LDH

In normal tissues, lactate generation is limited to anaerobic conditions where oxygen levels are low. In contrast, cancer cells preferentially convert glucose into lactate through glycolysis, even under normal oxygen concentrations, a phenomenon termed “aerobic glycolysis” or the Warburg effect. Anti-glycolytic therapeutic approaches against cancer have been (re-)evaluated, in consideration of the dependence that cancer cells have on a high glycolytic rate[1]. In particular, human LDH-A (or LDH-5; EC 1.1.1.27), a key glycolytic enzyme that catalyzes the formation of lactate from pyruvate and is frequently upregulated in clinical tumors, is currently being considered as a strategic target for the blockage of glycolysis. Since humans missing the LDH-A enzyme (as a hereditary disease), are healthy, it has been hypothesized that inhibition of LDH-A as an anticancer strategy should give no significant on-target side effects [2], [3].


[1] RA Ward et al. Design and synthesis of novel lactate dehydrogenase A inhibitors by fragment-based lead generation. J Med Chem. 2012 Apr 12;55(7):3285-306.
[2] C Granchi et al. Discovery of N-hydroxyindole-based inhibitors of human lactate dehydrogenase isoform A (LDH-A) as starvation agents against cancer cells. J Med Chem. 2011 Mar 24;54(6):1599-612.
[3] C Granchi et al. Assessing the differential action on cancer cells of LDH-A inhibitors based on the N-hydroxyindole-2-carboxylate (NHI) and malonic (Mal) scaffolds. Org Biomol Chem. 2013 Oct 14;11(38):6588-96.

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2450 NHI 2 Selective cell membrane permeable inhibitor of human lactate dehydrogenase A €90.00

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