Key result
Myofilament Ca2+ sensitivity is enhanced in failing human cardiomyocytes compared to non-failing cells, associated with a shift to dephosphorylated Troponin I and reduced MLC-2 phosphorylation.
Population
Single skinned human left ventricular cardiomyocytes mechanically isolated from end-stage failing human…
Design
Editorial
Authors
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Altered phosphorylation of myofilament proteins, particularly decreased Troponin I phosphorylation, contributes to increased Ca2+ sensitivity in end-stage human heart failure, providing a molecular rationale for the benefits of beta-blocker therapy.
Altered phosphorylation of myofilament proteins, particularly decreased Troponin I phosphorylation, contributes to increased Ca2+ sensitivity in end-stage human heart failure, providing a molecular rationale for the benefits of beta-blocker therapy.
W. Schillinger (2002) conducted an editorial in Heart failure. End-stage heart failure vs. Non-failing donor hearts was evaluated on Myofilament Ca2+ sensitivity and phosphorylation state of contractile proteins. Myofilament Ca2+ sensitivity is enhanced in failing human cardiomyocytes compared to non-failing cells, associated with a shift to dephosphorylated Troponin I and reduced MLC-2 phosphorylation.
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