt C.J., Hamer D.H. Cloning and sequence analysis of two monkey metallothionein cDNAs. Gene. 24:(1):1983;137-146.
56. Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G. Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. J. Biol. Chem. 275:(27):2000;20346-20354.
57. Shau H., Butterfield L.H., Chiu R., Kim A. Cloning and sequence analysis of candidate human natural killer-enhancing factor genes. Immunogenetics. 40:(2):1994;129-134.
58. Shichi H., Demar J.C. Non-selenium glutathione peroxidase without glutathione S-transferase activity from bovine ciliary body. Exp. Eye Res. 50:(5):1990;513-520.
59. Shih S.F., Wu Y.H., Hung C.H., Yang H.Y., Lin J.Y. Abrin triggers cell death by inactivating a thiol-specific antioxidant protein. J. Biol. Chem. 276:(24):2001;21870-21877.
60. Sies H. Oxidative stress: oxidants and antioxidants. Exp. Physiol. 82:(2):1997;291-295.
61. Singh A.K., Shichi H. A novel glutathione peroxidase in bovine eye. Sequence analysis, mRNA level, and translation. J. Biol. Chem. 273:(40):1998;26171-26178.
62. 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 Acids Res. 22:(22):1994;4673-4680.
63. Tsuji K., Copeland N.G., Jenkins N.A., Obinata M. Mammalian antioxidant protein complements alkylhydroperoxide reductase (AhpC) mutation in Escherichia coli. Biochem. J. 307:(Pt 2):1995;377-381.
64. Vanhooren J.C., Fransen M., de Bethune B., et al. Rat pristanoyl-CoA oxidase. cDNA cloning and recognition of its C-terminal (SQL) by the peroxisomal-targeting signal 1 receptor. Eur. J. Biochem. 239:(2):1996;302-309.
65. von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:(11):1986;4683-4690.
66. Wang X., Phelan S.A., Forsman-Semb K., et al. Mice with targeted mutation of peroxiredoxin 6 develop normally but are susceptible to oxidative stress. J. Biol. Chem. 278:(27):2003;25179-25190.
67. Watabe S., Kohno H., Kouyama H., Hiroi T., Yago N., Nakazawa T. Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex. J. Biochem. (Tokyo). 115:(4):1994;648-654.
68. Wen S.T., Van Etten R.A. The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity. Genes Dev. 11:(19):1997;2456-2467.
69. Wong C.M., Chun A.C., Kok K.H., et al. Characterization of human and mouse peroxiredoxin IV: evidence for inhibition by Prx-IV of epidermal growth factor- and p53-induced reactive oxygen species. Antioxid. Redox Signal. 2:(507):2000;507-518.
70. Wood Z.A., Schroder E., Robin Harris J., Poole L.B. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28:(1):2003;32-40.
71. Wood Z.A., Poole L.B., Karplus P.A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science. 300:2003;650-653.
72. Yamamoto T., Matsui Y., Natori S., Obinata M. Cloning of a housekeeping-type gene (MER5) preferentially expressed in murine erythroleukemia cells. Gene. 80:(2):1989;337-343.
73. Yamashita H., Avraham S., Jiang S., et al. Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro. J. Biol. Chem. 274:(42):1999;29897-29904.
74. Zhou Y., Zhang W., Easton R., et al. Presenilin-1 protects against neuronal apoptosis caused by its interacting protein PAG. Neurobiol. Dis. 9:(2):2002;126-138.