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


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.


Mouse Renalase homologue Molecular cloning Tissue distribution 



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.


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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

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