Profiles of creatine kinase isoenzyme compositions in single muscle fibres of different types

Yamashita, Katsumasa; Yoshioka, Toshitada

doi:10.1007/bf01781172

Cited by 90 publications

(58 citation statements)

References 35 publications

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“…Muscles composed primarily of fast-twitch fibers, such as the extensor digitorum longus, plantaris, gastrocnemius, and anterior tibialis (36), expressed relatively high levels of glycogen synthase. These differences in expression of transgenic glycogen synthase are consistent with the lower expression of endogenous muscle creatine kinase in slow-twitch muscle fibers (37,38), as well as with expression of other transgenic proteins driven by muscle creatine kinase regulatory gene cassettes (24,35).…”

Section: Resultssupporting

confidence: 69%

Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle.

Manchester

Skurat²,

Roach³

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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To investigate the role of glycogen synthase in controlling glycogen accumulation, we generated three lines of transgenic mice in which the enzyme was overexpressed in skeletal muscle by using promoter-enhancer elements derived from the mouse muscle creatine kinase gene. In all three lines, expression was highest in muscles composed primarily of fast-twitch fibers, such as the gastrocnemius and anterior tibialis. In these muscles, glycogen synthase activity was increased by as much as 10-fold, with concomitant increases (up to 5-fold) in the glycogen content. The uridine diphosphoglucose concentrations were markedly decreased, consistent with the increase in glycogen synthase activity. Levels of glycogen phosphorylase in these muscles increased (up to 3-fold), whereas the amount of the insulin-sensitive glucose transporter 4 either remained unchanged or decreased. The observation that increasing glycogen synthase enhances glycogen accumulation supports the conclusion that the activation of glycogen synthase, as well as glucose transport, contributes to the accumulation of glycogen in response to insulin in skeletal muscle.

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Section: Resultssupporting

confidence: 69%

Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle.

Manchester

Skurat²,

Roach³

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

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“…In our study, although patients with moderate COPD did not exhibit a significant reduction in diaphragm creatine kinase content, it could be hypothesised that moderate levels of ROS in their muscles may have already influenced enzyme activity, since their levels were indeed similar to those of the severe patients. Moreover, it has been well established that slow-twitch oxidative fibres exhibit the lowest creatine kinase activity in skeletal muscles [30]. On this basis, it is possible to conclude that the decreased creatine kinase activity in the diaphragms of our severe COPD patients could be partly due to their fibre-type shift towards a more fatigue-resistant phenotype.…”

Section: Diaphragm Carbonylated Proteinsmentioning

confidence: 56%

Oxidised proteins and superoxide anion production in the diaphragm of severe COPD patients

Minguella²,

et al. 2009

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In the diaphragms of chronic obstructive pulmonary disease (COPD) patients, the nature of oxidatively modified proteins and superoxide anion production were explored.Diaphragm specimens were obtained through thoracotomy because of localised lung lesions in COPD patients (16 severe and eight moderate) and 10 control subjects. Lung and respiratory muscle functions were evaluated. Oxidised proteins were identified using immunoblotting and mass spectrometry. Protein and activity levels of the identified proteins were determined using immunoblotting and activity assays. Lucigenin-derived chemiluminescence signals in a luminometer were used to determine superoxide anion levels in muscle compartments (mitochondria, membrane and cytosol) using selective inhibitors.In severe COPD patients compared with controls, respiratory muscle function was impaired; creatine kinase, carbonic anhydrase III, actin and myosin were oxidised; myosin carbonylation levels were increased five-fold; creatine kinase content and activity and myosin protein were reduced; superoxide anion levels were increased in both mitochondria and membrane compartments; and the percentage of superoxide anion inhibition achieved by rotenone was significantly greater.In severe COPD patients, oxidation of diaphragm proteins involved in energy production and contractile performance is likely to partially contribute to the documented respiratory muscle dysfunction. Furthermore, generation of the superoxide anion was increased in the diaphragms of these patients.

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“…Although the endogenous MCK gene is expressed in all skeletal muscle types, MCK mRNA and enzyme activity levels differ among fiber types. MCK enzyme activity is about twofold higher in rat fast glycolytic fibers than in slow oxidative fibers and intermediate in fast oxidative-glycolytic fibers (72). MCK mRNA is also more abundant in the predominantly fast plantaris and gastrocnemius mouse muscles than in the slow soleus muscle (66).…”

Section: Discussionmentioning

confidence: 92%

E-Box Sites and a Proximal Regulatory Region of the Muscle Creatine Kinase Gene Differentially Regulate Expression in Diverse Skeletal Muscles and Cardiac Muscle of Transgenic Mice

Shield

Haugen

Clegg

et al. 1996

Molecular and Cellular Biology

106

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Previous analysis of the muscle creatine kinase (MCK) gene indicated that control elements required for transcription in adult mouse muscle differed from those required in cell culture, suggesting that distinct modes of muscle gene regulation occur in vivo. To examine this further, we measured the activity of MCK transgenes containing E-box and promoter deletions in a variety of striated muscles. Simultaneous mutation of three E boxes in the 1,256-bp MCK 5 region, which abolished transcription in muscle cultures, had strikingly different effects in mice. The mutations abolished transgene expression in cardiac and tongue muscle and caused a reduction in expression in the soleus muscle (a muscle with many slow fibers) but did not affect expression in predominantly fast muscles: quadriceps, abdominals, and extensor digitorum longus. Other regulatory sequences with muscle-type-specific activities were found within the 358-bp 5-flanking region. This proximal region conferred relatively strong expression in limb and abdominal skeletal muscles but was inactive in cardiac and tongue muscles. However, when the 206-bp 5 enhancer was ligated to the 358-bp region, high levels of tissue-specific expression were restored in all muscle types. These results indicate that E boxes and a proximal regulatory region are differentially required for maximal MCK transgene expression in different striated muscles. The overall results also imply that within skeletal muscles, the steady-state expression of the MCK gene and possibly other muscle genes depends on transcriptional mechanisms that differ between fast and slow fibers as well as between the anatomical and physiological attributes of each specific muscle.Creatine kinase catalyzes the regeneration of ATP from creatine phosphate and provides energy for contraction in all striated muscle types. The muscle creatine kinase (MCK) gene is transcriptionally activated during differentiation of myoblasts to myocytes (8, 31) and encodes the predominant creatine kinase isoform expressed in mammalian skeletal and cardiac muscle. While it seems likely that intrinsic differences in striated muscle anatomy and physiology would affect MCK gene expression, little is known concerning the steady-state mechanisms of MCK transcription in diverse muscle types. This transgenic study seeks to identify regulatory regions and elements within the MCK gene that are involved in controlling muscle-type-specific expression.Several regions within the mouse MCK gene 5Ј-flanking sequence are required for muscle-specific expression in cultured myocytes and cardiomyocytes (1, 32, 64). Of particular interest is a 206-bp enhancer located approximately 1 kb upstream of the transcription start site. This region functions in an orientation-independent manner and drives the expression of heterologous promoters in skeletal myocytes (32). The 5Ј MCK enhancer contains a number of sequence motifs-including the E box, CArG, and AT-rich sites-which are recognized by tissue-specific and ubiquitous transcription factors. Mutation...

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Profiles of creatine kinase isoenzyme compositions in single muscle fibres of different types

Cited by 90 publications

References 35 publications

Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle.

Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle.

Oxidised proteins and superoxide anion production in the diaphragm of severe COPD patients

E-Box Sites and a Proximal Regulatory Region of the Muscle Creatine Kinase Gene Differentially Regulate Expression in Diverse Skeletal Muscles and Cardiac Muscle of Transgenic Mice

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