Posttranslational modifications of cardiac troponin T: An overview

Alexander S. Streng, Douwe de Boer, Jolanda van der Velden, Marja P. van Dieijen-Visser, Will K. W. H. Wodzig*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review


Cardiac troponin (cTn) is an important sarcomeric protein complex situated on the thin filament and is involved in the regulation of cardiac muscle contraction. This regulation is primarily controlled by Ca2+ binding to troponin C and in addition fine-tuned by the posttranslational modification of cTnI and cTnT. The vast majority of cTnT modifications involve the phosphorylation by protein kinase C (PKC) or other kinases and the N-terminal cleavage by caspase and calpain. In vitro studies employing reconstituted detergent-skinned fiber bundles and cell culture generally show a detrimental effect of cTnT phosphorylation on muscle contraction, which is backed by some in vivo studies finding increased cTnT phosphorylation in heart failure, but contradicted by others. In addition, N-terminal cleavage of cTnT is thought to be another factor influencing cardiac contraction. Time-dependent degradation of cTnT has been observed in human serum upon myocardial infarction. These molecular changes might influence the immunoreactivity of cTnT in the clinical immunoassay and have consequences for the clinical interpretations of these measurements. No consensus has yet been reached on the occurrence and extent of these observations and their underlying processes are subject of intense scientific debate. This review will focus on discussing these modifications, their implications on physiology and disease and summarizes the complex interplays of different enzymes on the molecular forms of cTnT and their associated effects.
Original languageEnglish
Pages (from-to)47-56
JournalJournal of Molecular and Cellular Cardiology
Publication statusPublished - Oct 2013


  • Cardiac troponin T
  • Cardiac physiology
  • Phosphorylation
  • Fragmentation


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