Relevant bibliographies by topics / Pyruvate kinase M2 (PKM2)

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Academic literature on the topic 'Pyruvate kinase M2 (PKM2)'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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

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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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Sturgill, Eric M., and Monica L. Guzman. "Cytokine Induced Nuclear Localization Of Pyruvate Kinase M2 In Acute Myeloid Leukemia." Blood 122, no. 21 (November 15, 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) plays a critical role in the maintenance of aerobic glycolysis in tumor cells and is important for their growth and development (Christofk et al. 2008). Pyruvate kinase produces pyruvate and one molecule of adenosine 5’-triphosphate (ATP) in the rate-limiting step of glycolysis. Pyruvate kinase coded for by PKM has two splice isoforms, the constitutively active PKM1 that exists only as a tetramer and PKM2 that can shift between a more active tetramer and less active dimers or monomers. The dynamic enzymatic activity of PKM2 is key to its preferential expression in tumor cells. By utilizing the less active form of PKM2, tumor cells can limit the levels of pyruvate available for OXPHOS and instead shunt glycolytic carbons towards anabolic processes. However, recent studies have revealed novel activities of PKM2 outside the realm of energy metabolism that also contribute to tumor formation, maintenance, and growth. The less active PKM2 dimer, whose structure is favored upon phosphorylation at Tyr105 (Hitosugi et al. 2009), can also translocate to the nucleus and act as a transcription factor for cell cycle associated genes like MYC and CCND1 upon stimulation with epidermal growth factor in certain cancer cell lines (Gao et al. 2012). Acute myeloid leukemia (AML) is a malignancy of hematopoietic progenitor cells characterized by the extraordinarily rapid growth of abnormal myeloid cells, making the proliferative influences of PKM2 an intriguing target for therapy. We have found that PKM2 is abundantly expressed in AML cell lines and primary AML patient samples and that low basal levels of PKM2 can be detected in their nuclei. Interestingly, stimulation with various cytokines such as IL-6 or GM-CSF can induce the nuclear translocation of PKM2 and association with histone H3 in these cells and concomitant treatment with PKM2 activating compounds that have been shown to promote its tetrameric structure and suppress tumor growth (Anastasiou et al. 2012) can inhibit this effect. These data show that the role of PKM2 in regulating transcription in addition to its metabolic activity may be important for the proliferation and maintenance of hematopoietic malignancies. Using fluorescence-activated cell sorting to isolate specific sub-populations of primary AML patient cells and elucidating PKM2’s interaction with protein kinases involved in known signaling pathways like JAK/STAT, ERK1/2, and FLT3, we show that the proliferative influences of PKM2 function and activity differ between AML cell phenotypes. For example, cells from AML patient samples sorted based on high or low levels of reactive oxygen species (ROS) differ in relative phosphorylation of PKM2 at Tyr105. These data, along with reports that the PKM2 dimer specifically plays a role in tumor cell antioxidant response (Anastasiou, et al. 2011) suggests that PKM2 may contribute to the maintenance of phenotypically ROS-low leukemia stem cells that are thought to contribute to patient relapse after achieving remission (Hope et al. 2004). Our data suggests that the broad cellular functions of PKM2 employed by AML cells and its direct influence on tumor growth and survival make it a promising potential target for therapy. Disclosures: No relevant conflicts of interest to declare.
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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 (November 29, 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 aerobic glycolysis compared to OXPHOS, which is well suited for high-energy demands during platelet activation. Pyruvate kinases (PKs) catalyzes the final step of glycolysis, the formation of pyruvate and ATP from phosphoenolpyruvate and ADP. Four PK isoforms exist in mammals: L and R isoforms are expressed in the liver and red blood cells; the M1 isoform is expressed in most adult tissues that have high catabolic demands including muscle and brain; M2 is expressed in cells including activated platelets and leukocytes. While PKM1 and tetrameric PKM2 favor ATP production from OXPHOS through the TCA cycle, dimeric PKM2 drives aerobic glycolysis. Objective: We tested an innovative concept that by manipulating the energy demand of activated platelets (metabolic plasticity), by targeting PKM2, will inhibit platelet function and thrombosis. Methods: Using a specific inhibitor of PKM2 (inhibits PKM2 dimerization and stabilizes tetramers) and standardized platelet in vitro assays, we determined the mechanistic role of PKM2 in modulating platelet function in human and mice. To provide definitive evidence, we generated a megakaryocyte or platelet-specific PKM2-/- mouse (PKM2fl/flPF4Cre). Lactate assay was performed in WT and PKM2 null platelets. Susceptibility to thrombosis was evaluated in vitro (microfluidics flow chamber) and in vivo (FeCl3-induced carotid artery thrombosis and laser injury models) by utilizing intravital microscopy. Results: We found that PKM2 is relatively highly expressed compared to PKM1 in human and murine platelets. Transmission electron microscopy (immunogold staining) revealed that PKM2 is found in the cytoplasm and a- granule in resting platelets, whereas most of PKM2 translocated to cytoplasm upon activation. Human and mouse platelets pretreated with PKM2 inhibitor exhibited decreased platelet aggregation to sub-optimal doses of collagen and convulxin but not to thrombin. In microfluidics flow chamber assay, human and whole mouse blood pretreated with PKM2 inhibitor formed small thrombi when perfused over collagen for 5 min at an arterial shear rate of 1500s-1 (P<0.05 vs. vehicle control). Platelets from PKM2fl/flPF4Cre mice exhibited decreased platelet aggregation to sub-optimal doses of collagen and convulxin, but not to thrombin, compared to PKM2fl/fl mice concomitant with decrease lactate production. In microfluidics flow chamber assay, whole blood from PKM2fl/flPF4Cre mice formed smaller thrombi when perfused over collagen for 5 min at an arterial shear rate of 1500s-1, compared to PKM2fl/fl mice. PKM2fl/flPF4Cre mice were less susceptible to thrombosis in the FeCl3-induced carotid and laser injury-induced mesenteric artery thrombosis models (P<0.05 vs. vehicle control, N=10 mice/group), without altering hemostasis. PKM2 regulates the phosphorylation signal transducer and activator of transcription 3 (STAT3) and p-STAT3 act as a protein scaffold that facilitates the catalytic process of activating PLCg by kinase Syk in response to low-doses of collagen and CRP, but not TRAP or ADP in human and murine platelets. Interestingly, we found that PKM2 and STAT3 colocalized in the convulixn- stimulated control platelets and less phosphorylation of STAT-3 was observed in activated PKM2 null platelets (P<0.05 vs. WT), suggesting a non-glycolytic role of the PKM2 in regulating collagen signaling. Conclusions: Our results suggest that dimeric PKM2 regulates platelet function and arterial thrombosis most likely via GPVI signaling pathway. We suggest that manipulating metabolic plasticity by targeting dimeric PKM2 may be explored as a novel strategy to inhibit platelet function and arterial thrombosis. Disclosures No relevant conflicts of interest to declare.
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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 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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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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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 (June 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 glycolysis by converting phosphoenolpyruvate (PEP) to pyruvate and ATP. On the other hand, dimeric PKM2 translocates to the nucleus and mediates gene regulation via its non-canonical protein kinase activity. Dimeric PKM2 regulates hypoxia, IL-1β expression and, phosphorylates signal transducer and activator of transcription 3 (STAT3) which functions downstream of the IL-6 signaling pathway.2Objectives:To investigate the role of PKM2 in GCA diagnosis and pathogenesis.Methods:Immunohistochemical staining for PKM2 was performed on inflamed (n=8) and non-inflamed (n=4) temporal artery biopsies (TAB) from GCA patients and on TAB from non-GCA (n=9) patients. To detect soluble, dimeric PKM2 in plasma commercially available dimeric PKM2 specific ELISA kit was used. To determine the modulation of dimeric PKM2 by treatment, samples of GCA patients at baseline (n=44), at 6 weeks (n=32) and at 1 year (n=31) after treatment were compared to samples from age- and sex-matched healthy controls (HC, n=45) As a positive control, samples from melanoma patients (n =8) were used. To investigate the role of dimeric PKM2 in the pathogenesis of GCA, we correlated PKM2 plasma levels with markers of inflammation (CRP, IL-6) and markers of angiogenesis (Angpt2, VEGF, YKL40). Statistical analysis included the Mann-Whitney U test for comparing different groups while the Wilcoxon rank test was used for paired samples. Correlations were assessed by Spearman’s rank correlation coefficient.Results:High expression of PKM2 was found in inflamed and non-inflamed TABs of GCA patients, while in non-GCA TABs PKM2 was sparsely expressed. Circulating levels of dimeric PKM2 were found elevated in melanoma and in GCA patients at baseline/active disease compared to those in healthy controls. Analysis of 6 weeks and 1 year follow up plasma samples showed that plasma levels of dimeric PKM2 significantly decreased upon treatment. Dimeric PKM2 weakly correlated with CRP at baseline (r=0.399, p=0.048) but not with angiogenesis markers.Conclusion:Dimeric PKM2 plasma levels were found elevated in GCA patients at baseline. PKM2 plasma levels were down modulated by treatment. PKM2 plasma levels weakly correlated with inflammation marker CRP. The data suggest that PKM2 as a marker of glycolysis may have relevance in GCA at diagnosis and for monitoring disease activity. Future studies should aim to validate PKM2 in an independent cohort. Additional studies are needed to determine the molecular mechanism underlying the increase in elevated dimeric PKM2 levels and how this may contribute to IL-6 signaling.References:[1]Samson M, Corbera-Bellalta M, Audia S, Planas-Rigol E, Martin L, Cid MC, Bonnotte B. Recent advances in our understanding of giant cell arteritis pathogenesis. Autoimmunity reviews. 2017;16(8):833-44.[2]Alquraishi M, Puckett DL, Alani DS, Humidat AS, Frankel VD, Donohoe DR, Whelan J, Bettaieb A. Pyruvate kinase M2: A simple molecule with complex functions. Free Radical Biology and Medicine.2019;143:176-192.Acknowledgments:This project received funding from the EU Horizon 2020 research and innovation program under the Marie Sklodowska-Curie grant agreement 754425.Disclosure of Interests:Idil Esen: None declared, Yannick van Sleen: None declared, Peter Heeringa: None declared, Annemieke Boots Consultant of: Grünenthal Gmbh until 2017, Elisabeth Brouwer Consultant of: Roche (consultancy fee 2017 and 2018 paid to the UMCG), Speakers bureau: Roche (2017 and 2018 paid to the UMCG)
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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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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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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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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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Dissertations / Theses on the topic "Pyruvate kinase M2 (PKM2)"

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Gao, Xueliang. "Nuclear Pyruvate Kinase M2 Functional Study in Cancer Cells." Digital Archive @ GSU, 2010. http://digitalarchive.gsu.edu/biology_diss/89.

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Cancer cells take more glucose to provide energy and phosphoryl intermediates for cancer progression. Meanwhile, energy-provider function of mitochondria in cancer cells is disrupted. This phenomenon is so-called Warburg effect, which is discovered over eighty years ago. The detail mechanisms for Warburg effect are not well defined. How glycolytic enzymes contribute to cancer progression is not well known. PKM2 is a glycolytic enzyme dominantly localized in the cytosol, catalyzing the production of ATP from PEP. In this study, we discovered that there were more nuclear PKM2 expressed in highly proliferative cancer cells. The nuclear PKM2 levels are correlated with cell proliferation rates. According to our microarry analyses, MEK5 gene was upregulated in PKM2 overexpression cells. Our studies showed that PKM2 regulated MEK5 gene transcription to promote cell proliferation. Moreover, nuclear PKM2 phosphorylated Stat3 at Y705 site using PEP as a phosphoryl group donor to regulate MEK5 gene transcription. Our study also showed that double phosphorylated p68 RNA helicase at Y593/595 interacted with PKM2 at its FBP binding site. Under the stimulation of growth factors, p68 interacted with PKM2 to promote the conversion from tetrameraic to dimeric form so as to regulate its protein kinase activity. Overexpression PKM2 in less aggressive cancer cells induced the formation of multinuclei by regulating Cdc14A gene transcription. Overall, this study presents a step forward in understanding the Warburg effect.
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Bahr, Brigham L. "Different Expression of Placental Pyruvate Kinase M2 in Normal, Preeclamptic, and Intrauterine Growth Restriction Pregnancies." BYU ScholarsArchive, 2014. https://scholarsarchive.byu.edu/etd/3901.

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This thesis will be organized into two chapters discussing the placental expression of two proteins, pyruvate kinase M2 (PKM2) and heat shock protein 27 (HSP 27), in human placentas. Understanding the mechanisms of placental metabolism in healthy and diseased placentas helps us understand how placenta disorders occur and how we can treat these disorders. The goal is to investigate these proteins to gain an understanding of their roles in placental disorders and help decrease maternal and fetal mortality rates. Chapter one covers the background of pyruvate kinase M2 (PKM2) in cancer and embryonic tissues, and the expression of PKM2 in the human placenta. Cancer PKM2 has been studied extensively, but little is know about the role of placental PKM2. Expression of PKM2 is confirmed in normal human placenta samples and described in preeclamptic and intrauterine growth restriction (IUGR) affected human placentas. Proteins associated with elevated PKM2 in cancer are also associated with elevated PKM2 in human placentas. Comparing normal and diseased placenta samples helps understand the similarities between cancer PKM2 and placental PKM2. Understanding the mechanisms of placental metabolism and PKM2 expression in the human placenta will clarify how the placenta is affected by preeclampsia and IUGR and the role placental PKM2 plays in each of these diseases. Chapter two will cover a paper that I wrote on the expression of phosphorylated heat shock protein 27 (HSP27) in the human placenta. Heat shock proteins are involved in the stress response and help inhibit apoptosis. The object of the study was to look for correlations between p-HSP27 and apoptosis in human and ovine placenta samples. P-HSP27 was quantified in human placenta samples and in placenta sampled collected from ovine models. Pregnant control and hyperthermic sheep models were used to quantify expression of p-HSP27 across gestation. This study showed similarities between human IUGR and our ovine IUGR model, suggesting a link between decreased p-HSP27 and increased apoptosis in IUGR.
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Kimball, Rebecca Lutz. "The Role of Hypoxia on Pyruvate Kinase M2, mammalian Target of Rapamycin, Mitochondrial Function, and Cell Invasion in the Trophoblast." BYU ScholarsArchive, 2016. https://scholarsarchive.byu.edu/etd/5723.

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This thesis will be organized into two chapters discussing the role of hypoxia in the human placenta. The goal of this thesis is to characterize pyruvate kinase M2, mammalian target of rapamycin, mitochondrial function, and cell invasion in hypoxic conditions in the trophoblast. Understanding the mechanisms of placental metabolism can lead to further treatments for placental diseases. Chapter one covers the background of intrauterine growth restriction, hypoxia, placental metabolism, and pyruvate kinase M2 (PKM2). Little is currently understood about the role of the mitochondria in placental diseases. Expression of PKM2, trophoblast cell invasion, and mitochondrial function is shown to be inhibited by hypoxia. PKM2 inhibition decreases trophoblast cell invasion and nuclear expression of PKM2, but increases mitochondrial function. Studying how hypoxia affects the placenta during placental diseases can help clarify the mechanisms by which these diseases occur. Chapter two further characterizes the background of intrauterine growth restriction and hypoxia. It also covers the background of mammalian target of rapamycin. The objective of this chapter was to assess activated mTOR in the trophoblast in hypoxia. Decreased placental and fetal weights, as well as trophoblast cell invasion were observed in hypoxia. A decrease in the activation of mTOR was also found in the hypoxic placenta. This study could provide insight into the physiological relevance of the pathways and could be targeted to help alleviate placental diseases.
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Mitchell, Rosie. "The regulation of human M2 pyruvate kinase." Thesis, University of Edinburgh, 2015. http://hdl.handle.net/1842/21690.

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Pyruvate kinase catalyses the final step in glycolysis and is responsible for net ATP production. There are four pyruvate kinase isoforms expressed in humans; LPYK, RPYK, M1PYK and M2PYK. The allosteric enzyme M2PYK plays an important role in cancer cell metabolism and is subject to complex regulation by numerous naturally occurring small-molecule metabolites. Post-translational modifications have also been found to play a key role in the regulation of M2PYK, among these cysteine oxidation. This thesis describes the production and characterisation of M2PYK cysteine point mutants in order to investigate the mechanism of regulation by cysteine modification. From a total of ten cysteines present in M2PYK, five were chosen for mutation based on a combination of the results from the cysteine oxidation prediction program (COPP) web interface and published experimental evidence for cysteine modification of M2PYK. Eight point mutants of these five cysteines were produced and characterised. Low resolution gel filtration of all the mutants shows that mutation of these cysteines has an effect on tetramer:dimer:monomer equilibrium of M2PYK suggesting that cysteine modifications could regulate M2PYK activity by affecting oligomeric state. Activity assays show that none of the cysteine point mutations are sufficient to protect M2PYK from oxidation by H2O2 indicating that more than one cysteine is involved in the regulation of M2PYK by oxidation. Nitric oxide (NO) imbalance has recently emerged as playing a key role in numerous diseases including cancer. NO regulates the function of target proteins through the addition of a nitroso moiety from NO-derived metabolites to a reactive cysteine, a process known as protein S-nitrosylation. M2PYK has been found to be S-nitrosylated in vivo. Using the biotin-switch assay in vitro combined with mass spectrometry I have shown that a likely candidate for the target of S-nitrosylation of M2PYK is C326. This thesis also describes the structures of two cysteine point mutants; M2PYK C424A and M2PYK C358S. The structures show that these mutations have very little effect on the overall conformation of M2PYK with only very subtle localised changes. The structure of the mutant M2PYK C358S shows some interesting features including varying occupation of the active site resulting in differing conformations of the B domains within the same tetramer, and an unusual B factor distribution which could be indicative of a perturbation in cooperativity within the tetramer caused by the mutation.
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Hasan, Diya [Verfasser]. "Hypoxic regulation and selective silencing of pyruvate kinase isoforms PKM1 and PKM2 by siRNA / Diya Hasan." Gießen : Universitätsbibliothek, 2012. http://d-nb.info/1064024580/34.

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Dayton, Talya Lucia. "Examining the roles of the pyruvate kinase isoforms, PKMI1 and PKM2, in systemic metabolism and tumor development." Thesis, Massachusetts Institute of Technology, 2016. http://hdl.handle.net/1721.1/104176.

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Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2016.
Cataloged from PDF version of thesis. Vita.
Includes bibliographical references.
Alternative splicing of the Pkm gene product generates the PKM1 and PKM2 isoforms of pyruvate kinase, and PKM2 expression is closely linked to embryogenesis, tissue regeneration, and cancer. PKM1 expression, on the other hand, is restricted mostly to skeletal muscle, heart, and brain. To interrogate the functional requirement for PKM1 or PKM2 during development and tissue homeostasis, we generated germline PKM1 (Pkm1-/-) or PKM2 null mice (Pkm2-/-). Unexpectedly, despite being the primary isoform expressed in most wild-type adult tissues, we found that Pkm2' mice are viable and fertile. Thus, PKM2 is not required for embryonic or postnatal development. Loss of PKM2 leads to compensatory expression of PKM1 in the tissues that normally express PKM2. We found that Pkm1-/- mice are also viable and fertile. Thus, neither PKM isoform is required for embryonic or postnatal development. In Pkm1-/- mice, loss of PKM1 leads to compensatory expression of PKM2 in the tissues that normally express PKM1. Aside from distinct changes in the plasma metabolite profiles of Pkm1-/- mice compared to wild-type (WT) mice, germline loss of PKMI appears to be of little phenotypic consequence. In contrast, PKM2 loss leads to a striking phenotype: spontaneous development of hepatocellular carcinoma (HCC) with high penetrance that is accompanied by progressive changes in systemic metabolism characterized by altered systemic glucose homeostasis, inflammation, and hepatic steatosis. Therefore, in addition to its role in cancer metabolism, PKM2 plays a role in controlling systemic metabolic homeostasis and inflammation, thereby preventing HCC by a non-cell-autonomous mechanism. To interrogate the cell-autonomous functional requirement for PKM2 during tumor initiation, we used a conditional Pkm2 allele (Pkm2f/) to abolish PKM2 expression in the context of two Kras driven mouse models - for lung adenocarcinoma and soft-tissue sarcoma (STS). In the sarcoma model, where the presumed tumor cell-of-origin expresses PKM1, deletion of PKM2 led to delayed tumor formation. In contrast, in the lung cancer model the presumed tumor cell-of-origin expresses PKM2 and deletion of PKM2 had no effect on tumor latency or tumor area. PKM2-null sarcomas expressed PKM1 and contained a high number of infiltrating PKM2+ stromal cells. Metabolite analysis of sarcoma cell lines generated from PKM2-null and wild-type tumors revealed metabolic changes in the PKM2-null tumors. These results argue that the consequences of PKM2 loss during tumor initiation depend on the tumor type and that the requirement for PKM2 expression can be overcome through metabolic adaptation. Taken together, the work presented in this thesis provides key insights into the pleiotropic roles played by PKM1 and PKM2 in the contexts of normal and malignant proliferation and in tumor and systemic metabolism. Our findings contribute to a more complete understanding of the distinct cell-intrinsic and cell-extrinsic roles of PKM isoform expression in the context of cancer, and may potentially inform strategies that target metabolism for the treatment of cancer.
by Talya Lucia Dayton.
Ph. D.
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Kumar, Y. "Clinical review and experimental evaluation of tumour M2-pyruvate kinase in pancreatic cancer." Thesis, University College London (University of London), 2009. http://discovery.ucl.ac.uk/17418/.

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The treatment of pancreatic cancer is challenging. Patients are often beyond curative surgical therapy and palliative treatment with chemotherapy provides limited benefit. New markers of cancer activity and therapeutic targets are required. This thesis has firstly reviewed the available literature on Tumour M2-PK, a dimeric form of M2 isoenzyme of pyruvate kinase, in GI cancer and carried out a meta-analysis of the clinical data on pancreatic cancer. Experimental work evaluated the measurement of M2-pyruvate kinase in human pancreatic cancer cell lines with altered microenvironment (hypoxia, acidic pH or glucose-deprived condition). Tumour M2-PK level was measured using ELISA, total M2-PK by immunoblotting and pyruvate kinase activity by spectrophotometric analysis. Apoptosis or necrosis was detected by measuring active Caspase 3/7 and 8, Bcl-2, Bax and Annexin V staining. Localisation of M2-PK in pancreatic cancer cell was studied by immunocytochemistry. The clinical review has shown that Tumour M2-PK is not an organ-specific marker of GI cancer but is elevated with positive predictive value of 86–88% in gastro-oesophageal and colorectal cancers. In pancreatic cancer the diagnostic odds ratio (DOR) of an elevated Tumour M2-PK was similar to those of CA19-9 with overall sensitivity of 94% and specificity of 55%. Higher levels of Tumour derived M2-pyruvate kinase were observed in Colo 357 cell lines compared to Panc-1 cells. Exposure of Colo 357 cells to altered culture conditions resulted in decreased cell proliferation accompanied by elevated Tumour M2-PK levels with unchanged total M2-PK levels suggesting tetramerdimer switch-over, which was confirmed by the corresponding change in the pyruvate kinase activity. No correlation of Tumour M2-PK level or PK activity with apoptotic or anti-apoptotic markers was observed. Immunocytochemistry suggested M2-PK localisation to intracellular membrane-bound structures with no translocation to nucleus or mitochondria under altered tumour microenvironment. Conclusion: Tumour M2-PK is a potential marker of pancreatic cancer. Altering the tumour microenvironment causes a switch to measured M2-PK levels. This may allow cells to overcome cell apoptosis and could be a pathway facilitating tumour survival.
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Zaccaro, Cristina <1987&gt. "Evaluation of Tumor M2 Pyruvate Kinase and Endocannabinoid System Expression in Colorectal Preneoplastic and Neoplastic Lesions: Possible Use for non Invasive Diagnosis." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2016. http://amsdottorato.unibo.it/7357/.

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Colorectal cancer (CRC) is a multistep process that goes through adenoma-carcinoma sequence. Many forms of CRC may be prevented by routine control, which can detect precancerous neoplasm before they undergo malignant transformation (123). For this reasons we hypothesized that a combination of simple faecal tests, may help to identify patients with higher risk of adenomas and/or CRC. The aim of this study is to clarify whether FOBT, enzyme Tumor M2-PK and endocannabinoid system molecules (CB1, CB2, FAAH), could represent diagnostic non-invasive markers, alone or in combination, for early diagnosis of CRC and its precancerous lesions. In a pivotal study we analyzed a selected population, using i-FOBT and quantitative ELISA stool test for t-M2-PK detection. i-FOBT showed the highest specificity and PPV (88.8% and 52.7% respectively); M2-PK had the best sensitivity (87.2%); the best results it obtained with combination tests; in fact if our patients had been subjected only to the i-FOBT test, 33 high risk adenoma and 14 CRC would not have been diagnosed. Supported by these findings, we analyzed a consecutive population: patients with both positive tests have only 31.6% risk of developing CRC; in contrast, patients negative to both markers, cancer risk was less than 2% (VPN 98.5%). We confirmed, also with immuoistochemistry, that increase of tumour M2-PK in patients with CRC, as well as in stool samples, is correlated with pre neoplastic stages. To investigate the expression of endocannabinoid system in CRC, CB1, CB2 and FAAH markers were studied immunochemically in different stages and normal tissue. CB receptors and their ligands, as well as FAAH inhibitions, showed to have a protective role in colorectal cancer. They, in combination with other markers (such as t-M2-PK and FOBT), could be indicated to develop a non-invasive test for an early diagnosis of cancerous and pre-cancerous colorectal lesions.
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Lavik, Andrew R. "The Role of Inositol 1,4,5-Trisphosphate Receptor-Interacting Proteins in Regulating Inositol 1,4,5-Trisphosphate Receptor-Dependent Calcium Signals and Cell Survival." Case Western Reserve University School of Graduate Studies / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=case1448532307.

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Dharaneeswaran, Harita. "Pyruvate kinase M2 (PKM2), a glycolytic enzyme, is required to maintain vascular barrier function." Thesis, 2017. https://hdl.handle.net/2144/23713.

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RATIONALE - Metabolic enzymes, like pyruvate kinase M2 (PKM2), play an essential role in altering endothelial cell (EC) phenotypes and behavior. Extensive research has elucidated the function of PKM2, a rate-limiting glycolytic enzyme, in the context of cancer cells and in activated immune cells, but its role in EC biology is only newly emerging. Recent findings show PKM2 acts as a key regulator of angiogenesis. Where exogenous circulating PKM2 induces EC cell proliferation leading to increased tumor angiogenesis and growth. Also, PKM2 deficient ECs exhibit decreased proliferation and migration. The relevance of PKM2 in modulating vascular barrier function is yet to be defined. OBJECTIVE -This study attempts to elucidate the role of PKM2 in regulating vascular barrier function. METHODS AND RESULTS - In vivo, EC specific deletion of PKM2 promotes increased vascular permeability in pulmonary capillary vessels and increased VEGF-induced acute vessel permeability in mouse dermal vessels. Similarly, in vitro, PKM2 deficient ECs exhibit decreased electrical resistance, disrupted VE-cadherin junctions and gap formations (illustrated via florescent VE-cadherin staining and phosphorylation of VE- cadherin protein at tyrosine residue Y658). Mechanistically, the deletion of PKM2 in ECs leads to increased angiopoietin-2 (Ang-2) expression, a well-known modulator of vascular permeability. Also, deletion of Ang-2 was sufficient to attenuate vascular leakage in PKM2 deficient endothelium, indicating that vascular leaky phenotype observed in PKM2 deficient endothelium is mediated by increased Ang-2 expression. CONCLUSIONS - PKM2, by modulating Ang-2 expression, plays a vital role in maintaining vascular barrier function.
2019-07-11T00:00:00Z
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Book chapters on the topic "Pyruvate kinase M2 (PKM2)"

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Prakasam, Gopinath, Mohammad Askandar Iqbal, Vibhor Gupta, Bhupender Kumar, and Rameshwar N. K. Bamezai. "Pyruvate Kinase M2." In Encyclopedia of Signaling Molecules, 4323–33. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101893.

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Prakasam, Gopinath, Mohammad Askandar Iqbal, Vibhor Gupta, Bhupender Kumar, and Rameshwar N. K. Bamezai. "Pyruvate Kinase M2." In Encyclopedia of Signaling Molecules, 1–11. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101893-1.

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Gupta, Vibhor, Mohd Askandar Iqbal, Bhupender Kumar, and Rameshwar N. K. Bamezai. "Pyruvate Kinase M2: A Metabolic Tuner." In Tumor Cell Metabolism, 123–42. Vienna: Springer Vienna, 2015. http://dx.doi.org/10.1007/978-3-7091-1824-5_6.

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Eigenbrodt, E., S. Mazurek, and R. R. Friis. "Double role of pyruvate kinase type M2 in the regulation of phosphometabolite pools." In Cell Growth and Oncogenesis, 15–30. Basel: Birkhäuser Basel, 1998. http://dx.doi.org/10.1007/978-3-0348-8950-6_2.

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Mazurek, S. "Pyruvate Kinase Type M2: A Key Regulator Within the Tumour Metabolome and a Tool for Metabolic Profiling of Tumours." In Oncogenes Meet Metabolism, 99–124. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/2789_2008_091.

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Conference papers on the topic "Pyruvate kinase M2 (PKM2)"

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Lim, Jae Yun, Sun Och Yoon, Soon Won Hong, Jong Won Kim, Seung Ho Choi, and Jae Yong Cho. "Abstract 4540: Pyruvate kinase M2 (PKM2) associated with poor prognosis in gastric signet ring cell carcinoma." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4540.

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Mishra, A., A. Jaiswal, N. Stahr, S. Makhija, M. Sandey, and A. Suryawanshi. "Pyruvate Kinase M2 (PKM2) - Mediated Glycolytic Upregulation in Lung CD11c+ Cells Facilitates Alternaria-Induced Acute Airway Inflammation." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a1286.

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Biyik-Sit, Rumeysa, Traci Kruer, Susan M. Dougherty, James Bradley, Michael L. Merchant, John O. Trent, and Brian F. Clem. "Abstract 4933: Nuclear Pyruvate Kinase M2 (PKM2) contributes to PSAT1-mediated cell migration in EGFR-activated lung cancer cells." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-4933.

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Sit, Rumeysa B., Traci Kruer, James Bradley, Michael Merchant, John O. Trent, and Brian F. Clem. "Abstract 3563: Potential role for a phosphoserine aminotransferase 1 and pyruvate kinase M2 (PSAT1:PKM2) functional interaction in lung cancer cells." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3563.

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Sturgill, Eric M., and Monica L. Guzman. "Abstract 4793: The M2 isoform of pyruvate kinase (PKM2) contributes to leukemia stem cell persistence by maintaining oxidative homeostasis and promoting glycolysis." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4793.

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Patel, Chirag B., Corinne Beinat, Yuanyang Xie, Edwin Chang, and Sanjiv S. Gambhir. "Abstract 5271: Molecular imaging of pyruvate kinase M2 (PKM2) with [18F]DASA-23 detects temozolomide- and tumor treating fields (TTFields)-induced changes in glycolysis in glioblastoma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-5271.

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Patel, Chirag B., Corinne Beinat, Yuanyang Xie, Edwin Chang, and Sanjiv S. Gambhir. "Abstract 5271: Molecular imaging of pyruvate kinase M2 (PKM2) with [18F]DASA-23 detects temozolomide- and tumor treating fields (TTFields)-induced changes in glycolysis in glioblastoma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-5271.

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Rai, N., T. Novoyatleva, N. Weissmann, H. A. Ghofrani, R. T. Schermuly, and W. Seeger. "Role of Pyruvate Kinase 2 Muscle (PKM2) Oligomerization in Pulmonary Arterial Hypertension." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5278.

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Xu, Zhi, Angela Liu, Nikki Lee, Jinfei Chen, and John M. Luk. "Abstract 3352: miR-122 targets pyruvate kinase M2 and affects metabolism of hepatocellular carcinoma." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3352.

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Tan, S., EJ Forty, PF Durrenberger, RJ McAnulty, RC Chambers, and PF Mercer. "P50 Localisation of the glycolytic isozyme, pyruvate kinase m2 in the lung of idiopathic pulmonary fibrosis." In British Thoracic Society Winter Meeting 2017, QEII Centre Broad Sanctuary Westminster London SW1P 3EE, 6 to 8 December 2017, Programme and Abstracts. BMJ Publishing Group Ltd and British Thoracic Society, 2017. http://dx.doi.org/10.1136/thoraxjnl-2017-210983.192.

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