Abstract
BackgroundSOD1 is an abundant enzyme that has been studied as a regulator of the antioxidant defence system, and this enzyme is well known for catalyzing the dismutation of superoxide into hydrogen peroxide. However the SOD1 in the progress of NPC and underlying mechanisms remain unclear.MethodsIn NPC tissue samples, SOD1 protein levels were measured by Western blot and immunohistochemical (IHC) staining. mRNA levels and SOD1 activity were monitored by qRT-PCR and SOD activity kit, respectively. Kaplan-Meier survival analysis was performed to explore the relationship between SOD1 expression and prognosis of NPC. The biological effects of SOD1 were investigated both in vitro by CCK-8, clonogenicity and apoptosis assays and in vivo by a xenograft mice model. Western blotting, ROS assay and triglyceride assays were applied to investigate the underlying molecular mechanism of pro-survival role of SOD1 in NPC.ResultsWe observed a significant upregulation of SOD1 in NPC tissue and high SOD1 expression is a predictor of poor prognosis and is correlated with poor outcome. We confirmed the pro-survival role of SOD1 both in vitro and in vivo. We demonstrated that these mechanisms of SOD1 partly exist to maintain low levels of the superoxide anion and to avoid the accumulation of lipid droplets via enhanced CPT1A-mediated fatty acid oxidation.ConclusionsThe results of this study indicate that SOD1 is a potential prognostic biomarker and a promising target for NPC therapy.
Highlights
SOD1 is an abundant enzyme that has been studied as a regulator of the antioxidant defence system, and this enzyme is well known for catalyzing the dismutation of superoxide into hydrogen peroxide
High SOD1 expression is associated with poor prognosis in nasopharyngeal carcinoma SOD1 is best known for its role in redox homeostasis and is often dysregulated during cancer development
We found that SOD1 mRNA was significantly increased in head and neck cancer tissues from the Oncomine microarray database (Fig. 1a, https://www.oncomine.org)
Summary
SOD1 is an abundant enzyme that has been studied as a regulator of the antioxidant defence system, and this enzyme is well known for catalyzing the dismutation of superoxide into hydrogen peroxide. Reactive oxygen species (ROS) are important for tumourigenesis and tumour progression, but a large increase in the ROS level usually causes cell death [2, 3]. Superoxide is the first species to be produced, and superoxide is converted to hydrogen peroxide through dismutase activity [4]. The cellular detoxification of harmful superoxide usually requires the dismutase activity. There are three distinct superoxide dismutases (SODs) [7]. SOD2 is a manganese-dependent enzyme located in the mitochondria, whereas SOD3 is an extracellular enzyme
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