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J Appl Physiol 88: 973-980, 2000;
8750-7587/00 $5.00
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Vol. 88, Issue 3, 973-980, March 2000

Myofibrillar or mitochondrial creatine kinase deficiency alone does not impair mouse diaphragm isotonic function

Jon F. Watchko1, Monica J. Daood1, Bé Wieringa2, and Alan P. Koretsky3

1 Department of Pediatrics, Magee-Womens Research Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213; 2 Department of Cell Biology and Histology, University of Nijmegen, Nijmegen, The Netherlands; and 3 Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213

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. The diaphragm (Dia) expresses both M-CK and ScCKmit in abundance. We compared the power and work output of 1) control CK-sufficient (Ctl), 2) M-CK-deficient [M-CK(-/-)], 3) ScCKmit-deficient [ScCKmit(-/-)], and 4) combined M-CK/ScCKmit-deficient null mutant [CK(-/-)] Dia during repetitive isotonic activations to determine the effect of CK phenotype on Dia function. Maximum power was obtained at ~0.4 tetanic force in all groups. M-CK(-/-) and ScCKmit(-/-) Dia were able to sustain power and work output at Ctl levels during repetitive isotonic activation (75 Hz, 330-ms duration repeated each second at 0.4 tetanic force load), and the duration of sustained Dia shortening was 67 ± 4 s in M-CK(-/-), 60 ± 4 s in ScCKmit(-/-), and 62 ± 5 s in Ctl Dia. In contrast, CK(-/-) Dia power and work declined acutely and failed to sustain shortening altogether by 40 ± 6 s. We conclude that Dia power and work output are not absolutely dependent on the presence of either M-CK or ScCKmit, whereas the complete absence of CK acutely impairs Dia shortening capacity during repetitive activation.

respiratory muscle; fatigue; myosin heavy chain


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