ArticleBiophysical journal2025
ATP directly modulates thick filament structure and function in porcine myocardium.
Article in Biophysical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Cardiac contraction is achieved through cyclic cross-bridge interactions between overlapping myosin-containing thick filaments and actin-containing thin filaments. This process is powered by ATP hydrolysis by myosin, which must be sufficient for maintaining cardiac output. Myocardial ATP concentration is tightly maintained via several mechanisms. However, in decompensated end-stage heart failure, these mechanisms fail, resulting in depressed myocardial ATP levels, impaired cross-bridge kinetics, and reduced cardiac output. Here, we tested the hypothesis that ATP has a direct effect on thick filament activation by subjecting permeabilized porcine myocardium to increasing concentrations of ATP. Small-angle x-ray diffraction showed that higher ATP concentrations caused a structural transition in myosin heads from quasihelically ordered OFF states, where they are held in close proximity to the thick filament backbone, to disordered ON states, where they are free to move closer to thin filaments. Mechanically, high ATP did not alter maximum calcium-activated tension, although increasing ATP right-shifted the tension versus calcium (Ca
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