|Values are valid only on day of printing.|
Detection of muscle disease
Aldolase is necessary for glycolysis in muscle as a "rapid response" pathway for production of adenosine triphosphate, independent of tissue oxygen.
Aldolase catalyses the conversion of fructose 1,6-diphosphate into dihydroxyacetone phosphate and glyceraldehyde 3-phosphate, an important reaction in the glycolytic breakdown of glucose to lactate in muscle.
Aldolase is a tetramer whose primary structure depends upon the tissue from which it was synthesized (liver, muscle, brain). The brain form of aldolase has, because of its preponderance in white cells, been suggested to be a leukemia marker, but this is not confirmed.
Elevated values are found in muscle diseases, such as Duchenne muscular dystrophy, dermatomyositis, polymyositis, and limb-girdle dystrophy.
0-16 years: <14.5 U/L
> or =17 years: <7.7 U/L
The highest levels of aldolase are found in progressive (Duchenne) muscular dystrophy. Lesser elevations are found in dermatomyositis, polymyositis, and limb-girdle dystrophy. In dystrophic conditions causing hyperaldolasemia, the increase in aldolase becomes less dramatic as muscle mass decreases.
Reference (normal) values are observed in polio, myasthenia gravis, and multiple sclerosis.
Aldolase increases in myocardial infarction in a time pattern similar to the aspartate aminotransferase.
Increases are also associated with acute viral hepatitis, but levels are normal or slightly elevated in chronic hepatitis, portal cirrhosis, and obstructive jaundice.
Elevations may also be seen with gangrene, prostate tumors, trichinosis, some carcinomas metastatic to the liver, some chronic leukemias, some blood dyscrasias, and delirium tremens.
No significant cautionary statements