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<p>Endothelial cells constitute the primary barrier within the vessel wall, exhibiting the capacity for angiogenesis, a process implicated in revascularisation.Endothelial cell-mediated angiogenesis is further recognised as a pivotal pathological factor in tumours, pulmonary hypertension, and ocular diseases. Pyruvate kinase type M2 (PKM2) represents a pivotal enzyme in glycolysis, exerting a role in the pathogenic process of diverse diseases through metabolic processes and the transcriptional regulation of key genes. This study established a correlation between PKM2 and angiogenesis in tumours, with the knockdown of PKM2 inhibiting proliferation, migration and angiogenesis in endothelial cells and the over-expression of PKM2 promoting it. Further studies identified ANGPT2 as a downstream target of PKM2, and the supplementation of endothelial cells with ANGPT2 restored proliferation, migration and angiogenesis inhibited by knockdown of PKM2. Collectively, these findings imply that ANGPT2 contributes significantly to the regulation of PKM2-mediated proliferation, migration and angiogenesis.</p>

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PKM2 regulates angiogenic activation via ANGPT2 in endothelial cells

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年8月26日

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  • Qiangqiang Ge,
  • Jianan Guo,
  • Liyuan Ye,
  • Yifei Le,
  • Ji Zhu

摘要

Endothelial cells constitute the primary barrier within the vessel wall, exhibiting the capacity for angiogenesis, a process implicated in revascularisation.Endothelial cell-mediated angiogenesis is further recognised as a pivotal pathological factor in tumours, pulmonary hypertension, and ocular diseases. Pyruvate kinase type M2 (PKM2) represents a pivotal enzyme in glycolysis, exerting a role in the pathogenic process of diverse diseases through metabolic processes and the transcriptional regulation of key genes. This study established a correlation between PKM2 and angiogenesis in tumours, with the knockdown of PKM2 inhibiting proliferation, migration and angiogenesis in endothelial cells and the over-expression of PKM2 promoting it. Further studies identified ANGPT2 as a downstream target of PKM2, and the supplementation of endothelial cells with ANGPT2 restored proliferation, migration and angiogenesis inhibited by knockdown of PKM2. Collectively, these findings imply that ANGPT2 contributes significantly to the regulation of PKM2-mediated proliferation, migration and angiogenesis.