Results 31 to 40 of about 14,270 (217)
PKM2 and cancer: The function of PKM2 beyond glycolysis
Oncology Letters, 2016 Metabolic reprogramming is a hallmark of cancer cells and is used by cancer cells for growth and survival. Pyruvate kinase muscle isozyme M2 (PKM2) is a limiting glycolytic enzyme that catalyzes the final step in glycolysis, which is key in tumor metabolism and growth.
Lin Xu +6 more
openaire +4 more sources
PKM2 in carcinogenesis and oncotherapy
Oncotarget, 2017 Tumor cell metabolism is characterized by abundant glucose consumption and aerobic glycolysis. And pyruvate kinase M2 (PKM2) plays a decisive role in glycolysis, significantly contributing to the Warburg effect, tumor growth, angiogenesis, cell division, metastasis and apoptosis.
Yilong Liu +7 more
openaire +2 more sources
The Complex Effects of PKM2 and PKM2:IP3R Disruption on Intracellular Ca2+ Handling and Cellular Functions [PDF]
Cells, 2023 Pyruvate kinase M (PKM) 2 was described to interact with the inositol 1,4,5-trisphosphate (IP3) receptor (IP3R) and suppress its activity. To further investigate the physiological importance of the PKM2:IP3R interaction, we developed and characterized HeLa PKM2 knockout (KO) cells.
Fernanda O. Lemos +4 more
openaire +3 more sources
Journal of Food Biochemistry, Volume 46, Issue 12, December 2022., 2022 Breast cancer (BC) is one of the most challenging cancers to treat. Nutraceuticals acting by attenuating Hedgehog, NF‐κB, and Wnt/β‐catenin pathways. Nutraceuticals have medical characteristics and may cure cancer Abstract Breast cancer (BC) is one of the most challenging cancers to treat, accounting for many cancer‐related deaths.
Khalid Saad Alharbi +11 more
wiley +1 more source
MiR-1286 inhibits lung cancer growth through aerobic glycolysis by targeting PKM2
Archives of Medical Science, 2019 Introduction This study aims to explore the effects of microRNA-1286 (miR-1286) on the development of non-small cell lung cancer (NSCLC) via the aerobic glycolysis pathway by targeting pyruvate kinase muscle isozyme M2 (PKM2).
Hui Li +6 more
doaj +1 more source
Nuclear PKM2 regulates the Warburg effect [PDF]
Cell Cycle, 2013 Pyruvate kinase is a rate-limiting glycolytic enzyme. The PKM1 and PKM2 isoforms result from mutually exclusive alternative splicing of the PKM pre-mRNA. PKM2 rather than PKM1 regulates the Warburg effect and tumorigenesis by poorly understood mechanisms.
Weiwei Yang, Zhimin Lu
openaire +3 more sources
PKM2 Is a Potential Diagnostic and Therapeutic Target for Retinitis Pigmentosa [PDF]
Disease Markers, 2021 Retinitis pigmentosa (RP) is a major cause of blindness that is difficult to diagnose and treat. PKM2, a subtype of pyruvate kinase, is strongly associated with oxidative stress and is expressed in photoreceptors. We investigated whether PKM2 reduces photoreceptor cell apoptosis and evaluated possible antiapoptotic mechanisms in RP.
Peiwen Zhu +3 more
openaire +2 more sources
Journal of Integrative Neuroscience, 2023 Background: The purpose of this study was to investigate the potential involvement of pyruvate kinase M2 (PKM2), an enzyme acting as a rate-limiting enzyme in the final phase of glycolysis, in the regulation of glial activation and brain damage of ...
Xiao-Yi Xiong +8 more
doaj +1 more source
PKM2: A gatekeeper between growth and survival [PDF]
Cell Research, 2011 Pyruvate kinase catalyzes the transfer of a high-energy phosphate group from phosphoenol pyruvate (PEP) to generate pyruvate and ATP, a reaction that is the rate-limiting step of the glycolytic pathway. The PKM1 alternatively-spliced isoform is ubiquitously expressed whereas the PKM2 isoform is normally highly expressed only in embryos and ...
Susan McCracken +2 more
openaire +3 more sources
Dual roles of PKM2 in cancer metabolism [PDF]
Acta Biochimica et Biophysica Sinica, 2013 Cancer cells have distinct metabolism that highly depends on glycolysis instead of mitochondrial oxidative phosphorylation alone, known as aerobic glycolysis. Pyruvate kinase (PK), which catalyzes the final step of glycolysis, has emerged as a potential regulator of this metabolic phenotype.
Huangying Le, Songfang Wu
openaire +3 more sources