Lactate Dehydrogenase Test
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Lactate Dehydrogenase Test
Lactate dehydrogenase, also called lactic dehydrogenase, or LDH, is an enzyme found in the cells of many body tissues, including the heart, liver, kidneys, skeletal muscle, brain, red blood cells, and lungs. It is responsible for converting muscle lactic acid into pyruvic acid, an essential step in producing cellular energy.
Lactic dehydrogenase is present in almost all body tissues, so the LDH test is used to detect tissue alterations and as an aid in the diagnosis of heart attack, anemia, and liver disease. Newer injury markers are becoming more useful than LDH for heart attack diagnosis.
Because the LDH enzyme is so widely distributed throughout the body, cellular damage causes an elevation of the total serum LDH. As a result, the diagnostic usefulness of this enzyme by itself is not as valuable as determination of the five fractions that comprise the LDH. These fractions are called isoenzymes and are better indicators of disease than is the total LDH. The fractions are LDH-1, LDH-2, LDH-3, LDH-4, and LDH-5. A normal total LDH level does not mean that individual isoenzyme levels should not be measured. Individual isoenzyme ranges can help differentiate a diagnosis.
When disease or injury affects tissues containing LDH, the cells release LDH into the bloodstream, where it is identified in higher than normal levels. For example, when a person has a heart attack, the LDH level begins to rise about 12 hours after the attack and usually returns to normal within 5-10 days. The LDH is also elevated in diseases of the liver, in certain types of anemia, and in cases of excessive destruction of cells, as in fractures, trauma, muscle damage, and shock.
Cancers can also elevate LDH level. Additionally, some patients have chronically elevated LDH with no identifiable cause and no apparent consequence.
This test requires a blood sample. It is not necessary for the patient to fast (nothing to eat or drink) before the test unless the physician requests it.
Risks for this test are minimal, but may include slight bleeding from the blood-drawing site, fainting or feeling lightheaded after venipuncture, or hematoma (blood accumulating under the puncture site).
Reference ranges for total LDH vary from laboratory to laboratory. Normal values are also higher in childhood. For adults, in most laboratories, the range can be up to approximately 200 units/L, but is usually found within 45-90 U/L.
Enzyme — A protein that regulates the rate of a chemical reaction in the body, increasing the speed at which the change occurs.
Isoenzyme — One of a group of enzymes that catalyze the same reaction but are differentiated by variations in physical properties.
Due to the fact that many common disease processes cause elevations in the total LDH level, a breakdown of the five different isoenzymes that make up the total LDH is often helpful for diagnosis. In certain disorders, the total LDH may be within normal limits, but individual isoenzyme elevations can indicate specific organ or tissue damage. For example, the LDH-2 fraction is normally greater than LDH-1 in the blood. After an acute heart attack, however, the LDH-1 rises over the LDH-2 in what is known as a "flipped LDH."
Certain diagnoses can be assisted by determination of the total LDH. One example is infectious mononucleosis, in which the LDH is usually more elevated than a liver enzyme called AST. Conversely, in cases of viral hepatitis, the liver enzymes AST and ALT are greatly increased over the LDH.
Pagana, Kathleen Deska. Mosby's Manual of Diagnostic and Laboratory Tests. St. Louis: Mosby, Inc., 1998.