Key result
Creatine kinase inhibition in computational models increases ATP synthesis amplitude ~163%, supporting temporal energy buffering.
Computational modeling suggests that creatine kinase contributes less than one-third to net transcytosolic energy transport in muscle cells.
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No immediate clinical implications from computational models; leaves open creatine kinase's quantitative role in cardiac energy transport pending in vivo data.
Background Distinct functions have been hypothesized for the creatine kinase (CK) enzyme catalyzing the reversible transfer of the high-energy phosphate group of ATP to creatine. In muscle cells, two CK isoforms might mediate (i) temporal energy buffering to maintain ATP homeostasis and (ii) energy transport from mitochondria to myofibrils via the “phosphocreatine shuttle” mechanism. Here we investigate the relative importance of the two roles using a computational model [1]. Model simulations predict a contribution of CK to the net transcytosolic energy transport of less than 1/3.
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Hettling et al. (2010) studied Cardiac muscle energy transport. Creatine kinase (CK) inhibition by 98% vs. Full CK activity was evaluated on Amplitude of ATP synthesis. In a computational model of cardiac muscle, 98% inhibition of creatine kinase increased the amplitude of ATP synthesis from 215±23 to 566±31 μM*s-1, supporting its role as a temporal energy buffer.
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