Skip to main content
Log in

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

  • Original Paper
  • Published:
Molecular Biology Reports Aims and scope Submit manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

References

  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 115:1275–1280

    PubMed  CAS  Google Scholar 

  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 139:137–147

    PubMed  Google Scholar 

  3. Chavers BM, Li S, Collins AJ, Herzog CA (2002) Cardiovascular disease in pediatric chronic dialysis patients. Kidney Int 62:648–653

    Article  PubMed  Google Scholar 

  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 18:374–378

    Article  PubMed  CAS  Google Scholar 

  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 65:1009–1016

    Article  PubMed  Google Scholar 

  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 47:559–565

    Article  PubMed  CAS  Google Scholar 

  7. Koomans HA, Blankestijn PJ, Joles JA (2004) Sympathetic hyperactivity in chronic renal failure: a wake-up call. J Am Soc Nephrol 15:524–537

    Article  PubMed  Google Scholar 

  8. Joles JA, Koomans HA (2004) Causes and consequences of increased sympathetic activity in renal disease. Hypertension 43:699–706

    Article  PubMed  CAS  Google Scholar 

  9. Tonelli M, Pfeffer MA (2007) Kidney disease and cardiovascular risk. Annu Rev Med 58:123–139

    Article  PubMed  CAS  Google Scholar 

  10. Tonelli M, Wiebe N, Culleton B et al (2006) Chronic kidney disease and mortality risk: a systematic review. J Am Soc Nephrol 17:2034–2047

    Article  PubMed  Google Scholar 

  11. Luft FC (2005) Renalase, a catecholamine-metabolizing hormone from the kidney. Cell Metab 1:358–360

    Article  PubMed  CAS  Google Scholar 

  12. Vaughan C (2005) Renalase could even survival odds in kidney disease. National Review of Medicine 2

  13. Bendtsen JD, Nielsen H, von Heijne G, Brunak S (2004) Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340:783–795

    Article  PubMed  Google Scholar 

  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 32:719–735

    Article  PubMed  CAS  Google Scholar 

  15. Schnaitman C, Greenawalt JW (1968) Enzymatic properties of the inner and outer membranes of rat liver mitochondria. J Cell Biol 38:158–175

    Article  PubMed  CAS  Google Scholar 

  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 46:173–179

    Article  PubMed  CAS  Google Scholar 

  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 88:3637–3641

    Article  PubMed  CAS  Google Scholar 

  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 122–130

    Google Scholar 

  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–W331

    Article  PubMed  CAS  Google Scholar 

  20. Rost B, Yachdav G, Liu J (2004) The PredictProtein server. Nucleic Acids Res 32(Web Server issue):W321–W326

    Article  PubMed  CAS  Google Scholar 

  21. Persson PB (2003) Renin: origin, secretion and synthesis. J Physiol 552:667–671

    Article  PubMed  CAS  Google Scholar 

  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–S296

    Article  PubMed  CAS  Google Scholar 

  23. Cases O, Seif I, Grimsby J (1995) Aggressive behavior and altered amounts of brain serotonin and norepinephrine in mice lacking MAO-A. Science 268:1763–1766

    Article  PubMed  CAS  Google Scholar 

  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 279:39645–39652

    Article  PubMed  CAS  Google Scholar 

  25. Shih JC, Chen K, Ridd MJ (1999) Monoamine oxidase: from genes to behavior. Annu Rev Neurosci 22:197–217

    Article  PubMed  CAS  Google Scholar 

  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 277:23973–23976

    Article  PubMed  CAS  Google Scholar 

  27. Chen K (2004) Organization of MAO-A and MAO-B promoters and regulation of gene expression. Neurotoxicology 25:31–36

    Article  PubMed  Google Scholar 

  28. Grimsby J, Lan NC, Neve R et al (1990) Tissue distribution of human monoamine oxidase A and B mRNA. J Neurochem 55:1166–1169

    Article  PubMed  CAS  Google Scholar 

  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 15:399–408

    Article  PubMed  CAS  Google Scholar 

  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 12:1977–1999

    PubMed  CAS  Google Scholar 

Download references

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.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Shu-Ping Zhang.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Wang, J., Qi, S., Cheng, W. et al. Identification, expression and tissue distribution of a renalase homologue from mouse. Mol Biol Rep 35, 613–620 (2008). https://doi.org/10.1007/s11033-007-9131-1

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11033-007-9131-1

Keywords

Navigation