Cardiac troponin I and troponin T: Are enzymes still relevant as cardiac markers?

Abstract

Creatine kinase (CK) MB and lactate dehydrogenase (LDH) isoenzyme 1 are not heart-specific. By contrast, the regulatory proteins troponin I and troponin T are expressed in three different isoforms, one for slow-twitch skeletal muscle fibers, one for fast-twitch skeletal muscle fibers, and one for cardiac muscle (cTnI, cTnT). cTnI and cTnT are usually not detectable in patients without myocardial damage, which is a prerequisite for high diagnostic performance. After acute myocardial infarction (AMI) cTnI, cTnT, and CKMB mass have a comparable early sensitivity. cTnI and cTnT usually peak in parallel except for patients without reperfusion in whom cTnI peaks about 1 day and cTnT approximately 3–4 days after onset of AMI. Both stay increased for at least 4–5 days. cTnT tends to stay increased longer than cTnI. Because the sensitivities of cTnI and cTnT for myocardial injury are comparable, their specificities are the main topic of current debate. Recent reports on mismatches of cTnI and cTnT in patients with renal failure and myopathy without other evidence for myocardial injury suggest that cTnT could be reexpressed similar to CKMB and LDH-1 in chronically damaged human skeletal muscle. In contrast to cTnT, CKMB, and LDH-1, cTnI is not expressed in skeletal muscle during fetal development. So far, an increase in cTnI has been reported only after myocardial damage. Because of currently higher costs, troponin measurement should be restricted at present to clinical settings that really require their high specificity. Based on its distinct functional association with the metabolism of acute ischemic myocardium and according to initial clinical results, glycogen phosphorylase isoenzyme BB is a promising enzyme for the early detection of ischemic myocardial damage.