Lactate dehydrogenase 5 (LDH-5) (LDH-5)

Lactate dehydrogenase 5 (LDH-5) is a tetrameric isoenzyme composed of four A subunits (LDHA) that plays a critical role in cellular metabolism by catalyzing the reversible conversion of pyruvate to lactate [StatPearls]. Under anaerobic conditions or in rapidly proliferating cells, LDH-5 facilitates the regeneration of NAD+ from NADH, which is essential for maintaining a high rate of glycolysis [UniProt]. In the context of oncology, LDH-5 is frequently upregulated as part of the Warburg effect, allowing cancer cells to thrive in hypoxic environments and produce large amounts of lactate that promote tumor invasion and immune suppression [PubMed]. Because of its central role in metabolic reprogramming, LDH-5 has emerged as a major therapeutic target; inhibiting its activity can starve cancer cells of energy and disrupt their survival mechanisms [NCBI]. Beyond its role as a target, LDH-5 serves as a valuable clinical biomarker, with elevated levels often correlating with poor prognosis and high tumor burden in various malignancies [PubMed].

Other names

Lactate dehydrogenase A4 [UniProt]LDH-M [StatPearls]Muscle-type lactate dehydrogenase [UniProt]LDHA [UniProt]A4 isoenzyme of LDH [PubMed]

Inhibition of the LDH-5 enzyme prevents the conversion of pyruvate to lactate and reduces the regeneration of NAD+, thereby stalling glycolysis and ATP production in cancer cells [PubMed].