Peroxiredoxin IV is a secretable protein with heparin-binding properties under reduced conditions

Journal of Biochemistry

Volumn 127, Issue 3, 2000, Pages 493-501

  Okado Matsumoto, Ayako ^a   Matsumoto, Akio ^a   Fujii, Junichi ^a,b   Taniguchi, Naoyuki ^a  

^a OSAKA UNIVERSITY MEDICAL SCHOOL   (Japan)

^b YAMAGATA UNIVERSITY   (Japan)

Author keywords

Heparin binding; Peroxiredoxin IV; Redox; Secretable protein; Thioredoxin glutathione dependent peroxidase

Indexed keywords

CALRETICULIN; HEPARAN SULFATE; HEPARIN; ISOPROTEIN; PEROXIDASE; PEROXIREDOXIN; RECOMBINANT PROTEIN; THIOREDOXIN;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELLULAR DISTRIBUTION; CONTROLLED STUDY; ENDOTHELIUM CELL; ENZYME ACTIVITY; HUMAN; HUMAN CELL; NONHUMAN; OXIDATIVE STRESS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN PROCESSING; PROTEIN SECRETION; REACTION ANALYSIS; REDUCTION; TISSUE DISTRIBUTION;

ANIMALIA; MAMMALIA; UNIDENTIFIED BACULOVIRUS;

EID: 0034073166     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022632     Document Type: Article

References (40)

1. Chae, H.Z., Robison, K., Poole, L.B., Church, G., Storz, G., and Rhee, S.G. (1994) Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc. Natl. Acad. Sci. USA 91, 7017-7021
2. Yamamoto, T., Matsui, Y., Natori, S., and Obinata, M. (1989) Cloning of a housekeeping-type gene (MER5) preferentially expressed in murine erythroleukemia cells. Gene 80, 337-343
3. Ishii, T., Yamada, M., Sato, H., Matsue, M., Taketani, S., Nakayama, K., Sugita, Y., and Bannai, S. (1993) Cloning and characterization of a 23-kDa stress-induced mouse peritoneal macrophage protein. J. Biol. Chem. 268, 18633-18636
4. Prosperi, M.T., Ferbus, D., Karczinski, I., and Goubin, G. (1993) 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, 11050-11056
5. Chae, H.Z., Uhm, T.B., and Rhee, S.G. (1994) Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc. Natl. Acad. Sci. USA 91, 7022-7026
6. Lim, Y.S., Cha, M.K., Kim, H.K., and Kim, I.H. (1994) The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions. Gene 140, 279-284
7. Watabe, S., Kohno, H., Kouyama, H., Hiroi, T., Yago, N., and Nakazawa, T. (1994) Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex. J. Biochem. 115, 648-654
8. Iwahara, S., Satoh, H., Song, D.X., Webb, J., Burlingame, A.L., Nagae, Y., and Muller-Eberhard, U. (1995) Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol. Biochemistry 34, 13398-13406
9. Jin, D.Y., Chae, H.Z., Rhee, S.G., and Jeang, K.T. (1997) Regulatory role for a novel human thioredoxin peroxidase in NF-κB activation. J. Biol. Chem. 272, 30952-30961
10. Kang, S.W., Baines, I.C., and Rhee, S.G. (1998) Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J. Biol. Chem. 273, 6303-6311
11. Kang, S.W., Chae, H.Z., Seo, M.S., Kim, K., Baines, I.C., and Rhee, S.G. (1998) Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J. Biol. Chem. 273, 6297-6302
12. Schreck, R., Rieber, P., and Baeuerle, P.A. (1991) Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κB transcription factor and HIV-1. EMBO J. 10, 2247-2258
13. Haridas, V., Ni, J., Meager, A., Su, J., Yu, G.L., Zhai, Y., Kyaw, H., Akama, K.T., Hu, J., Van Eldik, L.J., and Aggarwal, B.B. (1998) TRANK, a novel cytokine that activates NF-κB and c-Jun N-terminal kinase. J. Immunol. 161, 1-6
14. Matsumoto, A., Okado, A., Fujii, T., Fujii, J., Egashira, M., Niikawa, N., and Taniguchi, N. (1999) Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member. FEBS Lett. 443, 246-250
15. Tibell, L., Hjalmarsson, K., Edlund, T., Skogman, G., Engstrom, A., and Marklund, S.L. (1987) Expression of human extracellular superoxide dismutase in Chinese hamster ovary cells and characterization of the product. Proc. Natl. Acad. Sci. USA 84, 6634-6638
16. Yamamoto, Y. and Takahashi, K. (1993) Glutathione peroxidase isolated from plasma reduces phospholipid hydroperoxides. Arch. Biochem. Biophys. 305, 541-545
17. Fujii, J., Myint, T., Seo, H.G., Kayanoki, Y., Ikeda, Y., and Taniguchi, N. (1995) Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells. J. Neurochem. 64, 1456-1461
18. Shuvaev, V.V., Fujii, J., Kawasaki, Y., Itoh, H., Hamaoka, R., Barbier, A., Ziegler, O., Siest, G., and Taniguchi, N. (1999) Glycation of apolipoprotein E impairs its binding to heparin: identification of the major glycation site. Biochim. Biophys. Acta 1454, 296-308
19. Suzuki, K., Tatsumi, H., Satoh, S., Senda, T., Nakata, T., Fujii, J., and Taniguchi, N. (1993) Manganese-superoxide dismutase in endothelial cells: localization and mechanism of induction. Am. J. Physiol. 265, H1173-1178
20. Chae, H.Z., Chung, S.J., and Rhee, S.G. (1994) Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269, 27670-27678
21. Asahi, M., Fujii, J., Suzuki, K., Seo, H.G., Kuzuya, T., Hori, M., Tada, M., Fujii, S., and Taniguchi, N. (1995) Inactivation of glutathione peroxidase by nitric oxide. Implication for cytotoxicity. J. Biol. Chem. 270, 21035-21039
22. Philips, H.I. (1973 ) In Tissue Culture, Method and Applications pp. 407-408, Academic Press, New York
23. Houston, M., Estevez, A., Chumley, P., Aslan, M., Marklund, S., Parks, D.A., and Freeman, B.A. (1999) Binding of xanthine oxidase to vascular endothelium. Kinetic characterization and oxidative impairment of nitric oxide-dependent signaling. J. Biol. Chem. 274, 4985-4994
24. Adachi, T., Fukushima, T., Usami, Y., and Hirano, K. (1993) Binding of human xanthine oxidase to sulphated glycosaminoglycans on the endothelial-cell surface. Biochem. J. 289, 523-527
25. Asahi, M., Fujii, J., Takao, T., Kuzuya, T., Hori, M., Shimonishi, Y., and Taniguchi, N. (1997) The oxidation of selenocysteine is involved in the inactivation of glutathione peroxidase by nitric oxide donor. J. Biol. Chem. 272, 19152-19157
26. Tsunawaki, S. and Nathan, C.F. (1984) Enzymatic basis of macrophage activation. Kinetic analysis of superoxide production in lysates of resident and activated mouse peritoneal macrophages and granulocytes. J. Biol. Chem. 259, 4305-4312
27. Ailor, E. and Betenbaugh, M.J. (1999) Modifying secretion and post-translational processing in insect cells. Curr. Opin. Biotech. 10, 142-145
28. Hsu, T.A., Eiden, J.J., Bourgarel, P., Meo, T., and Betenbaugh, M.J. (1994) Effects of co-expressing chaperone BIP on functional antibody production in the baculovirus system. Protein Expr. Purif. 5, 595-603
29. Javis, D.L. and Garcia, A. (1994) Biosynthesis and processing of the Autographa californica nuclear polyhedrosis virus gp64 protein. Virology 205, 300-313
30. Adachi, T. and Marklund, S.I. (1989) Interactions between human extracellular superoxide dismutase C and sulfated polysaccharides. J. Biol. Chem. 264, 8537-8541
31. Adachi, T., Kodera, T., Ohta, H., Hayashi, K., and Hirano, K. (1992) The heparin binding site of human extracellular-superoxide dismutase. Arch. Biochem. Biophys. 297, 155-161
32. Liu, C.S. and Chang, J.Y. (1987) The heparin binding site of human antithrombin III. Selective chemical modification at Lys114, Lys125, and Lys287 impairs its heparin cofactor activity. J. Biol. Chem. 262, 17356-17361
33. Sies, H. and Summer, K.H. (1975) Hydroperoxide-metabolizing systems in rat liver. Eur. J. Biochem. 57, 503-512
34. Calabrese, L. and Leuzzi, U. (1984) Presence of reduced type 1 copper in ceruloplasmin as revealed by reaction with hydrogen peroxide. Biochem. Int. 8, 35-39
35. Kimn, I.G., Park, S.Y., Kim, K.C., and Yum, J.J. (1998) Thiollinked peroxidase activity of human ceruloplasmin. FEBS Lett. 431, 473-475
36. Park, Y.S., Suzuki, K., Taniguchi, N., and Gutteridge, J.M.C. (1999) Glutathione peroxidase-like activity of caeruloplasmin as an important lung antioxidant. FEBS Lett. 458, 133-136
37. Karlsson, K., Lindahl, U., and Marklund, S.L. (1988) Binding of human extracellular superoxide dismutase C to sulphated glycosaminoglycans. Biochem. J. 256, 29-33
38. Lim, H.L., Myers, B.M., Hamilton, B.A., Davis, G.L., and Lau, J.Y. (1995) Plasma glutathione concentration in patients with chronic hepatitis C virus infection. J. Viral. Hepat. 2, 211-214
39. Nakamura, H., De Rosa, S., Roederer, M., Anderson, M.T., Dubs, J.G., Yodoi, J., Holmgren, A., and Herzenberg, L.A. (1996) Elevation of plasma thioredoxin levels in HIV-infected individuals. Int. Immunol. 8, 603-611
40. Maddipati, K.R. and Marnett, L.J. (1987) Characterization of the major hydroperoxide-reducing activity of human plasma. Purification and properties of a selenium-dependent glutathione peroxidase. J. Biol. Chem. 262, 17398-17403