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- W2017696918 abstract "Background: A well-established function of titin is the determination of passive tension (Fpassive) in myocardium. Modifications to the elastic titin region have been suggested to contribute to left ventricular (LV) diastolic dysfunction in heart failure (HF). Titin-based stiffness can be modulated by isoform switch or phosphorylation. Results: We find that titin-isoform switch accounts for a significant amount of myocardial stiffness modulation, giving rise to increased or reduced Fpassive in different types of heart failure. In addition, both acute and chronic modulations of cardiomyocyte Fpassive occur via altered titin phosphorylation. Cyclic AMP-dependent protein kinase-A, cGMP-dependent protein kinase-G, and extracellular signal-regulated kinase-2 phosphorylate titin at a cardiac-specific domain, the N2Bus; this phosphorylation results in a reduction in cardiomyocyte Fpassive in various species. PKCα phosphorylates the PEVK-domain of titin, which increases Fpassive of normal mouse cardiomyocytes, but does not significantly alter Fpassive of cardiomyocytes obtained from a dog HF model. Calcium/calmodulin-dependent protein kinase-II (CaMKII) is the first kinase found to phosphorylate both the N2Bus and the PEVK-domain. This phosphorylation reduces cardiomyocyte Fpassive, as demonstrated in skinned mouse cardiomyocytes incubated with recombinant CaMKIIδ. Moreover, Fpassive is elevated in cardiomyocytes of CaMKIIγ/δ double knockout mice and reduced in those of CaMKIIδ-overexpressing transgenic mice. In both human and experimental HF, a global titin phosphorylation deficit is observed, but site-specific titin phosphorylation can be increased or decreased in HF, presumably depending on the activity and expression level of the relevant kinases. Conclusion: Titin phosphorylation may have beneficial effects in the heart via reducing myocardial diastolic stiffness and improving ventricular filling. Altered titin phosphorylation in HF may severely affect Fpassive and compromise cardiac function. The degree, to which the different protein kinases contribute to alterations in diastolic passive stiffness, needs to be determined." @default.
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- W2017696918 date "2014-01-01" @default.
- W2017696918 modified "2023-09-30" @default.
- W2017696918 title "Myocardial Titin: An Important Modifier of Cardiac Stiffness" @default.
- W2017696918 doi "https://doi.org/10.1016/j.bpj.2013.11.1972" @default.
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