Lactate dehydrogenase (LDH) catalyzes the oxidation of L-lactate to pyruvate. Five different isoforms are known which correspond to different tetrameric combinations of two, genetically distinct sub-units, namely the M and H sub-units. Isoenzyme 1 (LDH1 or H4) and 2 (LDH2 or M3H) predominate in the heart, the kidneys and red blood cells; LDH4 (MH3) and LDH5 (M4) are found in the liver, skeletal muscle and many kinds of neoplastic tissue; LDH3 (M2H2) is most abundant in platelets, lymphoid tissue and certain neoplasms. The amount of LDH in the serum depends on the rate at which it is being released from the tissues. Increased levels of the various isoforms are associated with different conditions: LDH1 with myocardial and renal infarction; LDH2 with renal and pulmonary infarction; LDH3 with acute pulmonary infarction; and LDH5 with muscle tissue necrosis, infectious mononucleosis and liver disease. See Lactate Dehydrogenase (LDH), Serum
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