Reactive oxygen species induce various posttranslational modifications of myofilament proteins, including direct oxidation, phosphorylation, and cleavage, which impact cardiac contractility.
Oxidative stress accompanies a wide spectrum of clinically important cardiac disorders, including ischemia/reperfusion, diabetes mellitus, and hypertensive heart disease. Although reactive oxygen species (ROS) can activate signaling pathways that contribute to ischemic preconditioning and cardioprotection, high levels of ROS induce structural modifications of the sarcomere that impact on pump function and the pathogenesis of heart failure. However, the precise nature of the redox-dependent change in contractility is determined by the source/identity of the oxidant species, the level of oxidative stress, and the chemistry/position of oxidant-induced posttranslational modifications on individual proteins within the sarcomere. This review focuses on various ROS-induced posttranslational modifications of myofilament proteins (including direct oxidative modifications of myofilament proteins, myofilament protein phosphorylation by ROS-activated signaling enzymes, and myofilament protein cleavage by ROS-activated proteases) that have been implicated in the control of cardiac contractility.
Susan F. Steinberg (Thu,) conducted a review in Cardiac disorders. Reactive oxygen species (ROS) was evaluated. Reactive oxygen species induce various posttranslational modifications of myofilament proteins, including direct oxidation, phosphorylation, and cleavage, which impact cardiac contractility.
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