糖酵解
磷酸甘油酸变位酶
丙酮酸激酶
磷酸甘油酸激酶
生物化学
酶
磷酸烯醇丙酮酸羧激酶
细胞生物学
三磷酸腺苷
磷酸果糖激酶
瓦博格效应
癌细胞
化学
己糖激酶
细胞
磷酸戊糖途径
生物
细胞生长
磷酸果糖激酶1
细胞周期
癌症
遗传学
作者
Matthew G. Vander Heiden,Jason W. Locasale,Kenneth D. Swanson,Hadar Sharfi,Gregory J. Heffron,Daniel Amador-Noguez,Heather R. Christofk,Gerhard Wagner,Joshua D. Rabinowitz,John M. Asara,Lewis C. Cantley
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2010-09-17
卷期号:329 (5998): 1492-1499
被引量:545
标识
DOI:10.1126/science.1188015
摘要
Glucose Metabolism Revisited Cancer cells are revved up to reproduce rapidly and typically consume glucose rapidly by glycolysis. Why then do cancer cells express an isoform of a rate-limiting enzyme in glycolysis, pyruvate kinase M2, which has decreased activity? Vander Heiden et al. (p. 1492 ) propose that consequent accumulation of phosphoenolpyruvate, with the help of an enzymatic activity that remains to be characterized, can lead to phosphate transfer to phosphoglycerate mutase, another glycolytic enzyme, providing the cell with a different way to make pyruvate. This may allow cancer cells to produce pyruvate without generating excess adenosine triphosphate, which can act through feedback to inhibit glycolyis.
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