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Identification, expression and tissue distribution of a renalase homologue from mouse
Jian Wang1, Shaoling Qi, Wei Cheng
1Laboratory for Functional Genomic Research, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, 100084, China.
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.
Insights
Researchers identified a mouse monoamine oxidase-C (mMAO-C), a homologue of human renalase. This mMAO-C is predominantly expressed in mouse kidney and testicle, suggesting key roles in these organs.
Area of Science:
- Biochemistry
- Genetics
- Molecular Biology
Background:
- Flavin adenine dinucleotide (FAD)-dependent monoamine oxidases (MAOs) are crucial for biological processes.
- Human renalase, a novel MAO, is reduced in end-stage renal disease (ESRD).
Purpose of the Study:
- To identify and characterize a mouse homologue of renalase, termed mMAO-C.
- To investigate the expression pattern and potential function of mMAO-C.
Main Methods:
- Gene cloning and sequencing of mMAO-C.
- Bioinformatic analysis including phylogenetic and sequence alignment.
- Protein expression in prokaryotic and eukaryotic systems.
- Tissue expression analysis using quantitative methods.
Main Results:
- The mMAO-C gene was identified on mouse chromosome 19C1, with a 7-exon coding region.
- Predicted amino acid sequence revealed a signal peptide and conserved amine oxidase domain.
- mMAO-C homologues are conserved across species.
- Recombinant mMAO-C protein was successfully expressed and secreted from human cell lines.
- mMAO-C is predominantly expressed in mouse kidney and testicle.
Conclusions:
- mMAO-C is a secreted protein with conserved structural features.
- Kidney and testicle are identified as primary sources of mMAO-C secretion.
- This study provides foundational insights into the physiological roles of mMAO-C and related enzymes in endocrine functions.
