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Am J Physiol Heart Circ Physiol 282: H2259-H2264, 2002. First published January 24, 2002; doi:10.1152/ajpheart.00264.2001
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Vol. 282, Issue 6, H2259-H2264, June 2002

Activation time of myocardial oxidative phosphorylation in creatine kinase and adenylate kinase knockout mice

Lori A. Gustafson and Johannes H. G. M. Van Beek

Laboratory for Physiology, Institute for Cardiovascular Research, Vrije Universiteit, 1081 BT Amsterdam, The Netherlands

Our goal was to determine whether mice genetically altered to lack either creatine kinase (M/MtCK-/-) or adenylate kinase (AK-/-) show altered properties in the dynamic regulation of myocardial oxygen consumption (MVO2). We measured contractile function, oxygen consumption, and the mean response time of oxygen consumption to a step increase in heart rate [i.e., mitochondrial response time (tmito)] in isolated Langendorff-perfused hearts from wild-type (n = 6), M/MtCK-/- (n = 6), and AK-/- (n = 4) mice. Left ventricular developed pressure was higher in M/MtCK-/- hearts (88.2 ± 6.8 mmHg) and lower in AK-/- hearts (46.7 ± 9.4 mmHg) compared with wild-type hearts (60.7 ± 10.1 mmHg) at the basal pacing rate. Developed pressure fell slightly when heart rate was increased in all three groups. Basal MVO2 at 300 beats/min was 19.1 ± 2.4, 19.4 ± 1.5, and 16.3 ± 1.9 µmol · min-1 · g dry wt-1 for M/MtCK-/-, AK-/-, and wild type, respectively, which increased to 25.5 ± 3.7, 25.4 ± 2.6, and 22.0 ± 2.6 µmol · min-1 · g-1, when heart rate was increased to 400 beats/min. The tmito was significantly faster in M/MtCK-/- hearts: 3.0 ± 0.3 versus 7.3 ± 0.6 and 8.0 ± 0.4 s for M/MtCK-/-, AK-/-, and wild-type hearts, respectively. Our results demonstrate that MVO2 of M/MtCK-/- hearts adapts more quickly to an increase in heart rate and thereby support the hypothesis that creatine kinase acts as an energy buffer in the cytosol, which delays the energy-related signal between sites of ATP hydrolysis and mitochondria.

oxygen consumption; mitochondria; metabolic wave


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