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PKM2 regulates endothelial cell junction dynamics and angiogenesis via ATP production
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Journal Article
PKM2 regulates endothelial cell junction dynamics and angiogenesis via ATP production
2019
Overview
Angiogenesis, the formation of new blood vessels from pre-existing ones, occurs in pathophysiological contexts such as wound healing, cancer, and chronic inflammatory disease. During sprouting angiogenesis, endothelial tip and stalk cells coordinately remodel their cell-cell junctions to allow collective migration and extension of the sprout while maintaining barrier integrity. All these processes require energy, and the predominant ATP generation route in endothelial cells is glycolysis. However, it remains unclear how ATP reaches the plasma membrane and intercellular junctions. In this study, we demonstrate that the glycolytic enzyme pyruvate kinase 2 (PKM2) is required for sprouting angiogenesis
in vitro
and
in vivo
through the regulation of endothelial cell-junction dynamics and collective migration. We show that PKM2-silencing decreases ATP required for proper VE-cadherin internalization/traffic at endothelial cell-cell junctions. Our study provides fresh insight into the role of ATP subcellular compartmentalization in endothelial cells during angiogenesis. Since manipulation of EC glycolysis constitutes a potential therapeutic intervention route, particularly in tumors and chronic inflammatory disease, these findings may help to refine the targeting of endothelial glycolytic activity in disease.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 14/33
/ 14/63
/ 64/60
/ Adenosine Triphosphate - biosynthesis
/ Animals
/ Carrier Proteins - metabolism
/ Human Umbilical Vein Endothelial Cells - metabolism
/ Humanities and Social Sciences
/ Humans
/ Intercellular Junctions - metabolism
/ Membrane Proteins - metabolism
/ Neovascularization, Physiologic
/ Pyruvate Kinase - metabolism
/ Science
/ Thyroid Hormone-Binding Proteins
/ Thyroid Hormones - metabolism
/ Tumors
