Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase

FOUCAULT, Georges; VACHER, Monique; Меркулова, Т. И.; Keller, Andreas; ARRIO-DUPONT, Martine

doi:10.1042/0264-6021:3380115

Cited by 20 publications

(19 citation statements)

References 23 publications

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“…Two‐dimensional gel electrophoresis allows the clear identification of the mouse enolase α and β subunits [19]. Previous analyses of rabbit striated muscle extracts have shown that the migration of the α and β subunits are quite similar to those observed in mice [18]. However, the α enolase subunit is barely detectable in rabbit skeletal muscles.…”

Section: Resultsmentioning

confidence: 99%

“…Protein extracts for two‐dimensional gel electrophoresis analysis were prepared from rabbit muscle as already described [18]. Two‐dimensional gel electrophoresis (2‐DE) was performed according to O’Farrell with minor modifications as previously described [18,19]. Briefly, in the first dimension, protein samples were submitted to a basic nonequilibrium pH gradient electrophoresis (NEPHGE) in 4% polyacrylamide gels containing 2% ampholines (pH 3.5–10.0).…”

Section: Methodsmentioning

confidence: 99%

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Denervation of rabbit gastrocnemius and soleus muscles

Nozais

Меркулова

Keller

et al. 1999

European Journal of Biochemistry

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We report here, for the first time, the expression of the muscle-specific isoform of the glycolytic enzyme, enolase (EC 4.2.1.11) (b enolase), in rabbit skeletal muscles. We have analysed the fast-twitch gastrocnemius and the slow-twitch soleus muscles during normal postnatal development and following denervation. We show that, in rabbit, as already described in rodents, b enolase gene expression behaves as a good marker of the fast-twitch fibers. In soleus muscle, the b enolase transcript level is 10±20% of that found in gastrocnemius. Denervation, performed at 8 postnatal days, induces an important drop of b enolase transcript levels in both developing soleus and gastrocnemius muscles, with a 80% decrease observed 1 week after denervation in the operated muscles, as compared to the corresponding contralateral muscles. Thereafter, the b enolase transcript level continues to decrease in the fast-twitch muscle, with the b enolase subunit being detectable only in the atrophic fast-twitch fibers. In contrast, the b transcript level tends to increase in the denervated slow-twitch muscle, reaching about 50% of that in contralateral soleus, at 7 weeks after surgery. The level of b enolase transcripts still expressed after denervation seems to stabilize at the same low level in both types of inactive muscles. This suggests that the small fraction of b enolase expression which is not controlled by the nerve, or by the contractile activity imposed by it, is independent of the muscle phenotype.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Denervation of rabbit gastrocnemius and soleus muscles

Nozais

Меркулова

Keller

et al. 1999

European Journal of Biochemistry

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“…However, some of the β immunoreactivity appeared striated. Using confocal microscopy, we could demonstrate its location at the M band [10,17]. The α subunit appeared mostly striated [8] and located at the level of the M band as well [10].…”

Section: Discussionmentioning

confidence: 99%

Differential modulation of α, β and γ enolase isoforms in regenerating mouse skeletal muscle

Меркулова

Dehaupas

Nevers

et al. 2000

European Journal of Biochemistry

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Nothing is known about the expression of the glycolytic enzyme enolase in skeletal muscle alterations such as myofiber degeneration and regeneration. Enolase is a dimeric enzyme which exhibits cell type specific isoforms. The embryonic form, aa, remains expressed in most adult tissues, whereas a transition towards specific isoforms occurs during ontogenesis in two cell types with high energy requirements: ag and gg in neurons, ab and bb in striated muscle cells. During murine myogenesis, b enolase transcripts are detected early in the forming muscles, and the b gene is further upregulated at specific stages of muscle development. The a and b subunits exhibit characteristic developmental microheterogeneity patterns. High levels of b enolase subunits characterize the glycolytic fast-twitch fibers of adult muscles. We have investigated the expression of enolase subunits in a mouse experimental model of muscle regeneration. Following a single intramuscular injection of the necrotic agent cardiotoxin, we observed a rapid decrease in the level of the major muscle enolase subunit b, accounting for the drop in total enolase activity that correlated with the degeneration of myofibers. Concomitant with the regeneration of new fibers, b subunit levels began to increase, reaching normal values by 30 days after injury. Changes in the embryonic and ubiquitous subunit, a, mimicked those occurring during development by two aspects: modifications in electrophoretic variants and redistribution between soluble and insoluble compartments of muscle extracts. Imunocytochemical analyses of a and b enolase subunits first revealed a homogeneous labeling within myofibers. Striations characteristic of normal adult muscle tissue were visible again by day 14 after injury. A perinuclear a and b immunoreactivity was often observed in regenerating myofibers but its functional significance remains to be elucidated. Double labeling experiments with anti-g enolase and FITC-a bungarotoxin allowed us to follow the neuromuscular junction remodeling that occurs during muscle regeneration despite the absence of nerve injury.

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“…The high ATP hydrolysis rates required for skeletal muscle contraction are supported by the anchoring to sarcomeres of glycolytic enzymes, including GAP, phosphoglycerate kinase, phosphoglycerate mutase, and enolase (Foucault et al, 1999;Sullivan et al, 2003). The high ATP hydrolysis rates required for skeletal muscle contraction are supported by the anchoring to sarcomeres of glycolytic enzymes, including GAP, phosphoglycerate kinase, phosphoglycerate mutase, and enolase (Foucault et al, 1999;Sullivan et al, 2003).…”

Section: Metabolic Compartmentalization Of Cilia and Flagellamentioning

confidence: 99%

ATP Production inChlamydomonas reinhardtiiFlagella by Glycolytic Enzymes

Mitchell

Pedersen

Feely

et al. 2005

MBoC

108

109

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Eukaryotic cilia and flagella are long, thin organelles, and diffusion from the cytoplasm may not be able to support the high ATP concentrations needed for dynein motor activity. We discovered enzyme activities in the Chlamydomonas reinhardtii flagellum that catalyze three steps of the lower half of glycolysis (phosphoglycerate mutase, enolase, and pyruvate kinase). These enzymes can generate one ATP molecule for every substrate molecule consumed. Flagellar fractionation shows that enolase is at least partially associated with the axoneme, whereas phosphoglycerate mutase and pyruvate kinase primarily reside in the detergent-soluble (membrane + matrix) compartments. We further show that axonemal enolase is a subunit of the CPC1 central pair complex and that reduced flagellar enolase levels in the cpc1 mutant correlate with the reduced flagellar ATP concentrations and reduced in vivo beat frequencies reported previously in the cpc1 strain. We conclude that in situ ATP synthesis throughout the flagellar compartment is essential for normal flagellar motility.

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Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase

Cited by 20 publications

References 23 publications

Denervation of rabbit gastrocnemius and soleus muscles

Denervation of rabbit gastrocnemius and soleus muscles

Differential modulation of α, β and γ enolase isoforms in regenerating mouse skeletal muscle

ATP Production inChlamydomonas reinhardtiiFlagella by Glycolytic Enzymes

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