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Targeting a moonlighting function of aldolase induces apoptosis in cancer cells
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Targeting a moonlighting function of aldolase induces apoptosis in cancer cells
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Journal Article
Targeting a moonlighting function of aldolase induces apoptosis in cancer cells
2019
Overview
Muscle fructose-1,6-bisphosphate aldolase (ALDOA) is among the most abundant glycolytic enzymes in all cancer cells. Here, we show that the enzyme plays a previously unknown and critical role in a cancer cell survival. Simultaneous inhibition of ALDOA activity and interaction with F-actin cytoskeleton using ALDOA slow-binding inhibitor UM0112176 leads to a rapid cofilin-dependent loss of F-actin stress fibers which is associated with elevated ROS production, inhibition of ATP synthesis, increase in calcium levels, caspase activation and arrested cellular proliferation. These effects can be reproduced by silencing of ALDOA. The mechanism of pharmacological action is, however, independent of the catalytic function of the enzyme, specific to cancer cells, and is most deleterious to cells undergoing the epithelial–mesenchymal transition, a process facilitating cancer cell invasion. Our results demonstrate that the overabundance of ALDOA in cancer cells is associated with its moonlighting rather than catalytic functions. This may have significant implications for development of novel broad-based anti-cancer therapies.
Publisher
Nature Publishing Group UK,Springer Nature B.V
Subject
/ 14
/ 14/19
/ 14/63
/ 82
/ 82/51
/ 82/80
/ 96
/ 96/109
/ Actin
/ Adenosine Triphosphate - metabolism
/ Animals
/ Biomedical and Life Sciences
/ Calcium
/ Cancer
/ Caspase
/ Cell Proliferation - drug effects
/ Cofilin
/ Enzyme Inhibitors - pharmacology
/ Enzymes
/ Epithelial-Mesenchymal Transition
/ Female
/ Fructose
/ Fructose-Bisphosphate Aldolase - antagonists & inhibitors
/ Fructose-Bisphosphate Aldolase - genetics
/ Fructose-Bisphosphate Aldolase - metabolism
/ Gene Expression Regulation, Neoplastic
/ Humans
/ Kinases
/ Mice
/ NADPH Oxidases - antagonists & inhibitors
