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Renalase, a new secretory enzyme responsible for selective degradation of catecholamines: Achievements and unsolved problems

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Abstract

Renalase is a recently discovered secretory enzyme responsible for selective degradation of blood catecholamines. The review summarizes literature data on expression of this enzyme and on its structure and functions. Special attention is paid to unsolved and questionable problems including: 1) prediction of the presence of FAD in the protein structure based on amino acid sequence similarity of renalase with known FAD-dependent enzymes; 2) identity of plasma and urinary renalase; 3) mechanism underlying conversion of inactive renalase into the active form.

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References

  1. Xu, J., Li, G., Wang, P., Velazquez, H., Yao, X., Li, Y., Wu, Y., Peixoto, A., Crowley, S., and Desir, G. V. (2005) J. Clin. Invest., 115, 1275–1280.

    PubMed  CAS  Google Scholar 

  2. Luft, F. C. (2005) Cell Metab., 1, 358–360.

    Article  PubMed  CAS  Google Scholar 

  3. Boomsma, F., and Tipton, K. F. (2007) J. Neural. Transm., 114, 775–776.

    Article  PubMed  CAS  Google Scholar 

  4. Zhao, Q., Fan, Z., He, J., Chen, S., Li, H., Zhang, P., Wang, L., Hu, D., Huang, J., Qiang, B., and Gu, D. (2007) J. Mol. Med., 85, 877–885.

    Article  PubMed  CAS  Google Scholar 

  5. Ghosh, S. S., Krieg, R. J., Sica, D. A., Wang, R., Fakhry, I., and Gehr, T. (2009) Pediatr. Nephrol., 24, 367–377.

    Article  PubMed  Google Scholar 

  6. Eisenhofer, G., Kopin, I. J., and Goldstein, D. S. (2004) Pharmacol. Rev., 56, 331–349.

    Article  PubMed  CAS  Google Scholar 

  7. O’sullivan, J., Unzeta, M., Healy, J., O’sullivan, M. I., Davey, G., and Tipton, K. F. (2004) Neurotoxicology, 25, 303–315.

    Article  PubMed  CAS  Google Scholar 

  8. Klinman, J. P. (2003) Biochim. Biophys. Acta, 1647, 131–137.

    PubMed  CAS  Google Scholar 

  9. Boomsma, F., Bhaggoe, U. M., van der Houwen, A. M., and van den Meiracker, A. H. (2003) Biochim. Biophys. Acta, 1647, 48–54.

    PubMed  CAS  Google Scholar 

  10. Gokturk, C., Sugimoto, H., Blomgren, B., Roomans, G. M., Forsberg-Nilsson, K., Oreland, L., and Sjoquist, M. (2007) Am. J. Hyperten., 20, 743–750.

    Article  CAS  Google Scholar 

  11. Lin, S. Y., Wang, C. C., Lu, Y. L., Wu, W. C., and Hou, W. C. (2008) Food Chem. Toxicol., 46, 2485–2492.

    Article  PubMed  CAS  Google Scholar 

  12. Healy, J., and Tipton, K. (2007) J. Neural. Transm., 114, 777–781.

    Article  PubMed  CAS  Google Scholar 

  13. Saenko, E. L., Siverina, O. B., Basevich, V. V., and Yaropolov, A. I. (1990) Biochem. Int., 20, 1049–1058.

    PubMed  CAS  Google Scholar 

  14. Ryan, T. P., Miller, D. M., and Aust, S. D. (1993) J. Biochem. Toxicol., 8, 33–39.

    Article  PubMed  CAS  Google Scholar 

  15. Hennebry, S. C., Eikelis, N., Socratous, F., Lambert, G., Straznicky, N., and Schlaich, M. P. (2009) Hypertension, 53, 1108.

    Google Scholar 

  16. Hennebry, S. C., Eikelis, N., Socratous, F., Desir, G., Lambert, G., and Schlaich, M. P. (2010) Mol. Psychiatry, 15, 234–236.

    Article  PubMed  CAS  Google Scholar 

  17. Wang, J., Qi, S., Cheng, W., Li, L., Wang, F., Li, Y. Z., and Zhang, S. P. (2008) Mol. Biol. Rep., 35, 613–620.

    Article  PubMed  CAS  Google Scholar 

  18. Li, G., Xu, J., Wang, P., Velazquez, H., Li, Y., Wu, Y., and Desir, G. V. (2008) Circulation, 117, 1277–1282.

    Article  PubMed  CAS  Google Scholar 

  19. Xu, J., and Desir, G. V. (2007) Curr. Opin. Nephrol. Hypertens., 16, 373–378.

    Article  PubMed  CAS  Google Scholar 

  20. Desir, G. V. (2008) Curr. Opin. Nephrol. Hypertens., 17, 181–185.

    Article  PubMed  CAS  Google Scholar 

  21. Socratous, F., Eikelis, N., Hennebry, S., and Schlaich, M. P. (2009) Hypertension, 53, 1117.

    Google Scholar 

  22. Bach, A. W. J., Lan, N. C., Johnson, D. L., Abell, C. W., Bembenek, M. E., Kwan, S.-W., Seeburg, P. H., and Shih, J. C. (1988) Proc. Natl. Acad. Sci. USA, 85, 4934–4938.

    Article  PubMed  CAS  Google Scholar 

  23. Gough, J., Karplus, K., Hughey, R., and Chothia, C. (2001) J. Mol. Biol., 313, 903–919.

    Article  PubMed  CAS  Google Scholar 

  24. Cozzetto, D., Giorgetti, A., Raimondo, D., and Tramontano, A. (2008) Mol. Biotechnol., 39, 1–8.

    Article  PubMed  CAS  Google Scholar 

  25. Nandigama, R. K., and Edmondson, D. E. (2000) J. Biol. Chem., 275, 20527–20532.

    Article  PubMed  CAS  Google Scholar 

  26. Fraaije, M. W., van den Heuvel, R. H. H., van Berkel, W. J. H., and Mattevi, A. (1999) J. Biol. Chem., 274, 35514–35520.

    Article  PubMed  CAS  Google Scholar 

  27. Nishikimi, M., Kobayashi, J., and Yagi, K. (1994) Biochem. Mol. Biol. Int., 3, 313–320.

    Google Scholar 

  28. Kiuchi, K., Nishikimi, M., and Yagi, K. (1980) Biochim. Biophys. Acta, 630, 330–337.

    PubMed  CAS  Google Scholar 

  29. Adachi, J., Kumar, Ch., Zhang, Y., Olsen, J. V., and Mann, M. (2006) Genome Biol., 9, R80 (http://genomebiology.com/2006/7/9/R80).

    Article  CAS  Google Scholar 

  30. Novotny, W. F., Chassande, O., Baker, M., Lazdunski, M., and Barbry, P. (1994) J. Biol. Chem., 269, 9921–9925.

    PubMed  CAS  Google Scholar 

  31. Giarnieri, D., Costa, M. T., Giarnieri, V., and Mondovi, B. (1985) Agents Actions, 16, 249–251.

    Article  PubMed  CAS  Google Scholar 

  32. Minamiura, N., Kimura, Y., Tsujino, K., and Yamamoto, T. (1975) J. Biochem., 77, 163–169.

    PubMed  CAS  Google Scholar 

  33. Ferey-Roux, G., Perrier, J., Forest, E., Marchis-Mouren, G., Puigserver, A., and Santimone, M. (1998) Biochim. Biophys. Acta, 1388, 10–20.

    PubMed  CAS  Google Scholar 

  34. Enroth, C., Eger, B. T., Okamoto, K., Nishinoi, T., Nishino, T., and Pai, E. F. (2000) Proc. Natl. Acad. Sci. USA, 97, 10723–10728.

    Article  PubMed  CAS  Google Scholar 

  35. Deller, S., Macheroux, P., and Sollner, S. (2008) Cell. Mol. Life Sci., 65, 141–160.

    Article  PubMed  CAS  Google Scholar 

  36. Moffa, D. J., Lotspeich, F. J., and Krause, R. F. (1970) J. Biol. Chem., 245, 439–447.

    PubMed  CAS  Google Scholar 

  37. Beutler, E. (1969) J. Clin. Invest., 48, 1957–1966.

    Article  PubMed  CAS  Google Scholar 

  38. Worthington, D. J., and Rosemeyer, M. (1975) Eur. J. Biochem., 60, 459–466.

    Article  PubMed  CAS  Google Scholar 

  39. Yubisui, T., Matsuki, T., Takeshita, M., and Yoneyama, Y. (1979) J. Biochem., 85, 719–728.

    PubMed  CAS  Google Scholar 

  40. Churchich, J. E. (1984) Eur. J. Biochem., 138, 327–332.

    Article  PubMed  CAS  Google Scholar 

  41. Musayev, F. N., Di Salvo, M. L., Ko, T. P., Schirch, V., and Safo, M. K. (2003) Protein Sci., 12, 1455–1463.

    Article  PubMed  CAS  Google Scholar 

  42. Tschantz, W. R., Digits, J. A., Pyun, H. J., Coates, R. M., and Casey, P. J. (2001) J. Biol. Chem., 276, 2321–2324.

    Article  PubMed  CAS  Google Scholar 

  43. Travis, J., and Salvesen, G. S. (1983) Annu. Rev. Biochem., 52, 655–709.

    Article  PubMed  CAS  Google Scholar 

  44. Gooptu, B., and Lomas, D. A. (2009) Annu. Rev. Biochem., 78, 147–176.

    Article  PubMed  CAS  Google Scholar 

  45. Ricart-Jane, D., Casanovas, A., Jane, N., Gonzalez, M. A., Buira-Morell, I., Ribera, J., Miquel Llobera, M., and Lopez-Tejero, M. D. (2008) Cell Physiol. Biochem., 22, 525–530.

    Article  PubMed  CAS  Google Scholar 

  46. Pandini, V., Ciriello, F., Tedeschi, G., Rossoni, G., Zanetti, G., and Aliverti, A. (2010) Protein Expr. Purif., doi:10.1016/j.pep.2010.03.008.

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Correspondence to A. E. Medvedev.

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Published in Russian in Biokhimiya, 2010, Vol. 75, No. 8, pp. 1045–1054.

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Medvedev, A.E., Veselovsky, A.V. & Fedchenko, V.I. Renalase, a new secretory enzyme responsible for selective degradation of catecholamines: Achievements and unsolved problems. Biochemistry Moscow 75, 951–958 (2010). https://doi.org/10.1134/S0006297910080018

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