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PKM2 and cancer: The function of PKM2 beyond glycolysis
Metabolic reprogramming is a hallmark of cancer cells and is used by cancer cells for growth and survival. Pyruvate kinase muscle isozyme M2 (PKM2) is a limiting glycolytic enzyme that catalyzes the final step in glycolysis, which is key in tumor metabolism and growth. The present review discusses t...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
D.A. Spandidos
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4774429/ https://www.ncbi.nlm.nih.gov/pubmed/26998110 http://dx.doi.org/10.3892/ol.2016.4168 |
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author | DONG, GAOCHAO MAO, QIXING XIA, WENJIE XU, YOUTAO WANG, JIE XU, LIN JIANG, FENG |
author_facet | DONG, GAOCHAO MAO, QIXING XIA, WENJIE XU, YOUTAO WANG, JIE XU, LIN JIANG, FENG |
author_sort | DONG, GAOCHAO |
collection | PubMed |
description | Metabolic reprogramming is a hallmark of cancer cells and is used by cancer cells for growth and survival. Pyruvate kinase muscle isozyme M2 (PKM2) is a limiting glycolytic enzyme that catalyzes the final step in glycolysis, which is key in tumor metabolism and growth. The present review discusses the expression and regulation of PKM2, and reports the dominant role that PKM2 plays in glycolysis to achieve the nutrient demands of cancer cell proliferation. In addition, the present study discusses the non-metabolic function of PKM2, and its role as a coactivator and protein kinase, which contributes to tumorigenesis. Furthermore, conflicting studies concerning the role of PKM2 as a therapeutic target are reviewed. The improved understanding of PKM2 may provide a noval approach for cancer treatment. |
format | Online Article Text |
id | pubmed-4774429 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | D.A. Spandidos |
record_format | MEDLINE/PubMed |
spelling | pubmed-47744292016-03-18 PKM2 and cancer: The function of PKM2 beyond glycolysis DONG, GAOCHAO MAO, QIXING XIA, WENJIE XU, YOUTAO WANG, JIE XU, LIN JIANG, FENG Oncol Lett Review Metabolic reprogramming is a hallmark of cancer cells and is used by cancer cells for growth and survival. Pyruvate kinase muscle isozyme M2 (PKM2) is a limiting glycolytic enzyme that catalyzes the final step in glycolysis, which is key in tumor metabolism and growth. The present review discusses the expression and regulation of PKM2, and reports the dominant role that PKM2 plays in glycolysis to achieve the nutrient demands of cancer cell proliferation. In addition, the present study discusses the non-metabolic function of PKM2, and its role as a coactivator and protein kinase, which contributes to tumorigenesis. Furthermore, conflicting studies concerning the role of PKM2 as a therapeutic target are reviewed. The improved understanding of PKM2 may provide a noval approach for cancer treatment. D.A. Spandidos 2016-03 2016-01-29 /pmc/articles/PMC4774429/ /pubmed/26998110 http://dx.doi.org/10.3892/ol.2016.4168 Text en Copyright: © Dong et al. This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made. |
spellingShingle | Review DONG, GAOCHAO MAO, QIXING XIA, WENJIE XU, YOUTAO WANG, JIE XU, LIN JIANG, FENG PKM2 and cancer: The function of PKM2 beyond glycolysis |
title | PKM2 and cancer: The function of PKM2 beyond glycolysis |
title_full | PKM2 and cancer: The function of PKM2 beyond glycolysis |
title_fullStr | PKM2 and cancer: The function of PKM2 beyond glycolysis |
title_full_unstemmed | PKM2 and cancer: The function of PKM2 beyond glycolysis |
title_short | PKM2 and cancer: The function of PKM2 beyond glycolysis |
title_sort | pkm2 and cancer: the function of pkm2 beyond glycolysis |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4774429/ https://www.ncbi.nlm.nih.gov/pubmed/26998110 http://dx.doi.org/10.3892/ol.2016.4168 |
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