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Pyruvate kinase M2 and cancer: an updated assessment
Author(s) -
Iqbal Mohd Askandar,
Gupta Vibhor,
Gopinath Prakasam,
Mazurek Sybille,
Bamezai Rameshwar N.K.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.04.011
Subject(s) - pkm2 , pyruvate kinase , glycolysis , carcinogenesis , biology , cancer cell , flux (metallurgy) , cancer , microbiology and biotechnology , cancer research , biochemistry , chemistry , enzyme , genetics , organic chemistry
Cancer cells are characterized by high glycolytic rates to support energy regeneration and anabolic metabolism, along with the expression of pyruvate kinase isoenzyme M2 (PKM2). The latter catalyzes the last step of glycolysis and reprograms the glycolytic flux to feed the special metabolic demands of proliferating cells. Besides, PKM2 has moonlight functions, such as gene transcription, favoring cancer. Accumulating evidence suggests a critical role played by the low‐activity‐dimeric PKM2 in tumor progression, supported by the identification of mutations which result in the down‐regulation of its activity and tumorigenesis in a nude mouse model. This review discusses PKM2 regulation and the benefits it confers to cancer cells. Further, conflicting views on PKM2's role in cancer, its therapeutic relevance and future directions in the field are also discussed.