Interactions between β-enolase and creatine kinase in the cytosol of skeletal muscle cells

FOUCAULT, Georges; VACHER, Monique; Cribier, Sophie; ARRIO-DUPONT, Martine

doi:10.1042/0264-6021:3460127

Cited by 7 publications

(4 citation statements)

References 18 publications

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“…Stimulation-induced changes also include an enhanced mitochondrial creatine kinase activity [47]. However, overall creatine kinase activity is lower in slow-twitching fibres as compared to fast muscles [48]. The densitometric analysis of unstimulated versus chronic electro-stimulated fibres agrees with these two findings and has demonstrated a concomitant increase in mitochondrial creatine kinase and a decrease in its extra-mitochondrial isozyme.…”

Section: Discussionsupporting

confidence: 76%

Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation

Donoghue

Doran

Dowling

et al. 2005

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Physiological and biochemical responses of skeletal muscle fibres to enhanced neuromuscular activity under conditions of maximum activation can be studied experimentally by chronic low-frequency stimulation of fast muscles. Stimulation-induced changes in the expression pattern of the rabbit fast skeletal muscle proteome were evaluated by two-dimensional gel electrophoresis and compared to the altered isoform expression profile of established transformation markers such as the Ca 2+ -ATPase, calsequestrin and the myosin heavy chain. Sixteen muscle proteins exhibited a marked change in their expression level. This included albumin with a 4-fold increase in abundance. In contrast, glycolytic enzymes, such as enolase and aldolase, showed a decreased expression. Concomitant changes were observed with marker elements of the contractile apparatus. While the fast isoforms of troponin T and myosin light chain 2 were drastically down-regulated, their slow counterparts exhibited increased expression. Interestingly, mitochondrial creatine kinase expression increased while the cytosolic isoform of this key muscle enzyme decreased. The expression of the small heat shock protein HSP-B5/aB-crystallin and the oxygen carrier protein myoglobin were both increased 2-fold following stimulation. The observed changes indicate that the conversion into fatigue-resistant red fibres depends on: (i) the optimum utilization of free fatty acids via albumin transportation, (ii) a rearrangement of the creatine kinase isozyme pattern for enhanced mitochondrial activity, (iii) an increased availability of oxygen for aerobic metabolism via myoglobin transport, (iv) the conversion of the contractile apparatus to isoforms with slower twitch characteristics and (v) the up-regulation of chaperone-like proteins for stabilising myofibrillar components during the fast-to-slow transition process. D

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Section: Discussionsupporting

confidence: 76%

Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation

Donoghue

Doran

Dowling

et al. 2005

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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“…290-295). Alterations in several of these, including carbonic anhydrase [33], enolase [34], phosphoglycerate mutase [35], pyruvate kinase [36], and creatine kinase [37], have been implicated in pathological processes.…”

Section: Resultsmentioning

confidence: 99%

Two‐dimensional protein map of human vastus lateralis muscle

et al. 2003

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Protein samples of human vastus lateralis muscle were analyzed by two-dimensional gel electrophoresis, using immobilized pH gradients encompassing several pH regions in the first dimension and sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the second dimension. More than 500 protein spots on each gel were detected by silver staining, of which 150 were excised, digested in-gel with trypsin and characterized by matrix assisted laser desorptioin/ionization-mass spectrometry and tandem electrospray mass spectrometry. Using these techniques, 124 spots including contractile proteins and metabolic enzymes were identified. This database should provide a valuable resource for the definition of the functional properties of muscle fibres and for assessment of the influence of e.g., hypoxia, ischaemia and ageing on protein level.

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“…There is evidence for the existence of interactions between ␤-enolase and creatine kinase M, two key enzymes of the muscle metabolism, in the cytosol of skeletal muscle cells (42). ␤-Enolase is known to interact with many other proteins: indeed, the association between ␤-enolase and aldolase or pyruvate kinase is of high affinity, and ␤-enolase also binds the sarcomeric protein troponin (40).…”

Section: Discussionmentioning

confidence: 99%

Identification of O-linked N-Acetylglucosamine Proteins in Rat Skeletal Muscle Using Two-dimensional Gel Electrophoresis and Mass Spectrometry

Cieniewski-Bernard

Bastide²,

Lefebvre

et al. 2004

Molecular & Cellular Proteomics

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O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation. O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide ␤-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose. Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach. Fourteen proteins were identified as being O-GlcNAc modified. These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain). A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction. These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.

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Interactions between β-enolase and creatine kinase in the cytosol of skeletal muscle cells

Cited by 7 publications

References 18 publications

Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation

Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation

Two‐dimensional protein map of human vastus lateralis muscle

Identification of O-linked N-Acetylglucosamine Proteins in Rat Skeletal Muscle Using Two-dimensional Gel Electrophoresis and Mass Spectrometry

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