Key result
Physiologically relevant covalent and noncovalent modifications in troponin, including isoform switching and missense mutations, directly affect sarcomeric regulation and cardiac contraction.
This review highlights the mechanisms by which covalent and noncovalent modifications of troponin regulate cardiac contraction.
Does not support clinical troponin modification testing yet; leaves open targeted therapies while extending mechanistic understanding.
Troponin is essential for the regulation of cardiac contraction. Troponin is a sarcomeric molecular switch, directly regulating the contractile event in concert with intracellular calcium signals. Troponin isoform switching, missense mutations, proteolytic cleavage, and posttranslational modifications are known to directly affect sarcomeric regulation. This review focuses on physiologically relevant covalent and noncovalent modifications in troponin as part of a thematic series on cardiac thin filament function in health and disease.
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Metzger et al. (2004) conducted a review in Cardiac contraction and thin filament function. Covalent and noncovalent modifications in troponin was evaluated. Physiologically relevant covalent and noncovalent modifications in troponin, including isoform switching and missense mutations, directly affect sarcomeric regulation and cardiac contraction.
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