A Spatially Explicit Model Shows How Titin Stiffness Modulates Muscle Mechanics and Energetics
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چکیده
منابع مشابه
Phosphorylation of Titin Modulates Passive Stiffness of Cardiac Muscle in a Titin Isoform-dependent Manner
We investigated the effect of protein kinase A (PKA) on passive force in skinned cardiac tissues that express different isoforms of titin, i.e., stiff (N2B) and more compliant (N2BA) titins, at different levels. We used rat ventricular (RV), bovine left ventricular (BLV), and bovine left atrial (BLA) muscles (passive force: RV > BLV > BLA, with the ratio of N2B to N2BA titin, approximately 90:1...
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Question: How does phosphorylation of titan affect cardiac function? Background: Sarcomeres are the repeating contractile subunits from which the myofibrils of striated muscle are built. Titin is a large sarcomeric protein involved in muscle elasticity and myofibril scaffolding, which provides passive tension to muscle based on physiological demands. In mammalian cardiac tissue, there are two i...
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The contractile units of striated muscle, the sarcomeres, comprise the thick (myosin) and thin (actin) filaments mediating active contraction and the titin filaments determining "passive" elasticity. We hypothesized that titin may be more active in muscle contraction by directly modulating thick-filament properties. We used single-myofibril mechanical measurements and atomic force microscopy of...
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1. To celebrate this Festschrift for Professor Colin Gibbs, as an invited speaker, I would like to review briefly my 35 year research career in cardiac physiology. 2. My career started in the late 1960s in Tokyo with my serendipitous discovery of E max (ventricular end-systolic maximum elastance) as a load-independent contractility index based on the time-varying elastance (E(t)) model of the v...
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ژورنال
عنوان ژورنال: Integrative and Comparative Biology
سال: 2018
ISSN: 1540-7063,1557-7023
DOI: 10.1093/icb/icy055