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• W2154554241 abstract "Rationale: In the myocardium, redox/cysteine modification of proteins regulating Ca 2+ cycling can affect contraction and may have therapeutic value. Nitroxyl (HNO), the one-electron-reduced form of nitric oxide, enhances cardiac function in a manner that suggests reversible cysteine modifications of the contractile machinery. Objective: To determine the effects of HNO modification in cardiac myofilament proteins. Methods and Results: The HNO-donor, 1-nitrosocyclohexyl acetate, was found to act directly on the myofilament proteins, increasing maximum force (F max ) and reducing the concentration of Ca 2+ for 50% activation (Ca 50 ) in intact and skinned cardiac muscles. The effects of 1-nitrosocyclohexyl acetate are reversible by reducing agents and distinct from those of another HNO donor, Angeli salt, which was previously reported to increase F max without affecting Ca50. Using a new mass spectrometry capture technique based on the biotin switch assay, we identified and characterized the formation by HNO of a disulfide-linked actin–tropomyosin and myosin heavy chain–myosin light chain 1. Comparison of the 1-nitrosocyclohexyl acetate and Angeli salt effects with the modifications induced by each donor indicated the actin–tropomyosin and myosin heavy chain–myosin light chain 1 interactions independently correlated with increased Ca 2+ sensitivity and force generation, respectively. Conclusions: HNO exerts a direct effect on cardiac myofilament proteins increasing myofilament Ca 2+ responsiveness by promoting disulfide bond formation between critical cysteine residues. These findings indicate a novel, redox-based modulation of the contractile apparatus, which positively impacts myocardial function, providing further mechanistic insight for HNO as a therapeutic agent." @default.
• W2154554241 created "2016-06-24" @default.
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• W2154554241 date "2012-09-28" @default.
• W2154554241 modified "2023-10-16" @default.
• W2154554241 title "Nitroxyl-Mediated Disulfide Bond Formation Between Cardiac Myofilament Cysteines Enhances Contractile Function" @default.
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• W2154554241 doi "https://doi.org/10.1161/circresaha.112.270827" @default.
• W2154554241 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3470471" @default.
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