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J Appl Physiol 84: 1166-1173, 1998;
8750-7587/98 $5.00
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Vol. 84, Issue 4, 1166-1173, April 1998

Absence of myofibrillar creatine kinase and diaphragm isometric function during repetitive activation

John J. Labella1, Monica J. Daood1, A. P. Koretsky2, Brian B. Roman2, Gary C. Sieck3, Be Wieringa4, and Jon F. Watchko1

1 Department of Pediatrics, Magee-Womens Research Institute, University of Pittsburgh School of Medicine, Pittsburgh 15213; 2 Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213; 3 Departments of Anesthesiology, and Physiology and Biophysics, Mayo Clinic and Mayo Medical School, Rochester, Minnesota 55905; and 4 Department of Cell Biology and Histology, University of Nijmegen, Nijmegen, The Netherlands

Creatine kinase (CK) provides ATP buffering in skeletal muscle and is expressed as 1) cytosolic myofibrillar CK (M-CK) and 2) sarcomeric mitochondrial CK (ScCKmit) isoforms that differ in their subcellular localization. We compared the isometric contractile and fatigue properties of 1) control CK-sufficient (Ctl), 2) M-CK-deficient (M-CK[-/-]), and 3) combined M-CK/ScCKmit-deficient null mutant (CK[-/-]) diaphragm (Dia) to determine the effect of the absence of M-CK activity on Dia performance in vitro. Baseline contractile properties were comparable across groups except for specific force, which was ~16% lower in CK[-/-] Dia compared with M-CK[-/-] and Ctl Dia. During repetitive activation (40 Hz, <FR><NU>1</NU><DE>3</DE></FR> duty cycle), force declined in all three groups. This decline was significantly greater in CK[-/-] Dia compared with Ctl and M-CK[-/-] Dia. The pattern of force decline did not differ between M-CK[-/-] and Ctl Dia. We conclude that Dia isometric muscle function is not absolutely dependent on the presence of M-CK, whereas the complete absence of CK acutely impairs isometric force generation during repetitive activation.

respiratory muscle; fatigue; oxidative capacity


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