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Lactate Dehydrogenase (LDH)
- Target
- LDH
- Molecular classification
- Enzyme, Oxidoreductase
01
Overview
Lactate dehydrogenase (LDH), also known as lactic acid dehydrogenase, is a key enzyme in cellular metabolism that catalyzes the reversible conversion of lactate to pyruvate. It is a tetramer composed of H and M subunits, forming five isoenzymes with tissue-specific distribution. LDH is present in nearly all tissues, with highest concentrations found in muscles, liver, kidneys, and red blood cells. Elevated LDH levels are measured to assess tissue damage or disease activity, indicating conditions like myocardial infarction, hemolytic anemia, liver diseases, muscle injury, and certain cancers. Isoenzyme testing helps localize the source of tissue damage. It is considered a therapeutic target, and LDH levels are used for prognosis and monitoring treatment response in various malignancies.
- Other names
- Lactic Acid Dehydrogenase
02
Mechanism of action
Inhibition of Lactate Dehydrogenase
03
Biological functions
Anaerobic GlycolysisEnergy ProductionConversion of Lactate to PyruvateCori Cycle
04
Disease associations
Myocardial InfarctionHemolytic AnemiaLiver DiseasesMuscle InjuryMuscle DystrophyCancerLymphomaTesticular Cancer
05
Safety considerations
Non-specific marker for tissue damageElevated levels can be caused by various conditions
06
Biomarkers
Elevated LDH levels in serum or fluidLDH-1 predominance (cardiac involvement)High LDH-5 (liver pathology)
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