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<p>Carbonic anhydrase 9 (CA9) is confirmed to be widely expressed in many malignant tumors, including oral squamous cell carcinoma (OSCC). However, more roles and potential molecular mechanisms of CA9 in OSCC progression need to be further elucidated. The mRNA and protein levels of CA9 and interferon regulatory factor-1 (IRF1) were determined by qRT-PCR and western blot. Cell glycolysis was assessed via detecting glucose uptake, lactate production, pH and oxygen consumption rate. Cell migration and apoptosis were measured using transwell assay and flow cytometry. Meanwhile, ROS, SOD, MDA and Fe<sup>2+</sup> levels were tested to evaluate cell ferroptosis. The interaction between IRF1 and CA9 promoter was analyzed by ChIP assay and dual-luciferase reporter assay. Animal study was performed to assess the effect of IRF1 interference on OSCC tumorigenesis. CA9 was upregulated in OSCC tissues and cells. CA9 knockdown inhibited OSCC cell glycolysis and migration, while enhanced cell apoptosis and ferroptosis. Besides, IRF1 increased CA9 expression by promoting its transcription. Moreover, IRF1 silencing inhibited glycolysis, reduced migration, accelerated apoptosis and promoted ferroptosis in OSCC cells, while these effects were eliminated by CA9 overexpression. Also, animal study revealed that interference of IRF1 reduced OSCC tumor growth in vivo via decreasing CA9 level<i>.</i> IRF1-mediated transcriptional activation of CA9 could facilitate OSCC progression, providing a novel target for OSCC treatment.</p>

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IRF1-activated CA9 accelerates oral squamous cell carcinoma process via regulating cell glycolysis, migration, apoptosis and ferroptosis

  • 期刊论文

  • 发表日期：

    2026年1月6日

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  • Yanrong Li,
  • Yanhui Li,
  • Shiying Liu

摘要

Carbonic anhydrase 9 (CA9) is confirmed to be widely expressed in many malignant tumors, including oral squamous cell carcinoma (OSCC). However, more roles and potential molecular mechanisms of CA9 in OSCC progression need to be further elucidated. The mRNA and protein levels of CA9 and interferon regulatory factor-1 (IRF1) were determined by qRT-PCR and western blot. Cell glycolysis was assessed via detecting glucose uptake, lactate production, pH and oxygen consumption rate. Cell migration and apoptosis were measured using transwell assay and flow cytometry. Meanwhile, ROS, SOD, MDA and Fe2+ levels were tested to evaluate cell ferroptosis. The interaction between IRF1 and CA9 promoter was analyzed by ChIP assay and dual-luciferase reporter assay. Animal study was performed to assess the effect of IRF1 interference on OSCC tumorigenesis. CA9 was upregulated in OSCC tissues and cells. CA9 knockdown inhibited OSCC cell glycolysis and migration, while enhanced cell apoptosis and ferroptosis. Besides, IRF1 increased CA9 expression by promoting its transcription. Moreover, IRF1 silencing inhibited glycolysis, reduced migration, accelerated apoptosis and promoted ferroptosis in OSCC cells, while these effects were eliminated by CA9 overexpression. Also, animal study revealed that interference of IRF1 reduced OSCC tumor growth in vivo via decreasing CA9 level. IRF1-mediated transcriptional activation of CA9 could facilitate OSCC progression, providing a novel target for OSCC treatment.