Changes in glycolytic network and mitochondrial design in creatine kinase-deficient muscles

Skeletal muscles respond with high plasticity to pathobiological conditions or changes in physiological demand by remodeling cytoarchitectural and metabolic characteristics of individual myocytes. We have previously shown that muscles of mice without mitochondrial and/or cytosolic creatine kinases (...

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Veröffentlicht in:Muscle & nerve 2001-09, Vol.24 (9), p.1188-1196
Hauptverfasser: de Groof, Ad J. C., Oerlemans, Frank T. J. J., Jost, Carolina R., Wieringa, Bé
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Sprache:eng
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Zusammenfassung:Skeletal muscles respond with high plasticity to pathobiological conditions or changes in physiological demand by remodeling cytoarchitectural and metabolic characteristics of individual myocytes. We have previously shown that muscles of mice without mitochondrial and/or cytosolic creatine kinases (ScCKmit−/− and/or M‐CK−/−) partly compensate for the defect(s) by redirecting metabolic pathways and ultrastructural characteristics. Here, we show by semiquantitative Western blot analysis that the compensatory changes involve mutation‐ and fiber‐type–specific coordinated regulation of divergent but functionally coupled groups of proteins. Fast‐twitch gastrocnemius muscle of CK−−/−− mice display a two‐ to fourfold upregulation of mitochondrial cytochrome c oxidase, inorganic phosphate carrier, adenine nucleotide translocator, and voltage‐dependent anion channel proteins. In parallel, cytosolic myoglobin is upregulated. Slow‐twitch soleus muscle responds with changes in the glycolytic enzyme pattern, including a shift in lactate dehydrogenase isoenzyme composition. Adaptations in the network for oxidative adenosine triphosphate (ATP) production are already apparent at 17 days of age. © 2001 John Wiley & Sons, Inc. Muscle Nerve 24: 1188–1196, 2001
ISSN:0148-639X
1097-4598
DOI:10.1002/mus.1131