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Articles in PresS, published online ahead of print January 24, 2002
Am J Physiol Heart Circ Physiol, 10.1152/ajpheart.00264.2001
Submitted on March 29, 2001
Accepted on December 31, 1969
1 Department of Anaesthesiology Academic Medical Centre, University of Amsterdam, Amsterdam, Netherlands
Our purpose 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. We measured contractile function, oxygen consumption and the mean response time of oxygen consumption to a step increase in heart rate (i.e. 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 lowered in AK -/- hearts (46.7 ±9.4 mmHg) compared to 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 myocardial oxygen consumption at 300 bpm was 19.1 ± 2.4, 19.4 ± 1.5 and 16.3 ± 1.9 µmol/min/g dwt 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/g, when heart rate was increased to 400 bpm. The tmito was significantly faster in M/MtCK -/- hearts: 3.0 ± 0.3 vs 7.3 ± 0.6 and 8.0 ± 0.4 sec for M/MtCK -/- , AK -/- and wild-type hearts, respectively. Our results demonstrate that myocardial oxygen consumption 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.
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