ArticleJournal of muscle research and cell motility2001
The muscle-specific enolase is an early marker of human myogenesis.
Article in Journal of muscle research and cell motility, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 56 citations in OpenAlex.
- Resistance-based exercise restores muscle health in dialysis patients.Journal of muscle research and cell motility · 2026Article
- The allergenic potential of enolases: physiological and pathophysiological insights.Current opinion in allergy and clinical immunology · 2025Review
- Article
- Multifunctional roles of γ-enolase in the central nervous system: more than a neuronal marker.Cell & bioscience · 2024Review
- Global genetic diversity, introgression, and evolutionary adaptation of indicine cattle revealed by whole genome sequencing.Nature communications · 2023Article
- Genome-wide epigenetic dynamics during postnatal skeletal muscle growth in Hu sheep.Communications biology · 2023Article
- Muscle Satellite Cell Heterogeneity: Does Embryonic Origin Matter?Frontiers in cell and developmental biology · 2021Review
- Neuromuscular Development and Disease: Learning FromFrontiers in cell and developmental biology · 2021Review
- Deleting Full Length Titin Versus the Titin M-Band Region Leads to Differential Mechanosignaling and Cardiac Phenotypes.Circulation · 2019Article
- Experimental and bioinformatic approach to identifying antigenic epitopes in human α- and β-enolases.Biochemistry and biophysics reports · 2018Article
- Modifications in the proteome of rainbow trout (Oncorhynchus mykiss) embryo and fry as an effect of triploidy induction.Fish physiology and biochemistry · 2017Article
- Inducing Stem Cell Myogenesis Using NanoScript.ACS nano · 2015Article
- Differential gene expression in small and large rainbow trout derived from two seasonal spawning groups.BMC genomics · 2014Article
- Sensor potency of the moonlighting enzyme-decorated cytoskeleton: the cytoskeleton as a metabolic sensor.BMC biochemistry · 2013Article
- α-Enolase, a multifunctional protein: its role on pathophysiological situations.Journal of biomedicine & biotechnology · 2012Review
- Gene expression profiling of alveolar soft-part sarcoma (ASPS).BMC cancer · 2009Article
Corrections and comments
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Authors and funding
7 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In higher vertebrates, the glycolytic enzyme enolase (2-phospho-D-glycerate hydrolase; EC 4.2.1.11) is active as a dimer formed from three different subunits, alpha, beta and gamma, encoded by separate genes. The expression of these genes is developmentally regulated in a tissue-specific manner. A shift occurs during development, from the unique embryonic isoform alphaalpha, towards specific isoforms in two tissues with high energy demands: alphagamma and gammagamma in the nervous system, alphabeta and betabeta in striated muscles. The alphaalpha remains widely distributed in adult tissues. Here we report the results of the first extensive study of beta enolase expression during human development. Indeed, the beta subunit is specifically expressed at early stages of human myogenesis. Immunocytochemical analyses demonstrated that it is first detected in the heart of 3-week-old embryos and in the myotomal compartment of somites from 4-week-old embryos. At this stage, the muscle-specific sarcomeric protein titin is expressed in this structure, which will give rise to all body skeletal muscles, but embryonic myosin heavy chain is not yet present. Analyses at the protein level show that, during human ontogenesis, myogenesis is accompanied by an increase in beta enolase expression and by a decrease in the expression of the two other alpha and gamma subunits. Furthermore, beta enolase subunit is expressed in proliferating myoblasts from both embryonic and post-natal muscles. In addition, clonal analysis of primary cell cultures, obtained from the leg muscle of a 7-week-old human embryo, revealed that the beta subunit is present in the dividing myoblasts of all four types, according to the classification of Edom-Vovard et al. [(1999) J Cell Sci 112: 191-199], but not in cells of the non-myogenic lineage. Myoblast fusion is accompanied by a large increase in beta enolase expression. Our results demonstrate that this muscle-specific isoform of a glycolytic enzyme (beta enolase) is among the earliest markers of myogenic differentiation in humans.
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