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Journal articles on the topic 'Pyruvate kinase M2'

Author: Grafiati
Published: 4 June 2021
Last updated: 9 February 2022

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1

Yang, W., and Z. Lu. "Pyruvate kinase M2 at a glance." Journal of Cell Science 128, no. 9 (March 13, 2015): 1655–60. http://dx.doi.org/10.1242/jcs.166629.

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2

Zhao, Penglong, Mengyan Zhou, Ruixiang Chen, and Renjie Su. "Suppressed “Warburg Effect” in Nasopharyngeal Carcinoma Via the Inhibition of Pyruvate Kinase Type M2-Mediated Energy Generation Pathway." Technology in Cancer Research & Treatment 19 (January 1, 2020): 153303382094580. http://dx.doi.org/10.1177/1533033820945804.

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Warburg effect describes the abnormal energy metabolism in cancer cells and pyruvate kinase type M2 is involved in the regulation of this effect. In the current study, the role of pyruvate kinase type M2 in the initiation of Warburg effect in nasopharyngeal carcinoma cells was explored. The expression status of pyruvate kinase type M2 was detected in nasopharyngeal carcinoma samples and analyzed by different clinicopathological characteristics. Then the level of pyruvate kinase type M2 was suppressed in 2 nasopharyngeal carcinoma cell lines. The effects of pyruvate kinase type M2 inhibition on cell viability, apoptosis, invasion, glucose uptake, ATP generation, and glycolysis metabolism were determined. The data showed that the high expression of pyruvate kinase type M2 in nasopharyngeal carcinoma tissues was associated with the larger tumor size and advanced metastasis in the patients. The inhibition of pyruvate kinase type M2 resulted in the repressed proliferation and invasion in nasopharyngeal carcinoma cells, along with the increased apoptotic rate. The lack of pyruvate kinase type M2 function inhibited glucose uptake, while increased ATP generation in nasopharyngeal carcinoma cells. Moreover, the production of glycolysis metabolites, including pyruvic acid, lactate, citrate, and malate, was also suppressed by pyruvate kinase type M2 inhibition. At molecular level, the expressions of glucose transporter and hexokinase 2 were downregulated by pyruvate kinase type M2 inhibition, confirming the changes in glucose metabolism. Collectively, the current study demonstrated that the function of pyruvate kinase type M2 was important to maintain the proliferation and invasion of nasopharyngeal carcinoma cells, and the inhibition of the factor would antagonize nasopharyngeal carcinoma by blocking Warburg effect.
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3

Gough, N. R. "Promoting Proliferation with Nuclear Pyruvate Kinase M2." Science Signaling 4, no. 202 (December 6, 2011): ec337-ec337. http://dx.doi.org/10.1126/scisignal.4202ec337.

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4

Cerwenka, Herwig. "Tumor M2-Pyruvate Kinase and Pancreatic Cancer." Pancreas 37, no. 2 (August 2008): 221–22. http://dx.doi.org/10.1097/mpa.0b013e3181619a45.

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5

Gupta, Vibhor, and Rameshwar N. K. Bamezai. "Human pyruvate kinase M2: A multifunctional protein." Protein Science 19, no. 11 (October 26, 2010): 2031–44. http://dx.doi.org/10.1002/pro.505.

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6

Kim, Boa, Cholsoon Jang, Harita Dharaneeswaran, Jian Li, Mohit Bhide, Steven Yang, Kristina Li, and Zolt Arany. "Endothelial pyruvate kinase M2 maintains vascular integrity." Journal of Clinical Investigation 128, no. 10 (September 17, 2018): 4543–56. http://dx.doi.org/10.1172/jci120912.

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7

Zou, Kejian, Yaodong Wang, Yan Hu, Liansheng Zheng, Wanfu Xu, and Guoxin Li. "Specific tumor-derived CCL2 mediated by pyruvate kinase M2 in colorectal cancer cells contributes to macrophage recruitment in tumor microenvironment." Tumor Biology 39, no. 3 (March 2017): 101042831769596. http://dx.doi.org/10.1177/1010428317695962.

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Development of colorectal cancer has been considered as a result of imbalance of pro- and anti-inflammatory intestinal microenvironment accompanied by macrophage recruitment. Despite macrophages are implicated in remodeling tumor microenvironment, the mechanism of macrophage recruitment is not fully elucidated yet. In this study, we reported clinical association of highly expressed pyruvate kinase M2 in colorectal cancer with macrophage attraction. The conditioned medium from Caco-2 and HT-29 cells with depleted pyruvate kinase M2 dramatically reduced macrophage recruitment, which is reversed by addition of, a critical chemotaxis factor to macrophage migration, rCCL2. Silencing of endogenous pyruvate kinase M2 markedly decreased CCL2 expression and secretion by real-time quantitative polymerase chain reaction and enzyme-linked immunosorbent assay. Endogenous pyruvate kinase M2 interacted with p65 and mediated nuclear factor-κB signaling pathway and mainly regulated phosphorylation of Ser276 on p65 nuclear factor-κB. In addition, inhibition of macrophage recruitment caused by pyruvate kinase M2 silencing was rescued by ectopic expression of p65. Interestingly, pyruvate kinase M2 highly expressed in colorectal cancer tissue, which is correction with macrophage distribution. Taken together, we revealed a novel mechanism of pyruvate kinase M2 in promoting colorectal cancer progression by recruitment of macrophages through p65 nuclear factor-κB–mediated expression of CCL2.
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8

Gao, Xueliang, Haizhen Wang, Jenny J. Yang, Jing Chen, Jiang Jie, Liangwei Li, Yinwei Zhang, and Zhi-Ren Liu. "Reciprocal Regulation of Protein Kinase and Pyruvate Kinase Activities of Pyruvate Kinase M2 by Growth Signals." Journal of Biological Chemistry 288, no. 22 (April 10, 2013): 15971–79. http://dx.doi.org/10.1074/jbc.m112.448753.

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9

Kumar, Yogesh, Niteen Tapuria, Naveed Kirmani, and Brian R. Davidson. "Tumour M2-pyruvate kinase: a gastrointestinal cancer marker." European Journal of Gastroenterology & Hepatology 19, no. 3 (March 2007): 265–76. http://dx.doi.org/10.1097/meg.0b013e3280102f78.

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10

Christofk, Heather R., Matthew G. Vander Heiden, Ning Wu, John M. Asara, and Lewis C. Cantley. "Pyruvate kinase M2 is a phosphotyrosine-binding protein." Nature 452, no. 7184 (March 2008): 181–86. http://dx.doi.org/10.1038/nature06667.

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11

Hsieh, I.-Shan, Balraj Gopula, Chi-Chi Chou, Hsiang-Yi Wu, Geen-Dong Chang, Wen-Jin Wu, Chih-Shiang Chang, Po-Chen Chu, and Ching S. Chen. "Development of Novel Irreversible Pyruvate Kinase M2 Inhibitors." Journal of Medicinal Chemistry 62, no. 18 (August 29, 2019): 8497–510. http://dx.doi.org/10.1021/acs.jmedchem.9b00763.

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12

Garcia-Gonzalo, Francesc R., Cristina Cruz, Purificación Muñoz, Sybille Mazurek, Erich Eigenbrodt, Francesc Ventura, Ramon Bartrons, and Jose Luis Rosa. "Interaction between HERC1 and M2-type pyruvate kinase." FEBS Letters 539, no. 1-3 (March 6, 2003): 78–84. http://dx.doi.org/10.1016/s0014-5793(03)00205-9.

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13

Hegele, A., Z. Varga, B. Kosche, T. Stief, A. Heidenreich, and R. Hofmann. "Pyruvate Kinase Type Tumor M2 in Urological Malignancies." Urologia Internationalis 70, no. 1 (2003): 55–58. http://dx.doi.org/10.1159/000067707.

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14

Liu, Kun, Fanzhou Li, Haichao Han, Yue Chen, Zebin Mao, Jianyuan Luo, Yingming Zhao, Bin Zheng, Wei Gu, and Wenhui Zhao. "Parkin Regulates the Activity of Pyruvate Kinase M2." Journal of Biological Chemistry 291, no. 19 (March 14, 2016): 10307–17. http://dx.doi.org/10.1074/jbc.m115.703066.

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15

Iqbal, Mohd Askandar, Vibhor Gupta, Prakasam Gopinath, Sybille Mazurek, and Rameshwar N. K. Bamezai. "Pyruvate kinase M2 and cancer: an updated assessment." FEBS Letters 588, no. 16 (April 18, 2014): 2685–92. http://dx.doi.org/10.1016/j.febslet.2014.04.011.

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16

Ignacak, J., and M. Gumińska. "Comparison of pyruvate kinase variants from rat liver and Morris hepatoma 7777, obtained by an affinity chromatography on blue sepharose CL-6B." Acta Biochimica Polonica 40, no. 2 (June 30, 1993): 261–67. http://dx.doi.org/10.18388/abp.1993_4827.

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Fractions A (salted out by ammonium sulphate between 21-30% saturation), and fractions B (salted out between 51-70% saturation) of pyruvate kinase (EC 2.7.1.40.) corresponding respectively to pyruvate kinase types L and M2 from rat liver and Morris hepatoma 7777 were purified by an affinity chromatography on Blue Sepharose CL-6B. Peaks of inactive proteins were eliminated and the enzyme fractions bound biospecifically to the gels were eluted by free ADP. The molecular mass of purified hepatoma pyruvate kinase fraction B was smaller than that of liver pyruvate kinase fraction B. Morris hepatoma pyruvate kinase fraction B represented a variant of type M2, characterised by greatest affinity to 2-phosphoenolpyruvate as a main substrate and different sensitivity to low-molecular effectors in comparison with types L from both liver and hepatoma and in comparison with type M2 from normal rat liver. Only this hepatoma fraction B showed a tumour specific sensitivity to L-cysteine and was insensitive to normal signal molecules i.e. to ATP and fructose-1,6-diphosphate which influence liver pyruvate kinase activity. L-Cysteine inhibited the tumour fraction B of pyruvate kinase by decreasing its Vmax and increasing the Km values in relation to 2-phosphoenolpyruvate.
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17

Chung-Faye, Guy, BuʼHussain Hayee, Susan Maestranzi, Nora Donaldson, Ian Forgacs, and Roy Sherwood. "Fecal M2-pyruvate kinase (M2-PK): A novel marker of intestinal inflammation." Inflammatory Bowel Diseases 13, no. 11 (November 2007): 1374–78. http://dx.doi.org/10.1002/ibd.20214.

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18

Vander Heiden, Matthew G., Heather R. Christofk, Eli Schuman, Alexander O. Subtelny, Hadar Sharfi, Edward E. Harlow, Jun Xian, and Lewis C. Cantley. "Identification of small molecule inhibitors of pyruvate kinase M2." Biochemical Pharmacology 79, no. 8 (April 2010): 1118–24. http://dx.doi.org/10.1016/j.bcp.2009.12.003.

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19

Liu, Vivian M., and Matthew G. Vander Heiden. "The Role of Pyruvate Kinase M2 in Cancer Metabolism." Brain Pathology 25, no. 6 (November 2015): 781–83. http://dx.doi.org/10.1111/bpa.12311.

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20

Spoden, Gilles A., Dieter Morandell, Daniela Ehehalt, Marc Fiedler, Pidder Jansen-Dürr, Martin Hermann, and Werner Zwerschke. "The SUMO-E3 ligase PIAS3 targets pyruvate kinase M2." Journal of Cellular Biochemistry 107, no. 2 (March 23, 2009): 293–302. http://dx.doi.org/10.1002/jcb.22125.

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21

Alquraishi, Mohammed, Dexter L. Puckett, Dina S. Alani, Amal S. Humidat, Victoria D. Frankel, Dallas R. Donohoe, Jay Whelan, and Ahmed Bettaieb. "Pyruvate kinase M2: A simple molecule with complex functions." Free Radical Biology and Medicine 143 (November 2019): 176–92. http://dx.doi.org/10.1016/j.freeradbiomed.2019.08.007.

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22

Yang, Weiwei, and Zhimin Lu. "Regulation and function of pyruvate kinase M2 in cancer." Cancer Letters 339, no. 2 (October 2013): 153–58. http://dx.doi.org/10.1016/j.canlet.2013.06.008.

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23

Apostolidi, Maria, Ioannis A. Vathiotis, Viswanathan Muthusamy, Patricia Gaule, Brandon M. Gassaway, David L. Rimm, and Jesse Rinehart. "Targeting Pyruvate Kinase M2 Phosphorylation Reverses Aggressive Cancer Phenotypes." Cancer Research 81, no. 16 (June 21, 2021): 4346–59. http://dx.doi.org/10.1158/0008-5472.can-20-4190.

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24

Sharma, Pankaj. "Molecular docking analysis of pyruvate kinase M2 with a potential inhibitor from the ZINC database." Bioinformation 17, no. 1 (January 31, 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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25

Gao, Xueliang, Haizhen Wang, Jenny J. Yang, Xiaowei Liu, and Zhi-Ren Liu. "Pyruvate Kinase M2 Regulates Gene Transcription by Acting as a Protein Kinase." Molecular Cell 45, no. 5 (March 2012): 598–609. http://dx.doi.org/10.1016/j.molcel.2012.01.001.

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26

Zhan, Cheng, Li Yan, Lin Wang, Jun Ma, Wei Jiang, Yongxing Zhang, Yu Shi, and Qun Wang. "Isoform Switch of Pyruvate Kinase M1 Indeed Occurs but Not to Pyruvate Kinase M2 in Human Tumorigenesis." PLOS ONE 10, no. 3 (March 4, 2015): e0118663. http://dx.doi.org/10.1371/journal.pone.0118663.

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27

Bunawan, Nur Chandra, and Marcellus Simadibrata. "The Role of Fecal M2-Pyruvate Kinase (M2-PK) in Colorectal Cancer Screening." Indonesian Journal of Gastroenterology, Hepatology, and Digestive Endoscopy 18, no. 1 (July 14, 2017): 38. http://dx.doi.org/10.24871/181201738-42.

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28

Hulleman, E., M. J. Broekhuis, R. Pieters, and M. L. Den Boer. "Pyruvate kinase M2 and prednisolone resistance in acute lymphoblastic leukemia." Haematologica 94, no. 9 (September 1, 2009): 1322–24. http://dx.doi.org/10.3324/haematol.2009.011437.

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29

Gupta, Vibhor, Kathryn Wellen, Sybille Mazurek, and Rameshwar N. Bamezai. "Pyruvate Kinase M2: Regulatory Circuits and Potential for Therapeutic Intervention." Current Pharmaceutical Design 20, no. 15 (May 12, 2014): 2595–606. http://dx.doi.org/10.2174/13816128113199990484.

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30

Zhou, Haiping, Xing Wang, Lan Mo, Yan Liu, Feng He, Fenglin Zhang, Kuo-How Huang, and Xue-Ru Wu. "Role of isoenzyme M2 of pyruvate kinase in urothelial tumorigenesis." Oncotarget 7, no. 17 (March 16, 2016): 23947–60. http://dx.doi.org/10.18632/oncotarget.8114.

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31

Anastasiou, Dimitrios, Yimin Yu, William J. Israelsen, Jian-Kang Jiang, Matthew B. Boxer, Bum Soo Hong, Wolfram Tempel, et al. "Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis." Nature Chemical Biology 8, no. 10 (August 26, 2012): 839–47. http://dx.doi.org/10.1038/nchembio.1060.

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32

Goldberg, Michael S., and Phillip A. Sharp. "Pyruvate kinase M2-specific siRNA induces apoptosis and tumor regression." Journal of Experimental Medicine 209, no. 2 (January 23, 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 specific knockdown of the former, resulting in decreased viability and increased apoptosis in multiple cancer cell lines but less so in normal fibroblasts or endothelial cells. In vivo delivery of siPKM2 additionally causes substantial tumor regression of established xenografts. Our results suggest that the inherent nucleotide-level specificity of siRNA can be harnessed to develop therapeutics that target isoform-specific exons in genes exhibiting differential splicing patterns in various cell types.
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33

Singh, Jay Prakash, Kevin Qian, Jeong-Sang Lee, Jinfeng Zhou, Xuemei Han, Bichen Zhang, Qunxiang Ong, et al. "O-GlcNAcase targets pyruvate kinase M2 to regulate tumor growth." Oncogene 39, no. 3 (September 9, 2019): 560–73. http://dx.doi.org/10.1038/s41388-019-0975-3.

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34

Isidor, Marie S., Sally Winther, Lasse K. Markussen, Astrid L. Basse, Bjørn Quistorff, Jan Nedergaard, Brice Emanuelli, and Jacob B. Hansen. "Pyruvate kinase M2 represses thermogenic gene expression in brown adipocytes." FEBS Letters 594, no. 7 (April 2020): 1218–25. http://dx.doi.org/10.1002/1873-3468.13716.

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35

Anitha, M., G. Kaur, N. Z. Baquer, and R. Bamezai. "Dominant Negative Effect of Novel Mutations in Pyruvate Kinase-M2." DNA and Cell Biology 23, no. 7 (July 2004): 442–49. http://dx.doi.org/10.1089/1044549041474797.

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36

Mazurek, S., H. Grimm, C. B. Boschek, P. Vaupel, and E. Eigenbrodt. "Pyruvate kinase type M2: a crossroad in the tumor metabolome." British Journal of Nutrition 87, S1 (January 2002): S23. http://dx.doi.org/10.1079/bjn2001454.

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37

Bettaieb, Ahmed, Jesse Bakke, Naoto Nagata, Kosuke Matsuo, Yannan Xi, Siming Liu, Daniel AbouBechara, et al. "Protein Tyrosine Phosphatase 1B Regulates Pyruvate Kinase M2 Tyrosine Phosphorylation." Journal of Biological Chemistry 288, no. 24 (May 2, 2013): 17360–71. http://dx.doi.org/10.1074/jbc.m112.441469.

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38

Mellati, Ali A., Meral Yücel, Nur Altinörs, and Ufuk Gündüz. "Purification and characterization of human meningioma M2-type pyruvate kinase." Clinical Biochemistry 26, no. 5 (October 1993): 383–88. http://dx.doi.org/10.1016/0009-9120(93)90114-l.

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39

Ignacak, J., and M. Gumińska. "N-acetylneuraminic acid, phosphate and thiol groups of pyruvate kinase isoenzymes from Morris hepatoma 7777 and normal rat liver." Acta Biochimica Polonica 44, no. 2 (June 30, 1997): 201–8. http://dx.doi.org/10.18388/abp.1997_4414.

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The highest amount of N-acetylneuraminic acid (AcNeu) was found in pyruvate kinase isoenzyme L from normal rat liver (24 moles/mole of enzyme tetramer), with the highest electrophoretic mobility. On the other hand, isoenzyme M2 from Morris hepatoma 7777, with the lowest electrophoretic mobility, had the lowest AcNeu content (5 moles/mole of enzyme tetramer). This tumour isoenzyme M2 of pyruvate kinase was, however, characterised by the highest phosphate content (12 moles/mole protein), in comparison to isoenzyme L (3 moles/mole protein) or normal liver isoenzyme M2 (6 moles/mole protein). This could indicate a regulatory change caused by reversible enzyme phosphorylation and dephosphorylation or sialization and desialization. Despite these differences, the sum of the two negatively charged residues was lower in tumour pyruvate kinase isoenzyme M2, with the slowest migration rate, than in normal rat liver isoenzyme M2. Moreover, isoenzyme M2 from tumour material, in comparison with isoenzyme M2 from normal rat liver, had a twice as high content of thiol groups (20 moles/mole protein), especially of free and superficially located ones, than the isoenzyme M2 from normal liver (10 moles/mole protein). This may explain abnormal susceptibility of tumour isoenzyme M2 to stereospecific inhibition by exogenous L-cysteine, and indicate genetically dependent changes in amino-acid content of tumour enzyme which take place during cell tumourigenic transformation.
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40

Gumińska, M., J. Ignacak, T. Kedryna, and M. B. Stachurska. "Tumor-specific pyruvate kinase isoenzyme M2 involved in biochemical strategy of energy generation in neoplastic cells." Acta Biochimica Polonica 44, no. 4 (December 31, 1997): 711–24. http://dx.doi.org/10.18388/abp.1997_4373.

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The differences in properties of pyruvate kinase (EC 2.1.7.40) from normal tissues and animal or human tumors are described and their significance for various metabolic abnormalities is reviewed. The tumor variant gamma3 from M2 isoenzyme of pyruvate kinase sensitive to L-cysteine inhibition, when over-expressed, can be used as a marker of tumorigenic transformation. It seems that this variant represents a tumor-specific oncoprotein, involved in a novel metabolic strategy of energy generation during increased cell proliferation.
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41

Choi, Hae-Seul, Chang-Zhu Pei, Jun-Hyeok Park, Soo-Yeon Kim, Seung-Yeon Song, Gyeong-Jin Shin, and Kwang-Hyun Baek. "Protein Stability of Pyruvate Kinase Isozyme M2 Is Mediated by HAUSP." Cancers 12, no. 6 (June 12, 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 spectrometry (MALDI-TOF/MS) analysis. The analysis showed that pyruvate kinase isoenzyme M2 (PKM2) was likely to be one of the substrates for HAUSP. Further study revealed that PKM2 binds to HAUSP, confirming the interaction between these proteins, and that PKM2 possesses the putative HAUSP binding motif, E or P/AXXS. Therefore, we generated mutant forms of PKM2 S57A, S97A, and S346A, and found that S57A had less binding affinity. In a previous study, we demonstrated that PKM2 is regulated by the UPS, and that HAUSP- as a DUB-acted on PKM2, thus siRNA for HAUSP increases PKM2 ubiquitination. Our present study newly highlights the direct interaction between HAUSP and PKM2.
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42

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 (September 25, 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 specimens and performed a functional analysis of human OSCC cells. We found that the PKM2/PKM1 ratio was higher in OSCC cells than in adjacent normal mucosal cells and in samples obtained from dysplasia patients. Furthermore, PKM2 expression was strongly correlated with OSCC tumor progression on immunohistochemistry. PKM2 expression was higher during cell growth, invasion, and apoptosis in HSC3 cells, which show a high energy flow and whose metabolism depends on aerobic glycolysis and oxidative phosphorylation. PKM2 expression was also associated with the production of reactive oxygen species (ROS) and integration of glutamine into lactate. Our results suggested that PKM2 has a variety of tumor progressive functions in OSCC cells.
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Guo, Chen, Guan Li, Jianing Hou, Xingming Deng, Sheng Ao, Zhuofei Li, and Guoqing Lyu. "Tumor pyruvate kinase M2: A promising molecular target of gastrointestinal cancer." Chinese Journal of Cancer Research 30, no. 6 (2018): 669–76. http://dx.doi.org/10.21147/j.issn.1000-9604.2018.06.11.

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44

Su, Yan, Sujuan Guo, Chunyan Liu, Na Li, Shuang Zhang, Yubin Ding, Xuemei Chen, et al. "Endometrial pyruvate kinase M2 is essential for decidualization during early pregnancy." Journal of Endocrinology 245, no. 3 (June 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 pregnancy and strongly expressed in the decidual zone after embryo implantation. PKM2 was dramatically increased with the onset of decidualization. Upon further exploration, PKM2 was found to be more highly expressed at the implantation sites than at the inter-implantation sites on days 5 to 7 of pregnancy. PKM2 expression was also significantly increased after artificial decidualization both in vivo and in vitro. After PKM2 expression was knocked down by siRNA, the number of embryo implantation sites in mice on day 7 of pregnancy was significantly reduced, and the decidualization markers BMP2 and Hoxa10 were also obviously downregulated in vivo and in vitro. Downregulated PKM2 could also compromise cell proliferation in primary endometrial stromal cells and in Ishikawa cells. The migration rate of Ishikawa cells was also obviously suppressed by si-PKM2 according to the wound healing assay. In conclusion, PKM2 might play an important role in decidualization during early pregnancy, and cell proliferation might be one pathway for PKM2 regulated decidualization.
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45

Ferguson, Emily C., and Jeffrey C. Rathmell. "New roles for pyruvate kinase M2: working out the Warburg effect." Trends in Biochemical Sciences 33, no. 8 (August 2008): 359–62. http://dx.doi.org/10.1016/j.tibs.2008.05.006.

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46

Varghese, Bentley, Gayathri Swaminathan, Alexander Plotnikov, Christos Tzimas, Ning Yang, Hallgeir Rui, and Serge Y. Fuchs. "Prolactin Inhibits Activity of Pyruvate Kinase M2 to Stimulate Cell Proliferation." Molecular Endocrinology 24, no. 12 (December 2010): 2356–65. http://dx.doi.org/10.1210/me.2010-0219.

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47

Shankar Babu, Mani, Sailendra Mahanta, Alexander J. Lakhter, Takashi Hato, Subhankar Paul, and Samisubbu R. Naidu. "Lapachol inhibits glycolysis in cancer cells by targeting pyruvate kinase M2." PLOS ONE 13, no. 2 (February 2, 2018): e0191419. http://dx.doi.org/10.1371/journal.pone.0191419.

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48

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 (November 29, 2018): 3919. http://dx.doi.org/10.1182/blood-2018-99-117899.

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Abstract:
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 localization and conformation change from tetramer to dimer of PKM2. Importantly, SUMOylation of PKM2 is prevalent in a variety of leukemic cell lines as well as primary samples from patients with hematologic malignancies. In consistency, predominant nuclear localization and dimeric forms of PKM2 in leukemic cells were observed. Using in vitro SUMOylation reaction-coupled liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS), we identified K270 lysine residue of PKM2 as the SUMOylation target. Replacement of endogenous PKM2 with mutant PKM2K270 showed a significant shift of PKM2 from tetramer to dimer. To investigate the potential leukemogenic effect of PKM2 SUMOylation, murine hematopoietic progenitor 32D clone 3 (32Dcl3) transfectants expressing wild type(WT) or mutant PKM2K270 were generated and G-CSF-induced differentiation was evaluated by morphology appearance and expression of myeloid associated surface markers CD11b and Gr-1. The results showed that expression of WT PKM2 but not mutant PKM2K270 significantly blocked myeloid differentiation. Further investigations revealed that SUMO1 modification of PKM2 at K270 is essential in mediating the interaction between PKM2 and Runt-related transcription factor 1(RUNX1), a master transcriptional factor implicated in the differentiation of hematopoietic cells. This interaction led to a downregulation of RUNX1 during G-CSF-induced myeloid differentiation of 32D cells, which could be abrogated by expression of mutant PKM2K270. Collectively, these data indicated that SUMOylated PKM2 blocks myeloid differentiation through suppressing RUNX1. These findings reveal a novel nonmetabolic function of PKM2 in modulating myeloid differentiation and highlight the critical role of SUMOylation in leukemogenesis. Disclosures No relevant conflicts of interest to declare.
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Anastasiou, Dimitrios, Yimin Yu, William J. Israelsen, Jian-kang Jiang, Matthew B. Boxer, Bum Soo Hong, Wolfram Tempel, et al. "Erratum: Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis." Nature Chemical Biology 8, no. 12 (November 26, 2012): 1008. http://dx.doi.org/10.1038/nchembio1212-1008b.

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50

Dombrauckas, Jill D., Bernard D. Santarsiero, and Andrew D. Mesecar. "Structural Basis for Tumor Pyruvate Kinase M2 Allosteric Regulation and Catalysis†,‡." Biochemistry 44, no. 27 (July 2005): 9417–29. http://dx.doi.org/10.1021/bi0474923.

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