Alves-Filho Jose C, Pålsson-McDermott Eva M
Department of Pharmacology, Ribeirao Preto Medical School, University of São Paulo , Ribeirao Preto , Brazil.
Biomedical Science Institute, School of Biochemistry and Immunology, Trinity College Dublin , Dublin , Ireland.
Front Immunol. 2016 Apr 21;7:145. doi: 10.3389/fimmu.2016.00145. eCollection 2016.
Pyruvate kinase (PK) is the enzyme responsible for catalyzing the last step of glycolysis. Of the four PK isoforms expressed in mammalian cells, PKM2 has generated the most interest due to its impact on changes in cellular metabolism observed in cancer as well as in activated immune cells. As our understanding of dysregulated metabolism in cancer develops, and in light of the growing field of immunometabolism, intense efforts are in place to define the mechanism by which PKM2 regulates the metabolic profile of cancer as well as of immune cells. The enzymatic activity of PKM2 is heavily regulated by endogenous allosteric effectors as well as by intracellular signaling pathways, affecting both the enzymatic activity of PKM2 as a PK and the regulation of the recently described non-canonical nuclear functions of PKM2. We here review the current literature on PKM2 and its regulation, and discuss the potential for this protein as a therapeutic target in inflammatory disorders.
丙酮酸激酶（PK）是负责催化糖酵解最后一步的酶。在哺乳动物细胞中表达的四种PK同工型中，PKM2因其对癌症以及活化免疫细胞中观察到的细胞代谢变化的影响而引起了最多关注。随着我们对癌症中代谢失调的理解不断发展，以及鉴于免疫代谢领域的不断扩大，人们正在付出巨大努力来确定PKM2调节癌症以及免疫细胞代谢谱的机制。PKM2的酶活性受到内源性变构效应物以及细胞内信号通路的严格调控，这既影响PKM2作为PK的酶活性，也影响最近描述的PKM2非经典核功能的调节。我们在此回顾了关于PKM2及其调节的当前文献，并讨论了该蛋白作为炎症性疾病治疗靶点的潜力。
