Targeting multifunctional human ALDOA in cancer signaling




Stancu, Bogdan Gabriel

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Human fructose-bisphosphate aldolase A (ALDOA) is a key enzyme in glycolysis that catalyzes the conversion of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. ALDOA has also been shown to play key moonlighting roles associated with cellular structure, motility and proliferation. This aldolase isoenzyme is significantly overexpressed in a number of human tumors and has been shown to have oncogenic potential. We have demonstrated that ALDOA overexpression has further inference through cycling of hypoxia inducible transcription factor-1 (HIF-1) regulation. This feed-forward loop mediated through AMPK is a new target to consider in the irregular hypoxic environment of solid tumors. The body of work that follows presents five different methods of targeting and inhibiting ALDOA function. Using small molecule probes, the function and regulation of these iterations is characterized, towards better understanding of the role of ALDOA in cells and in cancer



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