ArticleMolecular biology reports2025
NT5DC2 downregulation suppresses monoamine oxidase activity and promotes catecholamine synthesis in PC12D cells.
Article in Molecular biology reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundGenome-wide association studies have revealed the involvement of 5'-nucleotidase domain-containing protein 2 (NT5DC2) in neuropsychiatric disorders such as schizophrenia and bipolar disorder; however, its function remains unclear. We recently found that NT5DC2 downregulation in PC12D cells increases catecholamine synthesis by promoting tyrosine hydroxylase (TH) activity. In addition, affinity purification-mass spectrometry suggested a potential interaction between NT5DC2 and monoamine oxidase A (MAO A). In this study, we examined the impact of NT5DC2 on MAO A activity in PC12D cells and the related effects on catecholamine metabolism. METHODS AND
resultsWe analyzed changes in catecholamine metabolism in siRNA-mediated NT5DC2-downregulated PC12D cells by measuring the catecholamines and major acid metabolites produced by the addition of exogenous dopamine (DA) to PC12D cells, with DOPA synthesis suppressed by the addition of a TH inhibitor. Western blot analysis revealed that NT5DC2 primarily binds to the non-phosphorylated form of MAO A. NT5DC2 downregulation reduced MAO A activity, leading to decreased dopamine metabolism and increased noradrenaline synthesis.
conclusionOur findings suggest that NT5DC2 regulates MAO A activity to control catecholamine synthesis. This study provides valuable insights into disorders associated with catecholamine dysregulation, such as Parkinson's disease and neuropsychiatric disorders.
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