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Journal articles on the topic 'Pyruvate kinase M2 (PKM2)'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Kurihara-Shimomura, Miyako, Tomonori Sasahira, Chie Nakashima, Hiroki Kuniyasu, Hiroyuki Shimomura, and Tadaaki Kirita. "The Multifarious Functions of Pyruvate Kinase M2 in Oral Cancer Cells." International Journal of Molecular Sciences 19, no. 10 (2018): 2907. http://dx.doi.org/10.3390/ijms19102907.

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Head and neck cancers, including oral squamous cell carcinoma (OSCC), are the sixth most common malignancies worldwide. OSCC frequently leads to oral dysfunction, which worsens a patient’s quality of life. Moreover, its prognosis remains poor. Unlike normal cells, tumor cells preferentially metabolize glucose by aerobic glycolysis. Pyruvate kinase (PK) catalyzes the final step in glycolysis, and the transition from PKM1 to PKM2 is observed in many cancer cells. However, little is known about PKM expression and function in OSCC. In this study, we investigated the expression of PKM in OSCC speci

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2

Sturgill, Eric M., and Monica L. Guzman. "Cytokine Induced Nuclear Localization Of Pyruvate Kinase M2 In Acute Myeloid Leukemia." Blood 122, no. 21 (2013): 5406. http://dx.doi.org/10.1182/blood.v122.21.5406.5406.

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Abstract A common characteristic among nearly all cancers, including leukemia, is the cell’s metabolic proclivity for glycolysis over the more energy efficient process of oxidative phosphorylation (OXPHOS) in the presence of oxygen. This altered state of aerobic glycolysis was observed in tumor cells by Otto Warburg over fifty years ago (Warburg, 1956) and continues to be intensely investigated in hopes of ultimately exploiting this “Warburg effect” in the treatment of cancer (Vander Heiden et al. 2009). Recent studies have revealed that the M2 isoform of the enzyme pyruvate kinase (PKM2) play

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3

Nayak, Manasa, Nirav Dhanesha, Manish Jain, and Anil Chauhan. "Manipulating Metabolic Plasticity By Targeting Pyruvate Kinase M2 in Platelets Inhibits Arterial Thrombosis." Blood 132, Supplement 1 (2018): 868. http://dx.doi.org/10.1182/blood-2018-99-112704.

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Abstract Background: Most of the cellular responses initiated upon platelet activation are energy consuming. Like normal cells, resting platelets rely primarily on oxidative phosphorylation (OXPHOS) to generate ATP, whereas activated platelets exhibit a high level of aerobic glycolysis (conversion of glucose to lactate in the presence of oxygen, a phenomenon referred to as the Warburg effect in tumor cells) suggesting that metabolic plasticity exists in activated platelets. Although aerobic glycolysis yields less total ATP when compared to OXPHOS, the rate of ATP generation is faster in aerobi

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4

Xia, Li, Xin-Ran Wang, Ran Wei, Jin-Song Yan, Guo-Qiang Chen, and Ying Lu. "Sumoylation of Pyruvate Kinase M2 Inhibits Myeloid Differentiation in Hematopoietic Cells." Blood 132, Supplement 1 (2018): 3919. http://dx.doi.org/10.1182/blood-2018-99-117899.

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Abstract The pyruvate kinase (PK) is a rate-limiting glycolytic enzyme catalyzing the dephosphorylation of phosphoenolpyruvate to pyruvate. M2 form of PK (PKM2) is expressed during embryogenesis and is the predominant form in tumors of different types. In contrast to the essential role of PKM2 in solid tumors, much less is known about the effects of PKM2 in hematopoietic cells and the development of leukemia. Here we found that PKM2 is modified by small ubiquitin-like modifier 1(SUMO1), which can be reduced by a SUMO1-specific protease SENP1 in hematopoietic cells. SUMOylation induced nuclear

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5

Su, Yan, Sujuan Guo, Chunyan Liu, et al. "Endometrial pyruvate kinase M2 is essential for decidualization during early pregnancy." Journal of Endocrinology 245, no. 3 (2020): 357–68. http://dx.doi.org/10.1530/joe-19-0553.

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Embryo implantation is essential for normal pregnancy. Decidualization is known to facilitate embryo implantation and maintain pregnancy. Uterine stromal cells undergo transformation into decidual cells after embryo attachment to the endometrium. Pyruvate kinase M2 (PKM2) is a rate limiting enzyme in the glycolysis process which catalyzes phosphoenolpyruvic acid into pyruvate. However, little is known regarding the role of PKM2 during endometrial decidualization. In this study, PKM2 was found to be mainly located in the uterine glandular epithelium and luminal epithelium on day 1 and day 4 of

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6

Esen, I., Y. Van Sleen, P. Heeringa, A. Boots, and E. Brouwer. "AB0471 ELEVATED EXPRESSION OF PYRUVATE KINASE M2 IN GIANT CELL ARTERITIS." Annals of the Rheumatic Diseases 79, Suppl 1 (2020): 1534.1–1534. http://dx.doi.org/10.1136/annrheumdis-2020-eular.1699.

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Background:Giant Cell Arteritis (GCA) is an inflammatory disease of large and medium vessels. In GCA, expression of interleukin-6 (IL-6), a systemic marker of inflammation, is elevated and it has been shown that treatment with IL-6 receptor blockade (Tocilizumab) is beneficial for GCA patients.1To investigate the role of the IL-6 signaling pathway in GCA pathogenesis in more depth, we focused on the metabolic enzyme Pyruvate Kinase M2 (PKM2). PKM2 may exist as a tetramer, a dimer and/or a monomer in the cell. Tetrameric PKM2 acts as a glycolytic enzyme and catalyzes the last steps of glycolysi

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7

Goldberg, Michael S., and Phillip A. Sharp. "Pyruvate kinase M2-specific siRNA induces apoptosis and tumor regression." Journal of Experimental Medicine 209, no. 2 (2012): 217–24. http://dx.doi.org/10.1084/jem.20111487.

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The development of cancer-specific therapeutics has been limited because most healthy cells and cancer cells depend on common pathways. Pyruvate kinase (PK) exists in M1 (PKM1) and M2 (PKM2) isoforms. PKM2, whose expression in cancer cells results in aerobic glycolysis and is suggested to bestow a selective growth advantage, is a promising target. Because many oncogenes impart a common alteration in cell metabolism, inhibition of the M2 isoform might be of broad applicability. We show that several small interfering (si) RNAs designed to target mismatches between the M2 and M1 isoforms confer s

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8

Sharma, Pankaj. "Molecular docking analysis of pyruvate kinase M2 with a potential inhibitor from the ZINC database." Bioinformation 17, no. 1 (2021): 139–46. http://dx.doi.org/10.6026/97320630017139.

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The pyruvate kinase M2 isoform (PKM2) is linked with cancer. Therefore, it is of interest to document the molecular docking analysis of Pyruvate Kinase M2 (PDB ID: 4G1N) with potential activators from the ZINC database. Thus, we document the optimal molecular docking features of a compound having ID ZINC000034285235 with PKM2 for further consideration.

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9

Choi, Hae-Seul, Chang-Zhu Pei, Jun-Hyeok Park, et al. "Protein Stability of Pyruvate Kinase Isozyme M2 Is Mediated by HAUSP." Cancers 12, no. 6 (2020): 1548. http://dx.doi.org/10.3390/cancers12061548.

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The ubiquitin–proteasome system (UPS) is responsible for proteasomal degradation, regulating the half-life of the protein. Deubiquitinating enzymes (DUBs) are components of the UPS and inhibit degradation by removing ubiquitins from protein substrates. Herpesvirus-associated ubiquitin-specific protease (HAUSP) is one such deubiquitinating enzyme and has been closely associated with tumor development. In a previous study, we isolated putative HAUSP binding substrates by two-dimensional electrophoresis (2-DE) and identified them by matrix-assisted laser desorption-ionization time-of-flight mass

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10

Rathod, Bhagyashri, Shivam Chak, Sagarkumar Patel, and Amit Shard. "Tumor pyruvate kinase M2 modulators: a comprehensive account of activators and inhibitors as anticancer agents." RSC Medicinal Chemistry 12, no. 7 (2021): 1121–41. http://dx.doi.org/10.1039/d1md00045d.

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11

Wang, Guiping, Yingying Zhong, Jiecong Liang, Zhibin Li, and Yun Ye. "Upregulated expression of pyruvate kinase M2 mRNA predicts poor prognosis in lung adenocarcinoma." PeerJ 8 (February 20, 2020): e8625. http://dx.doi.org/10.7717/peerj.8625.

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Background Pyruvate kinase M2 (PKM2) is critical regulator contributing to Warburg effect. However, the expression pattern and prognostic value of PKM2 remain unknown in lung adenocarcinoma (LUAD). The aim of this study is to clarify the prognostic value of PKM2 via intergrated bioinformatics analysis. Methods Firstly, mRNA expression levels of PKM2 in LUAD were systematically analyzed using the ONCOMINE and TCGA databases. Then, the association between PKM2 expression and clinical parameters was investigated by UALCAN. The Kaplan–Meier Plotter was used to assess the prognostic significance of

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12

Nayak, Manasa K., Madankumar Ghatge, Nirav Dhanesha, et al. "Targeting Metabolic Enzyme Pyruvate Kinase M2: A Novel Strategy to Inhibit Platelet Function and Arterial Thrombosis." Blood 134, Supplement_1 (2019): 1056. http://dx.doi.org/10.1182/blood-2019-129027.

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Background: The cellular responses initiated upon platelet activation are energy consuming. Activated platelets, in comparison to their resting state, exhibit a high level of aerobic glycolysis (conversion of glucose to lactate in the presence of oxygen) relative to oxidative phosphorylation (OXPHOS), suggesting that metabolic plasticity exists in platelets. Although aerobic glycolysis yields less total ATP when compared to OXPHOS, the rate of ATP generation is faster in aerobic glycolysis compared to OXPHOS, which we hypothesize is well suited for high-energy requirement during platelet activ

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13

Nandi, Suparno, Mortezaali Razzaghi, Dhiraj Srivastava, and Mishtu Dey. "Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation." Journal of Biological Chemistry 295, no. 51 (2020): 17425–40. http://dx.doi.org/10.1074/jbc.ra120.015800.

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Pyruvate kinase muscle isoform 2 (PKM2) is a key glycolytic enzyme and transcriptional coactivator and is critical for tumor metabolism. In cancer cells, native tetrameric PKM2 is phosphorylated or acetylated, which initiates a switch to a dimeric/monomeric form that translocates into the nucleus, causing oncogene transcription. However, it is not known how these post-translational modifications (PTMs) disrupt the oligomeric state of PKM2. We explored this question via crystallographic and biophysical analyses of PKM2 mutants containing residues that mimic phosphorylation and acetylation. We f

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14

Kim, Hyunju, Seong Ho Kim, Dohyeon Hwang, et al. "Extracellular pyruvate kinase M2 facilitates cell migration by upregulating claudin-1 expression in colon cancer cells." Biochemistry and Cell Biology 98, no. 2 (2020): 219–26. http://dx.doi.org/10.1139/bcb-2019-0139.

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Extensive studies have been reported the non-canonical functions of pyruvate kinase M2 (PKM2) as a kinase, transcriptional regulator, and even cell-to-cell communicator, emphasizing its importance in various signaling pathways. However, the role of secreted PKM2 in cancer progression and its signaling pathway is yet to be elucidated. In this study, we found that extracellular PKM2 enhanced the migration of low-metastatic, benign colon cancer cells by upregulating claudin-1 expression and internalizing it to the cytoplasm and nucleus. Knock-down of claudin-1 significantly reduced extracellular

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15

Kumar, Amit, Priya Gupta, Minakshi Rana, Tulika Chandra, Madhu Dikshit, and Manoj Kumar Barthwal. "Role of pyruvate kinase M2 in oxidized LDL-induced macrophage foam cell formation and inflammation." Journal of Lipid Research 61, no. 3 (2020): 351–64. http://dx.doi.org/10.1194/jlr.ra119000382.

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Pyruvate kinase M2 (PKM2) links metabolic and inflammatory dysfunction in atherosclerotic coronary artery disease; however, its role in oxidized LDL (Ox-LDL)-induced macrophage foam cell formation and inflammation is unknown and therefore was studied. In recombinant mouse granulocyte-macrophage colony-stimulating factor-differentiated murine bone marrow-derived macrophages, early (1–6 h) Ox-LDL treatment induced PKM2 tyrosine 105 phosphorylation and promotes its nuclear localization. PKM2 regulates aerobic glycolysis and inflammation because PKM2 shRNA or Shikonin abrogated Ox-LDL-induced hypo

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Dey, Son, Kundu, et al. "Knockdown of Pyruvate Kinase M2 Inhibits Cell Proliferation, Metabolism, and Migration in Renal Cell Carcinoma." International Journal of Molecular Sciences 20, no. 22 (2019): 5622. http://dx.doi.org/10.3390/ijms20225622.

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Emerging evidence indicates that the activity of pyruvate kinase M2 (PKM2) isoform is crucial for the survival of tumor cells. However, the molecular mechanism underlying the function of PKM2 in renal cancer is undetermined. Here, we reveal the overexpression of PKM2 in the proximal tubule of renal tumor tissues from 70 cases of patients with renal carcinoma. The functional role of PKM2 in human renal cancer cells following small-interfering RNA-mediated PKM2 knockdown, which retarded 786-O cell growth was examined. Targeting PKM2 affected the protein kinase B (AKT)/mechanistic target of the r

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Chen, Kuan-Chung, Kuen-Bao Chen, Hsin-Yi Chen, and Calvin Yu-Chian Chen. "In SilicoInvestigation of Potential Pyruvate Kinase M2 Regulators from Traditional Chinese Medicine against Cancers." BioMed Research International 2014 (2014): 1–14. http://dx.doi.org/10.1155/2014/189495.

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A recent research in cancer research demonstrates that tumor-specific pyruvate kinase M2 (PKM2) plays an important role in chromosome segregation and mitosis progression of tumor cells. To improve the drug development of TCM compounds, we aim to identify potent TCM compounds as lead compounds of PKM2 regulators. PONDR-Fit protocol was utilized to predict the disordered disposition in the binding domain of PKM2 protein before virtual screening as the disordered structure in the protein may cause the side effect and downregulation of the possibility of ligand to bind with target protein. MD simu

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18

Yang, Peng, Guo-Bin Ding, Wen Liu, Rong Fu, Amin Sajid, and Zhuoyu Li. "Tannic acid directly targets pyruvate kinase isoenzyme M2 to attenuate colon cancer cell proliferation." Food & Function 9, no. 11 (2018): 5547–59. http://dx.doi.org/10.1039/c8fo01161c.

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Tannic acid, which ubiquitously exists in grapes and green tea, binds to K433 to trigger dissociation of PKM2 tetramers and further block the metabolic activity of PKM2 to suppress colorectal cancer cell proliferation.

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19

Dai, Jinlu, June Escara-Wilke, Jill M. Keller, et al. "Primary prostate cancer educates bone stroma through exosomal pyruvate kinase M2 to promote bone metastasis." Journal of Experimental Medicine 216, no. 12 (2019): 2883–99. http://dx.doi.org/10.1084/jem.20190158.

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Prostate cancer (PCa) metastasizes selectively to bone through unknown mechanisms. In the current study, we identified exosome-mediated transfer of pyruvate kinase M2 (PKM2) from PCa cells into bone marrow stromal cells (BMSCs) as a novel mechanism through which primary tumor-derived exosomes promote premetastatic niche formation. We found that PKM2 up-regulates BMSC CXCL12 production in a HIF-1α-dependent fashion, which subsequently enhances PCa seeding and growth in the bone marrow. Furthermore, serum-derived exosomes from patients with either primary PCa or PCa metastasis, as opposed to hea

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Tsai, Kary Y. F., Benton Tullis, Juan Mejia, Paul R. Reynolds, and Juan A. Arroyo. "Regulation of trophoblast cell invasion by Pyruvate Kinase isozyme M2 (PKM2)." Placenta 103 (January 2021): 24–32. http://dx.doi.org/10.1016/j.placenta.2020.10.019.

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Li, Zhichao, Hanqing Li, Yangxu Lu, Peng Yang, and Zhuoyu Li. "Berberine Inhibited the Proliferation of Cancer Cells by Suppressing the Activity of Tumor Pyruvate Kinase M2." Natural Product Communications 12, no. 9 (2017): 1934578X1701200. http://dx.doi.org/10.1177/1934578x1701200909.

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Berberine, an isoquinoline alkaloid extracted from coptis, exerts anti-proliferation and anticancer properties. Pyruvate kinase M2 (PKM2) is a key enzyme of aerobic glycolysis and considered as the potential anticancer target. However, the inhibition effects and interaction action between Berberine and PKM2 is not well known. In this study, berberine showed antitumor activity of HCT-116 and HeLa cells with the suppression of cell proliferation. Moreover, berberine inhibited the enzyme activity of PKM2 in cancer cells, but had no impact on PKM2 expression. Further research showed that the inter

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Lee, Seoung-Ae, Charles Ho, Madison Troxler, Chin-Yo Lin, and Sang-Hyuk Chung. "Non-Metabolic Functions of PKM2 Contribute to Cervical Cancer Cell Proliferation Induced by the HPV16 E7 Oncoprotein." Viruses 13, no. 3 (2021): 433. http://dx.doi.org/10.3390/v13030433.

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Pyruvate kinase M2 (PKM2) mainly catalyzes glycolysis, but it also exerts non-glycolytic functions in several cancers. While it has been shown to interact with the human papillomavirus 16 (HPV16) E7 oncoprotein, the functional significance of PKM2 in HPV-associated cervical cancer has been elusive. Here, we show that HPV16 E7 increased the expression of PKM2 in cervical cancer cells. TCGA data analyses revealed a higher level of PKM2 in HPV+ than HPV− cervical cancers and a worse prognosis for patients with high PKM2 expression. Functionally, we demonstrate that shRNA-mediated PKM2 knockdown d

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Miao, Yi, Meng Lu, Qin Yan, Shuangdi Li, and Youji Feng. "Inhibition of Proliferation, Migration, and Invasion by Knockdown of Pyruvate Kinase-M2 (PKM2) in Ovarian Cancer SKOV3 and OVCAR3 Cells." Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics 24, no. 6 (2016): 463–75. http://dx.doi.org/10.3727/096504016x14685034103671.

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Pyruvate kinase (PK) is a key enzyme in the process of glycolysis, catalyzing phosphoenolpyruvate (PEP) into pyruvate. Currently, PK isozyme type M2 (PKM2), one subtype of PK, has been proposed as a new tumor marker with high expression in various tumor tissues. Here we aimed to explore the effects of siRNA-PKM2 on ovarian carcinoma (OC) cell lines SKOV3 and OVCAR3, in which PKM2 was notably expressed. PKM2 gene interference lentivirus vectors were built by miRNA transfection assay. siRNA-PKM2-transfected SKOV3 and OVCAR3 cells were evaluated for cell proliferation, cell cycle distribution, ce

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Jiang, Lei, Yuanlin Gao, Gaiying Wang, and Jie Zhong. "PKM2 overexpression protects against 6-hydroxydopamine-induced cell injury in the PC12 cell model of Parkinson's disease via regulation of the brahma-related gene 1/STAT3 pathway." RSC Advances 9, no. 26 (2019): 14834–40. http://dx.doi.org/10.1039/c9ra01760g.

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Biyik-Sit, Rumeysa, Traci Kruer, Susan Dougherty, et al. "Nuclear Pyruvate Kinase M2 (PKM2) Contributes to Phosphoserine Aminotransferase 1 (PSAT1)-Mediated Cell Migration in EGFR-Activated Lung Cancer Cells." Cancers 13, no. 16 (2021): 3938. http://dx.doi.org/10.3390/cancers13163938.

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An elevated expression of phosphoserine aminotransferase 1 (PSAT1) has been observed in multiple tumor types and is associated with poorer clinical outcomes. Although PSAT1 is postulated to promote tumor growth through its enzymatic function within the serine synthesis pathway (SSP), its role in cancer progression has not been fully characterized. Here, we explore a putative non-canonical function of PSAT1 that contributes to lung tumor progression. Biochemical studies found that PSAT1 selectively interacts with pyruvate kinase M2 (PKM2). Amino acid mutations within a PKM2-unique region signif

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Li, Qi, Xue Liu, Yu Yin, et al. "Insulin Regulates Glucose Consumption and Lactate Production through Reactive Oxygen Species and Pyruvate Kinase M2." Oxidative Medicine and Cellular Longevity 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/504953.

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Although insulin is known to regulate glucose metabolism and closely associate with liver cancer, the molecular mechanisms still remain to be elucidated. In this study, we attempt to understand the mechanism of insulin in promotion of liver cancer metabolism. We found that insulin increased pyruvate kinase M2 (PKM2) expression through reactive oxygen species (ROS) for regulating glucose consumption and lactate production, key process of glycolysis in hepatocellular carcinoma HepG2 and Bel7402 cells. Interestingly, insulin-induced ROS was found responsible for the suppression of miR-145 and miR

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Meoli, Luca, Nitin K. Gupta, Nima Saeidi, et al. "Nonalcoholic fatty liver disease and gastric bypass surgery regulate serum and hepatic levels of pyruvate kinase isoenzyme M2." American Journal of Physiology-Endocrinology and Metabolism 315, no. 4 (2018): E613—E621. http://dx.doi.org/10.1152/ajpendo.00296.2017.

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Treatment of nonalcoholic fatty liver disease (NAFLD) focuses on the underlying metabolic syndrome, and Roux-en-Y gastric bypass surgery (RYGB) remains one of the most effective options. In rodents and human patients, RYGB induces an increase in the gene and protein expression levels of the M2 isoenzyme of pyruvate kinase (PKM2) in the jejunum. Since PKM2 can be secreted in the circulation, our hypothesis was that the circulating levels of PKM2 increase after RYGB. Our data, however, revealed an unexpected finding and a potential new role of PKM2 for the natural history of metabolic syndrome a

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Li, Le, Lei Tang, Xiaoping Yang, et al. "Gene Regulatory Effect of Pyruvate Kinase M2 is Involved in Renal Inflammation in Type 2 Diabetic Nephropathy." Experimental and Clinical Endocrinology & Diabetes 128, no. 09 (2020): 599–606. http://dx.doi.org/10.1055/a-1069-7290.

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Abstract Background and Aims The inflammation of glomerular endothelial cells induces and promotes the activation of macrophages and contributes to the development of diabetic nephropathy. Thus, this study aimed to investigate the gene regulatory effect and potential role of pyruvate kinase M2 (PKM2) in inflammatory response in diabetic nephropathy. Methods The plasma PKM2 levels of patients with diabetes were evaluated. Eight-week-old mice were divided into three groups (WT, db/db mice, and db/db mice treated with TEPP-46) and raised for 12 weeks. Blood and kidney samples were collected at th

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Puckett, Dexter L., Mohammed Alquraishi, Winyoo Chowanadisai, and Ahmed Bettaieb. "The Role of PKM2 in Metabolic Reprogramming: Insights into the Regulatory Roles of Non-Coding RNAs." International Journal of Molecular Sciences 22, no. 3 (2021): 1171. http://dx.doi.org/10.3390/ijms22031171.

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Pyruvate kinase is a key regulator in glycolysis through the conversion of phosphoenolpyruvate (PEP) into pyruvate. Pyruvate kinase exists in various isoforms that can exhibit diverse biological functions and outcomes. The pyruvate kinase isoenzyme type M2 (PKM2) controls cell progression and survival through the regulation of key signaling pathways. In cancer cells, the dimer form of PKM2 predominates and plays an integral role in cancer metabolism. This predominance of the inactive dimeric form promotes the accumulation of phosphometabolites, allowing cancer cells to engage in high levels of

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James, Andrew D., Daniel A. Richardson, In-Whan Oh, et al. "Cutting off the fuel supply to calcium pumps in pancreatic cancer cells: role of pyruvate kinase-M2 (PKM2)." British Journal of Cancer 122, no. 2 (2019): 266–78. http://dx.doi.org/10.1038/s41416-019-0675-3.

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Abstract Background Pancreatic ductal adenocarcinoma (PDAC) has poor survival and treatment options. PDAC cells shift their metabolism towards glycolysis, which fuels the plasma membrane calcium pump (PMCA), thereby preventing Ca2+-dependent cell death. The ATP-generating pyruvate kinase-M2 (PKM2) is oncogenic and overexpressed in PDAC. This study investigated the PKM2-derived ATP supply to the PMCA as a potential therapeutic locus. Methods PDAC cell growth, migration and death were assessed by using sulforhodamine-B/tetrazolium-based assays, gap closure assay and poly-ADP ribose polymerase (P

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Ouyang, Xinxing, Yuheng Han, Guojun Qu, et al. "Metabolic regulation of T cell development by Sin1–mTORC2 is mediated by pyruvate kinase M2." Journal of Molecular Cell Biology 11, no. 2 (2018): 93–106. http://dx.doi.org/10.1093/jmcb/mjy065.

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Abstract Glucose metabolism plays a key role in thymocyte development. The mammalian target of rapamycin complex 2 (mTORC2) is a critical regulator of cell growth and metabolism, but its role in early thymocyte development and metabolism has not been fully studied. We show here that genetic ablation of Sin1, an essential component of mTORC2, in T lineage cells results in severely impaired thymocyte development at the CD4−CD8− double negative (DN) stages but not at the CD4+CD8+ double positive (DP) or later stages. Notably, Sin1-deficient DN thymocytes show markedly reduced proliferation and gl

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Ren, JunYu, Wenliang Li, Guoqing Pan, et al. "miR-142-3p Modulates Cell Invasion and Migration via PKM2-Mediated Aerobic Glycolysis in Colorectal Cancer." Analytical Cellular Pathology 2021 (July 13, 2021): 1–8. http://dx.doi.org/10.1155/2021/9927720.

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Decreased expression of miR-142-3p was observed in human cancers. However, the function and mechanism of miR-142-3p in human colorectal cancer remain obscure. The expressions of miR-142-3p in human colorectal cancer tissues and cell lines were measured by RT-qPCR. The effects of miR-142-3p on cell invasion and migration were detected by transwell assays. The efficiency of aerobic glycolysis was determined by glucose consumption and lactate production. Dual-luciferase reporter assays were performed to confirm the correlation between miR-142-3p and pyruvate kinase isozyme M2 (PKM2). The level of

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Zhao, Xuezhu, Fancheng Tan, Xiaoru Cao, et al. "PKM2-dependent glycolysis promotes the proliferation and migration of vascular smooth muscle cells during atherosclerosis." Acta Biochimica et Biophysica Sinica 52, no. 1 (2019): 9–17. http://dx.doi.org/10.1093/abbs/gmz135.

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Abstract Increased glycolysis is involved in the proliferation and migration of vascular smooth muscle cells (VSMCs). Pyruvate kinase isoform M2 (PKM2), a key rate-limiting enzyme in glycolysis, accelerates the proliferation and migration of tumor cells. Although the intracellular mechanisms associated with oxidized low-density lipoprotein (oxLDL)-stimulated VSMC proliferation and migration have been extensively explored, it is still unclear whether oxLDL promotes the proliferation and migration of VSMCs by enhancing PKM2-dependent glycolysis. In the present study, we detected PKM2 expression

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Li, Yunfeng, Yongsheng Chang, Lifeng Zhang, et al. "High glucose upregulates pantothenate kinase 4 (PanK4) and thus affects M2-type pyruvate kinase (Pkm2)." Molecular and Cellular Biochemistry 277, no. 1-2 (2005): 117–25. http://dx.doi.org/10.1007/s11010-005-5535-1.

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Yuan, Peng, Yiyi Zhou, Rui Wang, et al. "TRIM58 Interacts with Pyruvate Kinase M2 to Inhibit Tumorigenicity in Human Osteosarcoma Cells." BioMed Research International 2020 (March 7, 2020): 1–9. http://dx.doi.org/10.1155/2020/8450606.

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Background. Tripartite motif containing 58 (TRIM58), an E3 ubiquitin ligase, is reported as a suppressor gene in certain human tumors. However, the biological function of TRIM58 in osteosarcoma (OS) is still less identified. Methods. In the present study, TRIM58 induced silencing and overexpression in OS cells using RNA interference (RNAi) and lentiviral-mediated vector, respectively. Cell proliferation profiles were analyzed using cell counting kit-8 (CCK-8) assay. Cell apoptosis profiles were determined using a flow cytometer. qRT-PCR and western blot were used to determine gene expression.

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Wong, Nicholas, Jason De Melo, and Damu Tang. "PKM2, a Central Point of Regulation in Cancer Metabolism." International Journal of Cell Biology 2013 (2013): 1–11. http://dx.doi.org/10.1155/2013/242513.

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Aerobic glycolysis is the dominant metabolic pathway utilized by cancer cells, owing to its ability to divert glucose metabolites from ATP production towards the synthesis of cellular building blocks (nucleotides, amino acids, and lipids) to meet the demands of proliferation. The M2 isoform of pyruvate kinase (PKM2) catalyzes the final and also a rate-limiting reaction in the glycolytic pathway. In the PK family, PKM2 is subjected to a complex regulation by both oncogenes and tumour suppressors, which allows for a fine-tone regulation of PKM2 activity. The less active form of PKM2 drives gluco

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Mohammad, Goran Hamid, Vessela Vassileva, Pilar Acedo, et al. "Targeting Pyruvate Kinase M2 and Lactate Dehydrogenase A Is an Effective Combination Strategy for the Treatment of Pancreatic Cancer." Cancers 11, no. 9 (2019): 1372. http://dx.doi.org/10.3390/cancers11091372.

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Reprogrammed glucose metabolism is one of the hallmarks of cancer, and increased expression of key glycolytic enzymes, such as pyruvate kinase M2 (PKM2) and lactate dehydrogenase A (LDHA), has been associated with poor prognosis in various malignancies. Targeting these enzymes could attenuate aerobic glycolysis and inhibit tumor proliferation. We investigated whether the PKM2 activator, TEPP-46, and the LDHA inhibitor, FX-11, can be combined to inhibit in vitro and in vivo tumor growth in preclinical models of pancreatic cancer. We assessed PKM2 and LDHA expression, enzyme activity, and cell p

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Zheng, Mengying, Chunyan Liu, Yuanyuan Shao, et al. "The Effect of Pyruvate Kinase M2: Inhibitor(shikonin) on the Function of Mdc in Severe Aplastic Anemia Mouse Model." Blood 134, Supplement_1 (2019): 5021. http://dx.doi.org/10.1182/blood-2019-126726.

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Severe aplastic anemia (SAA) is a rare disease characterized by severe pancytopenia and bone marrow failure. Over-activated myeloid dendritic cells (mDCs) play an important role in the pathogenesis of SAA. In recent years, the role of pyruvate kinase M2 (PKM2) in DC function and autoimmune response has been gradually recognized. In this study, an immune attack-mediated AA mouse model was constructed by total body irradiation and lymphocyte infusion. The AA model mice showed pancytopenia, decreased ratio of CD4+/CD8+ cells, increased expression of cytotoxic molecules perforin and granzyme in CD

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Shao, Zonghong, and Mengying Zheng. "Abnormal Levels of PKM2 in Mdcs from Patients with Severe Aplastic." Blood 126, no. 23 (2015): 4766. http://dx.doi.org/10.1182/blood.v126.23.4766.4766.

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Abstract Severe aplastic anemia (SAA) is a hematologic disease characterized by pancytopenia with severe bone marrow failure. Our previous studies have demonstrated that activated myeloid dendritic cells (mDCs) increased in the bone marrow of SAA patients, which might promote Th0 cells to polarize to Th1 cells and cause the subsequent over-function of T lymphocytes and hematopoiesis failure in SAA. The other notable finding in our study is that abnormal expression of pyruvate kinase M2 (PKM2) in mDCs from SAA patients may be one of the reason for mDC hyperfunction. Human pyruvate kinase M2, wh

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Irokawa, Hayato, Satoshi Numasaki, Shin Kato, et al. "Comprehensive analyses of the cysteine thiol oxidation of PKM2 reveal the effects of multiple oxidation on cellular oxidative stress response." Biochemical Journal 478, no. 7 (2021): 1453–70. http://dx.doi.org/10.1042/bcj20200897.

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Redox regulation of proteins via cysteine residue oxidation is involved in the control of various cellular signal pathways. Pyruvate kinase M2 (PKM2), a rate-limiting enzyme in glycolysis, is critical for the metabolic shift from glycolysis to the pentose phosphate pathway under oxidative stress in cancer cell growth. The PKM2 tetramer is required for optimal pyruvate kinase (PK) activity, whereas the inhibition of inter-subunit interaction of PKM2 induced by Cys358 oxidation has reduced PK activity. In the present study, we identified three oxidation-sensitive cysteine residues (Cys358, Cys42

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Bhardwaj, Abhishek, and Sanjeev Das. "SIRT6 deacetylates PKM2 to suppress its nuclear localization and oncogenic functions." Proceedings of the National Academy of Sciences 113, no. 5 (2016): E538—E547. http://dx.doi.org/10.1073/pnas.1520045113.

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SIRT6 (sirtuin 6) is a member of sirtuin family of deacetylases involved in diverse processes including genome stability, metabolic homeostasis, and tumorigenesis. However, the role of SIRT6 deacetylase activity in its tumor-suppressor functions is not well understood. Here we report that SIRT6 binds to and deacetylates nuclear PKM2 (pyruvate kinase M2) at the lysine 433 residue. PKM2 is a glycolytic enzyme with nonmetabolic nuclear oncogenic functions. SIRT6-mediated deacetylation results in PKM2 nuclear export. We further have identified exportin 4 as the specific transporter mediating PKM2

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Zhu, Haiyan, Hui Luo, Xuejie Zhu, Xiaoli Hu, Lihong Zheng, and Xueqiong Zhu. "Pyruvate kinase M2 (PKM2) expression correlates with prognosis in solid cancers: a meta-analysis." Oncotarget 8, no. 1 (2016): 1628–40. http://dx.doi.org/10.18632/oncotarget.13703.

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He, Yunhua, Yuchan Wang, Hong Liu, et al. "Pyruvate kinase isoform M2 (PKM2) participates in multiple myeloma cell proliferation, adhesion and chemoresistance." Leukemia Research 39, no. 12 (2015): 1428–36. http://dx.doi.org/10.1016/j.leukres.2015.09.019.

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Lai, Chou, Lin, et al. "Pyruvate Kinase M2 Expression: A Potential Metabolic Biomarker to Differentiate Endometrial Precancer and Cancer That Is Associated with Poor Outcomes in Endometrial Carcinoma." International Journal of Environmental Research and Public Health 16, no. 23 (2019): 4589. http://dx.doi.org/10.3390/ijerph16234589.

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Background: Pyruvate kinase M2 (PKM2) is a regulator of the processes of glycolysis and oxidative phosphorylation, but the roles that it plays in endometrial cancer remain largely unknown. This study evaluated the PKM2 expression in normal endometrium, endometrial hyperplasia, and endometrial carcinoma, and its prognostic value was investigated in endometrial carcinoma patients. Methods: A hospital-based retrospective review was conducted to examine the immunohistochemical PKM2 distribution in 206 endometrium samples from biopsies or hysterectomies. The immunoreactivity of PKM2 was divided int

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Le, Sheng, Hao Zhang, Xiaofan Huang та ін. "PKM2 Activator TEPP-46 Attenuates Thoracic Aortic Aneurysm and Dissection by Inhibiting NLRP3 Inflammasome-Mediated IL-1β Secretion". Journal of Cardiovascular Pharmacology and Therapeutics 25, № 4 (2020): 364–76. http://dx.doi.org/10.1177/1074248420919966.

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Background: The development of thoracic aortic aneurysm and dissection (TAAD) is mediated by inflammasome activation, which exacerbates the secretion of pro-inflammatory cytokines, chemokines, matrix metalloproteinases (MMPs), and reactive oxygen species (ROS). The glycolytic enzyme pyruvate kinase M2 (PKM2) has shown a protective role against various disorders with an inflammatory basis, such as sepsis, tumorigenesis, and diabetic nephropathy. However, its potential role in TAAD has not been investigated so far. Approach and Results: We analyzed aortic tissues from TAAD patients and the β-ami

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Li, Ning, Dandan Meng, Yue Xu, et al. "Pyruvate Kinase M2 Knockdown Suppresses Migration, Invasion, and Epithelial-Mesenchymal Transition of Gastric Carcinoma via Hypoxia-Inducible Factor Alpha/B-Cell Lymphoma 6 Pathway." BioMed Research International 2020 (December 9, 2020): 1–10. http://dx.doi.org/10.1155/2020/7467104.

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Gastric carcinoma is a common malignant cancer. Pyruvate kinase M2 (PKM2) is highly expressed in cancers, including gastric carcinoma. However, its function and molecular mechanism in gastric carcinoma remains unclear. Here, we aimed to explore the function and the underlying mechanism of PKM2 on malignant phenotypes in gastric carcinoma. In this study, the mRNA levels and protein levels of PKM2 in gastric carcinoma cell lines and normal gastric mucosa epithelial cell lines were detected using quantitative real-time PCR and western blot, respectively. PKM2 was downregulated by siRNA transfecti

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Shirai, Tsuyoshi, Rafal R. Nazarewicz, Barbara B. Wallis, et al. "The glycolytic enzyme PKM2 bridges metabolic and inflammatory dysfunction in coronary artery disease." Journal of Experimental Medicine 213, no. 3 (2016): 337–54. http://dx.doi.org/10.1084/jem.20150900.

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Abnormal glucose metabolism and enhanced oxidative stress accelerate cardiovascular disease, a chronic inflammatory condition causing high morbidity and mortality. Here, we report that in monocytes and macrophages of patients with atherosclerotic coronary artery disease (CAD), overutilization of glucose promotes excessive and prolonged production of the cytokines IL-6 and IL-1β, driving systemic and tissue inflammation. In patient-derived monocytes and macrophages, increased glucose uptake and glycolytic flux fuel the generation of mitochondrial reactive oxygen species, which in turn promote d

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Cho, Eun-Seok, Hyeon-Jeong Jeon, Si-Woo Lee, et al. "Association of a Pyruvate Kinase M2 (PKM2) Polymorphism with Back Fat Thickness in Berkshire Pigs." Journal of Animal Science and Technology 55, no. 6 (2013): 515–20. http://dx.doi.org/10.5187/jast.2013.55.6.515.

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Lee, Jungwoon, Hye Kyoung Kim, Yong-Mahn Han, and Jungho Kim. "Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription." International Journal of Biochemistry & Cell Biology 40, no. 5 (2008): 1043–54. http://dx.doi.org/10.1016/j.biocel.2007.11.009.

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Almousa, Ahmed A., Marc Morris, Sharyle Fowler, Jennifer Jones, and Jane Alcorn. "Elevation of serum pyruvate kinase M2 (PKM2) in IBD and its relationship to IBD indices." Clinical Biochemistry 53 (March 2018): 19–24. http://dx.doi.org/10.1016/j.clinbiochem.2017.12.007.

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