Key result
Post-translational cTnT modifications alter myocardial contractility and serve as key cardiovascular disease biomarkers.
Why the study?
Post-translational modifications such as phosphorylation and fragmentation of cTnT alter cardiac contractility and change during CVDs, but their mechanisms and roles in pathophysiology and laboratory diagnosis need discussion.
Post-translational modifications of cardiac troponin T, including phosphorylation and fragmentation, are important for regulating cardiac contractility and serve as key factors in the pathophysiology and laboratory diagnosis of cardiovascular diseases.
PTM of cTnT may refine troponin interpretation in CVD; leaves open whether targeting these modifications improves outcomes.
Cardiac troponin T (cTnT), a protein essential for calcium-regulated, myofibrillar ATPase activity, is extremely sensitive to the action of a significant number of intra- and extracellular enzymes, the action of which causes post-translational modifications (PTMs) of amino acid structure and functioning cTnT. PTMs of cTnT may play important roles in the regulation of cardiac contractility. The vast majority of cTnT modifications involve the phosphorylation by a variety of Ser/Thr kinases, including PKC. At the same time, the activity of cTnT phosphorylation can change under physiological conditions and in some CVDs, including HF, AMI, and arrhythmias. Along with cTnT phosphorylation, cTnT fragmentation occurs, the activity of which can also change. This article discusses the mechanisms of cTnT phosphorylation and fragmentation, discusses the important role of these processes in the pathophysiology and laboratory diagnosis of some CVD, and notes promising directions for further research.
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Aleksey M. Chaulin (2021) conducted a review in Cardiovascular disease. Post-translational modifications of cardiac troponin T, including phosphorylation and fragmentation, alter myocardial contractility and serve as important biomarkers in cardiovascular diseases.
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