LDHA

**LDHA (Lactate Dehydrogenase A)**

Lactate dehydrogenase A (LDHA) is a key enzyme involved in the metabolism of carbohydrates, specifically in the conversion of lactate to pyruvate during anaerobic conditions. It belongs to the lactate dehydrogenase (LDH) family, which consists of five isoforms (LDH1-LDH5) encoded by different genes, with LDHA being one of the most abundant in human tissues.

LDHA catalyzes the reversible oxidation of lactate to pyruvate using nicotinamide adenine dinucleotide (NAD+) as an electron acceptor. This reaction is crucial for maintaining cellular energy homeostasis, particularly in tissues with high glycolytic activity such as skeletal muscle, heart, and cancer cells. Under aerobic conditions, pyruvate can enter the mitochondria to proceed through the citric acid cycle, while under anaerobic conditions, lactate is produced and transported to other tissues for reoxidation.

LDHA plays a significant role in cancer metabolism, often referred to as the "Warburg effect," where rapidly dividing cancer cells predominantly rely on glycolysis even in the presence of oxygen. Elevated LDHA activity is associated with tumor progression, metastasis, and resistance to certain therapies. This has led to interest in LDHA inhibitors as potential anticancer drugs, though their clinical efficacy remains under investigation.

In addition to its metabolic functions, LDHA has been implicated in various cellular processes, including apoptosis regulation, oxidative stress responses, and immune modulation. Research continues to explore its broader biological roles and potential therapeutic targets in diseases beyond cancer, such as cardiovascular disorders and neurodegenerative conditions.

LDHA is encoded by the *LDHA* gene, located on chromosome 11 (11q13.3) in humans. Genetic variations in LDHA have been linked to certain metabolic disorders and may influence individual responses to metabolic therapies. Further studies are needed to fully elucidate its physiological and pathological significance.