Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Total creatine kinase measurement in serum has remained the best overall marker for detection and monitoring of skeletal muscle diseases, despite that different human tissues exhibit varying distributions of cytoplasmic and mitochondrial isoenzymes of creatine kinase. Acute myocardial infarction aside, increases in total serum creatine kinase, as reflected by the MM isoenzyme, are most commonly caused by injury or diseases to striated muscle. Enzyme markers of skeletal muscle injury that have been previously used (eg, aldolase, enolase, aspartate aminotransferase, and lactate dehydrogenase isoenzyme 5) are not as specific as creatine kinase and have limited clinical utility. However, new enzyme and protein markers are currently being investigated, eg, troponin and carbonic anhydrase III, which are more specific than creatine kinase toward particular tissues. Moreover, measurement of creatine kinase isoforms may provide information about whether muscle turnover is acute or chronic.
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PMID:Clinical applications of muscle enzymes and proteins. 145 75

The concentration of carbonic anhydrase III isoenzyme (CA-III) in serum samples from 216 clinically normal Thoroughbreds was determined by use of an enzyme immunoassay. The concentration range of CA-III was from 16.0 to 254.5 ng/ml (mean, 56.5 +/- 11.9 ng/ml). Significant differences were not detected according to age or sex. To confirm whether serum CA-III concentration was high in horses with muscle disease, serum samples of 11 horses with exertional rhabdomyolysis were analyzed by enzyme immunoassay. Their serum CA-III concentration was about 56 times (3,136 +/- 2,610 ng/ml) that of healthy Thoroughbreds. Concentration of CA-III was higher in horses with rhabdomyolysis that had been transiently recumbent than in horses with mild disease that were reluctant to move. Blood samples obtained serially from 6 horses with exertional rhabdomyolysis were studied. Serum activities of aldolase, creatine kinase, aspartate transaminase, and lactate dehydrogenase were high. Increases and decreases in concentration of CA-III were more rapid than that for aldolase, creatine kinase, aspartate transaminase, and lactate dehydrogenase activities; thus, CA-III may be clinically applicable as a diagnostic marker for muscle disease in horses.
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PMID:Determination of carbonic anhydrase III isoenzyme concentration in sera of racehorses with exertional rhabdomyolysis. 771 78

Relatively low levels of reactive oxygen species (ROS) produced inside resting skeletal muscles play important functions in cell signaling. When ROS production increases to levels beyond the buffering capacity of muscle antioxidant systems, a state of oxidative stress develops, which leads to skeletal muscle contractile dysfunction. A clear association between oxidative stress and depressed skeletal muscle performance has been described in several acute and chronic conditions, such as systemic inflammation and chronic obstructive lung diseases. The observation that the levels of oxidant-derived posttranslational protein modifications, including protein carbonylation, are elevated inside skeletal muscle fibers when oxidative stress develops suggest that these modifications play important roles in regulating muscle function. This proposal is supported by recent studies that unveiled that several myofilament (myosin heavy chain and actin), mitochondrial (aconitase, creatine kinase), and cytosolic (enolase, aldolase and glyceraldehyde 3-phosphate dehydrogenase and carbonic anhydrase III) proteins are carbonylated inside skeletal muscle fibers in many animal models of muscle dysfunction, and in humans with impaired skeletal muscle contractility. However, the functional importance of carbonylation in determining the function of muscle-specific proteins and the precise contribution of carbonylation-induced dysfunction of these proteins to overall muscle contractile deficit in various pathologies remain to be determined.
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PMID:Protein carbonylation in skeletal muscles: impact on function. 1968 36

Early recognition of muscle injury, up to development of exertional rhabdomyolysis (ER), is essential for many clinical and practical reasons, such as planning the suitable period of recovery and deciding an appropriate time for return to exercise. Albeit magnetic resonance imaging (MRI) remains the reference technique for assessing muscle injuries, and ultrasonography (US) may be a complementary approach for easy, inexpensive and fast screening, the potential drawbacks of both techniques may be overcome by some laboratory tests, which may help guiding both diagnostic reasoning and clinical decision making. Current evidence attest that creatine kinase remains the most validated test across the clinical spectrum of muscles injuries, as its measurement may be helpful for screening subjects with suggestive signs and symptoms, its concentration substantially reflects the amount of injured muscle and its kinetics appears suitable, combined with clinics and results of imaging testing, for making decisions on return to exercise. Relatively low cost and widespread availability are additional advantages of this test. In athletes with ER, myoglobin assessment may provide adjunctive useful information, due to high predictive value for development of acute kidney injury. Regarding other historical biomarkers, namely aldolase and lactate dehydrogenase, the kinetics, correlation with injury severity, laboratory standardization and availability make their measurement unsuitable and redundant. Some innovative biomarkers have also been tested in recent years, including fatty acid-binding proteins and carbonic anhydrase III, myosin light chain 3 and muscle micro RNAs. However, their clinical effectiveness, standardization, availability in clinical laboratories and costs are still regarded as major drawbacks.
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PMID:Diagnostic biomarkers of muscle injury and exertional rhabdomyolysis. 3071 Apr 78