Laktátdehidrogenáz

Laktátdehidrogenáz, often abbreviated as LDH, is an enzyme found in the cytoplasm of cells throughout the body. Its primary function is to catalyze the interconversion of lactate and pyruvate, a crucial step in cellular respiration, particularly during anaerobic conditions. In humans, LDH exists as multiple isoenzymes, which are variants of the enzyme that differ slightly in their amino acid sequence and physical properties. These isoenzymes are tissue-specific, meaning certain isoenzymes are more prevalent in particular organs or tissues. For instance, LDH1 is abundant in the heart and red blood cells, while LDH5 is more concentrated in the liver and skeletal muscle.

Measuring LDH levels in the blood is a common diagnostic tool. Elevated LDH in serum can indicate tissue damage or cell turnover occurring in various parts of the body. Conditions that can lead to increased LDH include myocardial infarction (heart attack), liver disease, muscle injury, hemolysis (destruction of red blood cells), certain cancers, and infections. Conversely, very low LDH levels are generally not clinically significant. Due to its widespread presence, elevated LDH is a non-specific marker, meaning it points to general cellular damage rather than a specific disease. Further investigations are usually required to pinpoint the underlying cause of an elevated LDH.