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Published on: January 25, 2018
Creatine kinase activity in rat skeletal muscle relates to myosin phenotype during development
J F Watchko1, M J Daood, J J LaBella
1Department of Pediatrics, Magee-Womens Research Institute, University of Pittsburgh School of Medicine, Pennsylvania 15213, USA.
Insights
Creatine kinase (CK) activity increases in rat skeletal muscles after birth, correlating with myosin heavy chain (MHC) changes. Type IIb MHC expression significantly predicts this rise in CK activity.
Area of Science:
- Muscle Physiology
- Biochemistry
- Developmental Biology
Background:
- Creatine kinase (CK) plays a crucial role in maintaining intracellular energy supply in skeletal muscle through ATP buffering.
- Understanding the developmental expression of CK and its relationship with muscle fiber type is essential for comprehending muscle energetics.
Purpose of the Study:
- To investigate the postnatal expression patterns of CK activity and isoform phenotype in different rat skeletal muscles.
- To correlate developmental changes in CK activity with myosin heavy chain (MHC) phenotype, an indicator of contractile protein energetic demands.
Main Methods:
- Assessed CK activity and isoform phenotype across four distinct skeletal muscles (diaphragm, intercostal, external abdominal oblique, soleus) during postnatal development in rats.
- Correlated CK activity with MHC isoform composition, analyzing the ratio of adult to developmental MHC isoforms.
- Utilized stepwise regression analysis to identify specific MHC isoforms influencing CK activity variance.
Main Results:
- CK activity was low at birth and increased postnatally in all studied muscles, with the highest levels observed in adult intercostal and external abdominal oblique muscles.
- A strong correlation was found between CK activity and MHC phenotype (r2 = 0.93, p < 0.001).
- Type IIb MHC expression was the primary determinant, explaining 79% of the developmental variance in CK activity.
Conclusions:
- CK activity exhibits muscle-specific increases during postnatal development, closely linked to the energetic demands reflected by MHC isoform composition.
- The energy buffering role of CK is hypothesized to be most significant in muscles predominantly expressing the IIb MHC isoform.
Abstract:
Creatine kinase (CK) has been implicated in the maintenance of skeletal muscle intracellular energy supply via its ATP buffering capacity. We examined the postnatal expression of CK activity and isoform phenotype in four skeletal muscles [diaphragm (DIA), intercostal (IC), external abdominal oblique (EAO), and the soleus (SOL)] of the rat. Moreover, we correlated CK activity during development with postnatal changes in myosin heavy chain (MHC) phenotype, the latter an index of relative changes in the energetic demands of muscle contractile proteins. CK activity was lowest in the immediate newborn period and increased in all muscles during postnatal development; the highest levels of CK activity were observed in the adult IC and EAO. CK activity did relate to the MHC phenotype as indexed by the ratio of adult MHC isoform content (slow + IIa + IIx + IIb) to developmental MHC isoform content (slow + neonatal; r2 = 0.93, p < 0.001). Stepwise regression revealed that type IIb MHC expression alone accounted for 79% of the developmental variance in CK activity. We conclude that CK activity increases during postnatal development in a muscle specific fashion and relates to the energetic demands of the muscle contractile proteins as reflected by MHC isoform composition. We speculate that the role of CK as an energy buffer is greatest in muscles expressing the IIb MHC isoform.
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