Molecular Biology Reports

, Volume 35, Issue 4, pp 613–620 | Cite as

Identification, expression and tissue distribution of a renalase homologue from mouse

  • Jian Wang
  • Shaoling Qi
  • Wei Cheng
  • Li Li
  • Fu Wang
  • Ying-Zi Li
  • Shu-Ping Zhang
Original Paper

Abstract

FAD (flavin adenine dinucleotide)-dependent monoamine oxidases play very important roles in many biological processes. A novel monoamine oxidase, named renalase, has been identified in human kidney recently and is found to be markedly reduced in patients with end-stage renal disease (ESRD). Here, we reported the identification of a renalase homologue from mouse, termed mMAO-C (mouse monoamine oxidase-C) after the monoamine oxidase-A and -B (MAO-A and -B). This gene locates on the mouse chromosome 19C1 and its coding region spans 7 exons. The deuced amino acid sequences were predicted to contain a typical secretive signal peptide and a conserved amine oxidase domain. Phylogenetic analysis and multiple sequences alignment indicated that mMAO-C-like sequences exist in all examined species and share significant similarities. This gene has been submitted to the NCBI GenBank database (Accession number: DQ788834). With expression vectors generated from the cloned mMAO-C gene, exogenous protein was effectively expressed in both prokaryotic and eukaryotic cells. Recombinant mMAO-C protein was secreted out of human cell lines, indicating the biological function of its signal peptide. Moreover, tissue expression pattern analysis revealed that mMAO-C gene is predominantly expressed in the mouse kidney and testicle, which implies that kidney and testicle are the main sources of renalase secretion. Shortly, this study provides an insight into understanding the physiological and biological functions of mMAO-C and its homologues in endocrine.

Keywords

Mouse Renalase homologue Molecular cloning Tissue distribution 

Notes

Acknowledgments

This work was supported by the grants: The National Natural Science Foundation of China (No. 30671036), the National Basic Research Program (also called 973 Program) of China (No. 2006CB705700), National High Technology Research and Development Program (also called 863 Program) of China (No. 2006AA020504) and the National Natural Science Education Foundation of China for Training Students in Biological Science (No. J0630647). We appreciate Prof. Li Liu (The Institute of Basic Medical Sciences, Peking Union Medical College) and Dr. Shaoyong Chen (BIDMC, Harvard Medical School) for discussions and suggestions in experimental design and manuscript preparation. We also appreciate Ms Hui Zhang for technical assistance.

References

  1. 1.
    Xu J, Li G, Wang P, Velazquez H et al (2005) Renalase is a novel, soluble monoamine oxidase that regulates cardiac function and blood pressure. J Clin Invest 115:1275–1280PubMedGoogle Scholar
  2. 2.
    Levey AS, Coresh J, Balk E et al (2003) National Kidney Foundation. National Kidney Foundation practice guidelines for chronic kidney disease: evaluation, classification, and stratification. Ann Intern Med 139:137–147PubMedGoogle Scholar
  3. 3.
    Chavers BM, Li S, Collins AJ, Herzog CA (2002) Cardiovascular disease in pediatric chronic dialysis patients. Kidney Int 62:648–653PubMedCrossRefGoogle Scholar
  4. 4.
    Levey AS, Andreoli SP, DuBose T et al (2007) Chronic kidney disease: common, harmful, and treatable—World Kidney Day 2007. J Am Soc Nephrol 18:374–378PubMedCrossRefGoogle Scholar
  5. 5.
    Oberg BP, McMenamin E, Lucas FL et al (2004) Increased prevalence of oxidant stress and inflammation in patients with moderate to severe chronic kidney disease. Kidney Int 65:1009–1016PubMedCrossRefGoogle Scholar
  6. 6.
    Girndt M, Kohler H, Schiedhelm-Weick E et al (1995) Production of interleukin-6, tumor necrosis factor alpha and interleukin-10 in vitro correlates with the clinical immune defect in chronic hemodialysis patients. Kidney Int 47:559–565PubMedCrossRefGoogle Scholar
  7. 7.
    Koomans HA, Blankestijn PJ, Joles JA (2004) Sympathetic hyperactivity in chronic renal failure: a wake-up call. J Am Soc Nephrol 15:524–537PubMedCrossRefGoogle Scholar
  8. 8.
    Joles JA, Koomans HA (2004) Causes and consequences of increased sympathetic activity in renal disease. Hypertension 43:699–706PubMedCrossRefGoogle Scholar
  9. 9.
    Tonelli M, Pfeffer MA (2007) Kidney disease and cardiovascular risk. Annu Rev Med 58:123–139PubMedCrossRefGoogle Scholar
  10. 10.
    Tonelli M, Wiebe N, Culleton B et al (2006) Chronic kidney disease and mortality risk: a systematic review. J Am Soc Nephrol 17:2034–2047PubMedCrossRefGoogle Scholar
  11. 11.
    Luft FC (2005) Renalase, a catecholamine-metabolizing hormone from the kidney. Cell Metab 1:358–360PubMedCrossRefGoogle Scholar
  12. 12.
    Vaughan C (2005) Renalase could even survival odds in kidney disease. National Review of Medicine 2Google Scholar
  13. 13.
    Bendtsen JD, Nielsen H, von Heijne G, Brunak S (2004) Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340:783–795PubMedCrossRefGoogle Scholar
  14. 14.
    Schnaitman C, Erwin VG, Greenawalt JW (1967) The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J Cell Biol 32:719–735PubMedCrossRefGoogle Scholar
  15. 15.
    Schnaitman C, Greenawalt JW (1968) Enzymatic properties of the inner and outer membranes of rat liver mitochondria. J Cell Biol 38:158–175PubMedCrossRefGoogle Scholar
  16. 16.
    Greenawalt JW, Schnaitman C (1970) An appraisal of the use of monoamine oxidase as an enzyme marker for the outer membrane of rat liver mitochondria. J Cell Biol 46:173–179PubMedCrossRefGoogle Scholar
  17. 17.
    Grimsby J, Chen K, Wang LJ et al (1991). Human monoamine oxidase A and B genes exhibit identical exon–intron organization. Proc Natl Acad Sci USA 88:3637–3641PubMedCrossRefGoogle Scholar
  18. 18.
    Nielsen H, Krogh A (1998) Prediction of signal peptides and signal anchors by a hidden Markov model. Proceedings of the sixth international conference on intelligent systems for molecular biology (ISMB 6). AAAI Press, California, pp 122–130Google Scholar
  19. 19.
    Marchler-Bauer A, Bryant SH et al (2004) CD-search: protein domain annotations on the fly. Nucleic Acids Res 32(Web Server issue):W327–W331PubMedCrossRefGoogle Scholar
  20. 20.
    Rost B, Yachdav G, Liu J (2004) The PredictProtein server. Nucleic Acids Res 32(Web Server issue):W321–W326PubMedCrossRefGoogle Scholar
  21. 21.
    Persson PB (2003) Renin: origin, secretion and synthesis. J Physiol 552:667–671PubMedCrossRefGoogle Scholar
  22. 22.
    Youdim MB, Bakhle YS (2006) Monoamine oxidase: isoforms and inhibitors in Parkinson’s disease and depressive illness. Br J Pharmacol 147(Suppl 1):S287–S296PubMedCrossRefGoogle Scholar
  23. 23.
    Cases O, Seif I, Grimsby J (1995) Aggressive behavior and altered amounts of brain serotonin and norepinephrine in mice lacking MAO-A. Science 268:1763–1766PubMedCrossRefGoogle Scholar
  24. 24.
    Chen K, Holschneider DP, Wu W, Rebrin I, Shih JC (2004) A spontaneous point mutation produces monoamine oxidase A/B knock-out mice with greatly elevated monoamines and anxiety-like behavior. J Biol Chem 279:39645–39652PubMedCrossRefGoogle Scholar
  25. 25.
    Shih JC, Chen K, Ridd MJ (1999) Monoamine oxidase: from genes to behavior. Annu Rev Neurosci 22:197–217PubMedCrossRefGoogle Scholar
  26. 26.
    Binda C, Mattevi A, Edmondson DE (2002) Structure-function relationships in flavoenzyme-dependent amine oxidations: a comparison of polyamine oxidase and monoamine oxidase. J Biol Chem 277:23973–23976PubMedCrossRefGoogle Scholar
  27. 27.
    Chen K (2004) Organization of MAO-A and MAO-B promoters and regulation of gene expression. Neurotoxicology 25:31–36PubMedCrossRefGoogle Scholar
  28. 28.
    Grimsby J, Lan NC, Neve R et al (1990) Tissue distribution of human monoamine oxidase A and B mRNA. J Neurochem 55:1166–1169PubMedCrossRefGoogle Scholar
  29. 29.
    Saura J, Richards JG, Mahy N (1994) Differential age-related changes of MAO-A and MAO-B in mouse brain and peripheral organs. Neurobiol Aging 15:399–408PubMedCrossRefGoogle Scholar
  30. 30.
    Saura J, Kettler R, Da Prada M, Richards JG (1992) Quantitative enzyme radioautography with 3H-Ro 41–1049 and 3H-Ro 19-6327 in vitro: localization and abundance of MAO-A and MAO-B in rats CNS, peripheral organs, and human brain. J Neurosci 12:1977–1999PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Jian Wang
    • 1
  • Shaoling Qi
    • 1
  • Wei Cheng
    • 1
  • Li Li
    • 1
  • Fu Wang
    • 1
  • Ying-Zi Li
    • 1
  • Shu-Ping Zhang
    • 1
  1. 1.Laboratory for Functional Genomic Research, Department of Biological Sciences and BiotechnologyTsinghua UniversityBeijingChina

Personalised recommendations