Relevant bibliographies by topics / Pyruvate kinase M2

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Pyruvate kinase M2'

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

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Journal articles on the topic "Pyruvate kinase M2"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Pyruvate kinase M2"

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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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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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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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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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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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Li, Liangwei. "Extracellular Pyruvate Kinase M2 regulates tumor angiogenesis." 2014. http://scholarworks.gsu.edu/biology_diss/141.

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Pyruvate kinase M2 (PKM2) has been studied for decades on its role in cancer metabolism. Recently, PKM2 is highlighted again for its new function: promoting gene transcription by acting as a protein kinase. Moreover, the PKM2 levels in patient circulation have been used as a diagnostic marker for many types of cancers. However, it remains unclear whether PKM2 in blood circulation has any physiological or pathological function. In my dissertation, I demonstrate that PKM2 released from cancer cells facilitates tumor growth by promoting tumor angiogenesis. Our experiments show that PKM2 promotes endothelial cell proliferation, migration and survival. Only the dimeric PKM2, not the tetrameric PKM2 possesses the activity in angiogenesis promotion. Our results further indicate that PKM2 regulates angiogenesis by integrin αvβ3 activation and integrin redistribution. I also found that PKM2 enhances drug resistance of cancer cells expressing integrin αvβ3.
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Chung, Yi, and 鍾怡. "The role of Pyruvate Kinase M2 in Chronic myelogenous Leukemia progression." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/52516784838481385354.

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碩士
國立陽明大學
醫學生物技術暨檢驗學系
104
Chronic myelogenous leukemia (CML) is a type of cancer that begins in certain bone marrow blood-forming cells. It is a form of leukemia characterized by the increased and unregulated growth of predominantly myeloid cells in the bone marrow and the accumulation of these cells in the blood. We used the gene set enrichment analysis (GSEA) study and found an important glycolytic enzyme, Pyruvate kinase M2 (PKM2) that regulates the gene pattern and is correlated with the leukemia stem cell (LSC) population (Lin- CD34 -/+) in CML microarray result. PKM2 is a glycolytic enzyme for metabolism and the nuclear function for cancer progression. We therefore focus on studying the role of PKM2 in CML progression. We generated a PKM2 knockdown cell-line and found that the loss of PKM2 decreases CML cell clonogenic potential and promotes erythrocytic differentiation in K562 cells. Next we determined the critical signal for PKM2 nuclear localization in CML. Using inhibitor and cytokine screening results we found that BCR-ABL and STAT5 are important activation signals to induce PKM2 nuclear localization. We then used the GSEA study and found that serine proteinase inhibitor Kazal-type 2 (SPINK2) is one of the core enrichment genes in LSC signature and PKM2 regulated gene sets. SPINK2 knockdown in CML cells also decreases colongenic potential. We finally performed the chromatin immunoprecipitation (ChIP) assay and found that PKM2 and STATs occupied the SPINK2 promoter. Collectively, these results demonstrate that the CML dominant signal BCR-ABL-STAT5 plays a role in PKM2 nuclear localization. We also found that nuclear PKM2 and STATs may collaboratively drive gene expression including SPINK2 for CML progression.
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Zhang, Yinwei. "Functions of Extracellular Pyruvate Kinase M2 in Tissue Repair and Regeneration." 2016. http://scholarworks.gsu.edu/biology_diss/166.

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Pyruvate kinase M2 (PKM2) is a glycolytic enzyme expressed in highly proliferating cells. Studies of PKM2 have been focused on its function of promoting cell proliferation in cancer cells. Our laboratory previously discovered that extracellular PKM2 released from cancer cells promoted angiogenesis by activating endothelial cell proliferation and migration. PKM2 activated endothelial cells through integrin αvβ3. Angiogenesis and myofibroblast differentiation are key processes during wound healing. In this dissertation, I demonstrate that extracellular PKM2 released from activated neutrophils promotes angiogenesis and myofibroblast differentiation during wound healing. PKM2 activates dermal fibroblasts through integrin αvβ3 and PI3K signaling pathway. I also claim that extracellular PKM2 plays a role during liver fibrosis. PKM2 protects hepatic stellate cells from apoptosis by activating the survival signaling pathway.
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Book chapters on the topic "Pyruvate kinase M2"

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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"

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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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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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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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Hasan, Diya Y., Florentine Kamlah, Werner Seeger, Frank Rose, and Jörg Hänze. "Hypoxic Regulation Of Pyruvate Kinase Isoforms M1 And M2 And Their Inhibition By SiRNA In A549 Cells." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2061.

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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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Kimura, Tetsuo, Priya Bhardwaj, Domenick J. Falcone, Andrew J. Dannenberg, and Kotha Subbaramaiah. "Abstract B36: Pyruvate kinase M2 regulates adipocyte differentiation and the expression of enzymes involved in glucose metabolism." In Abstracts: Thirteenth Annual AACR International Conference on Frontiers in Cancer Prevention Research; September 27 - October 1, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1940-6215.prev-14-b36.

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Moll, K., S. Weidemann, S. Huber, G. Tiegs, and AK Horst. "Pyruvate kinase M2-deficiency in T cells leads to exacerbation of ConA hepatitis and alterations of T cell polarization." In 36. Jahrestagung der Deutschen Arbeitsgemeinschaft zum Studium der Leber. Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0039-3402269.

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Konno, Masamitsu, Atsushi Hamabe, Yuichiro Doki, Masaki Mori, and Hideshi Ishii. "Abstract 1044: Pyruvate kinase M2 stimulates the epithelial-mesenchymal transition by genetically controlling E-cadherin expression in colon cancer." 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.am2014-1044.

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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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Yashiro, Masakazu, and Kishu Kitayama. "Abstract 5484: Pyruvate kinase isozymes M2 and glutaminase might be promising molecular targets for the treatment of gastric cancer." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-5484.

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You might also be interested in the extended bibliographies on the topic 'Pyruvate kinase M2' for particular source types:
Journal articles
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