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Manipulation of glucose and hydroperoxide metabolism to improve radiation response [PDF]
Floberg, John M, Schwarz, Julie K
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2023 
Key Points: 1. Platelet activation increases PKM2 dimer formation, which modulates platelet functions and arterial thrombosis. 2. PKM2 regulates PI3Kmediated Akt and GSK3 signaling.
Nayak, Manasa +8 more
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Key Points: 1. Platelet activation increases PKM2 dimer formation, which modulates platelet functions and arterial thrombosis. 2. PKM2 regulates PI3Kmediated Akt and GSK3 signaling.
Nayak, Manasa +8 more
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Activators of PKM2 in Cancer Metabolism
Future Medicinal Chemistry, 2014Pyruvate kinase converts phosphoenolpyruvate to pyruvate, catalyzing the rate-limiting step of glycolysis. The M1 isoenzyme of pyruvate kinase (PKM1) is found in adult tissues; whereas, PKM2 is a splicesome variant found in embryonic and cancer cells.
Kent J. Carpenter +2 more
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PKM2 contributes to cancer metabolism
Cancer Letters, 2015Reprogramming of cell metabolism is essential for tumorigenesis, and is regulated by a complex network, in which PKM2 plays a critical role. PKM2 exists as an inactive monomer, less active dimer and active tetramer. While dimeric PKM2 diverts glucose metabolism towards anabolism through aerobic glycolysis, tetrameric PKM2 promotes the flux of glucose ...
Damu Tang +3 more
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PKM2, a potential target for regulating cancer
Gene, 2018Aberrated glucose metabolism is a key future of cancer cells. Unlike normal cells, tumor cells favor glycolysis even in the presence of sufficient oxygen. Pyruvate kinase (PK), a key glucose metabolic enzyme, converts phosphoenolpyruvate (PEP) to pyruvate by transferring the high-energy phosphate group to adenosine diphosphate (ADP) to produce ...
Yu-huan Li +6 more
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PKM2 Is Essential for Bladder Cancer Growth and Maintenance
Cancer Research, 2021Abstract Pyruvate kinase M2 (PKM2) has been shown to promote tumorigenesis by facilitating the Warburg effect and enhancing the activities of oncoproteins. However, this paradigm has recently been challenged by studies in which the absence of PKM2 failed to inhibit and instead accelerated ...
Yong Xia +7 more
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Nature Reviews Molecular Cell Biology, 2012 
Pyruvate kinase isoform M2 (PKM2) is a glycolytic enzyme that mediates the conversion of phosphoenolpyruvate (PEP) to pyruvate. It has been suggested that PKM2 may have additional enzymatic activities and localizes to the nucleus to regulate transcription. Here, the authors show that PKM2 can act as a kinase in the nucleus. They found that nuclear PKM2
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Pyruvate kinase isoform M2 (PKM2) is a glycolytic enzyme that mediates the conversion of phosphoenolpyruvate (PEP) to pyruvate. It has been suggested that PKM2 may have additional enzymatic activities and localizes to the nucleus to regulate transcription. Here, the authors show that PKM2 can act as a kinase in the nucleus. They found that nuclear PKM2
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PKM2: A New Player in the β-Catenin Game
Future Oncology, 2012β-catenin is a key player in the regulation of gene expression during morphogenesis and tumorigenesis. Although its transactivation often results from stimulation of the Wnt signaling pathway, Wnt-independent regulation of β-catenin has also been observed in cancer cells.
Frédéric Canal, Christine Perret
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The multifaceted regulation and functions of PKM2 in tumor progression
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer, 2014Tumor cells undergo metabolic rewiring from oxidative phosphorylation towards aerobic glycolysis to maintain the increased anabolic requirements for cell proliferation. It is widely accepted that specific expression of the M2 type pyruvate kinase (PKM2) in tumor cells contributes to this aerobic glycolysis phenotype. To date, researchers have uncovered
Zongwei Li +3 more
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PKM2 Moonlights as a Protein Kinase
Science Signaling, 2012Pyruvate kinase M2 phosphorylates the transcription factor STAT3.
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