L-lactate dehydrogenase
L-lactate dehydrogenase
Overview
L-lactate dehydrogenase (LDH) is a key metabolic enzyme that catalyzes the reversible interconversion of pyruvate and L-lactate with concomitant interconversion of NADH and NAD(^+). This reaction is central to anaerobic glycolysis, redox balance, and cellular energy metabolism. In biomedical literature, LDH is often discussed both as a functional enzyme and as a clinical biomarker, because elevated circulating LDH can reflect tissue injury, hemolysis, inflammation, hypoxia, or high tumor burden.
In recent research, L-lactate dehydrogenase has been studied in several contexts: as a prognostic marker in malignancy and inflammatory disease, as a readout of cell damage or pyroptosis in experimental systems, and as a potential therapeutic target in metabolic inhibition strategies. Its relevance spans cancer immunotherapy, cardiovascular and renal injury, COVID-19-associated complications, and experimental models of diabetes, fibrosis, and oxidative stress.
Focus of Latest Publications
Recent publications have examined L-lactate dehydrogenase (LDH) primarily as a clinical biomarker and, in some settings, as a therapeutic target. In hypertensive disorders of pregnancy, maternal serum LDH was evaluated for its association with adverse pregnancy outcomes and for possible modification by metabolic risk factors. In post-COVID-19 syndrome, LDH was among the soluble blood biomarkers measured alongside markers of endothelial dysfunction and metabolism, and prior SARS-CoV-2 infection was associated with higher LDH levels. In severe COVID-19, LDH was also assessed in relation to inflammation and coagulation, where it showed statistically significant associations with coagulopathy in a critically ill cohort, although the reported correlations were weak and not statistically significant.
Several studies focused on LDH as a marker of tissue injury or treatment response. In a rabbit model of cartilage defects treated with allogeneic mesenchymal stem cells, serum LDH increased significantly in all MSC-treated groups compared with controls, while synovial fluid LDH did not change significantly, suggesting limited value for monitoring cartilage repair. In glioblastoma research, stiripentol was investigated as a putative LDH inhibitor; the compound produced only moderate LDH inhibition but was associated with increased reactive oxygen species, reduced mitochondrial membrane potential, and induction of senescence in tumor cells. Another cancer-focused study linked normal LDH levels with longer overall survival in the DDR-wild-type cohort of the MD Anderson IMPACT2 study, alongside absence of liver metastases and normal albumin.
LDH also appeared in studies of pathogen-specific diagnostics and drug discovery. A cellulose nanobead-based lateral flow immunoassay was developed for highly sensitive detection of Plasmodium vivax LDH, achieving improved sensitivity over conventional gold nanoparticle-based rapid tests and showing no cross-reactivity with P. falciparum LDH or human LDH. In parallel, computational drug design efforts targeted Babesia microti LDH, identifying sanguinarine derivatives with favorable docking scores, predicted pharmacokinetic properties, and stable molecular dynamics behavior. Together, these studies underscore LDH’s continuing relevance as a biomarker in pregnancy, infection, inflammation, and cancer, as well as a target for diagnostic and therapeutic development.