Abstract
Skeletal muscle converts the thermodynamic force of the non-equilibrium ATP/ADP concentration ratio in the cytosol into mechanical force during contrac-tion1 [1]. As such, skeletal muscle function can be described using engineering concepts as a chemo-mechano transducer (Fig. 1). The molecular machinery in-volved in this conversion consists, amongst others, of filaments of actin and the motor protein myosin ATPase, and the calcium (Ca2+)-activated switch protein troponin [1]. The non-equilibrium cytosolic ATP/ADP concentration potential is thermodynamically buffered by the cellular pool of mitochondria via oxidative ADP phosphorylation. Kinetically, this cytosolic potential is buffered on a fast (i.e. (sub)second) time scale by creatine kinase (CK) and glycolysis, and on a slow (i.e. minutes) timescale by oxidative phosphorylation [2]. Muscle contraction and the associated conversion of thermodynamic ATP energy force is under voluntary, neural control [1]. It is initiated at the cellular level by action potential-gated re-lease of Ca2+ions from the sarcoplasmic reticulum (SR) stores into the myoplasm2.
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Jeneson, J.A.L., Westerhoff, H.V., Kushmerick, M.J. (2004). Metabolic Control Analysis of the ATPase Network in Contracting Muscle: Regulation of Contractile Function and ATP Free Energy Potential. In: Deutsch, A., Howard, J., Falcke, M., Zimmermann, W. (eds) Function and Regulation of Cellular Systems. Mathematics and Biosciences in Interaction. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-7895-1_4
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