Thyroid hormones differentially modulate enolase isozymes during rat skeletal and cardiac muscle development

Меркулова, Т. И.; Keller, Andreas; Oliviéro, P.; Marotte, F.; Samuel, J. L.; Rappaport, L.; Lamandé, Noël; Lucas, Marguerite

doi:10.1152/ajpendo.2000.278.2.e330

Cited by 19 publications

(17 citation statements)

References 46 publications

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“…T3 is known to stimulate gluconeogenesis and glucose production in the liver, thereby opposing the action of insulin on hepatic glucose production [111]. Our results extended this knowledge by showing that T3 significantly enhances the level of α -enolase, thereby participating in glycolysis and gluconeogenesis.…”

Section: Thyroid Hormones and Thyroid Statessupporting

confidence: 79%

Studies of Complex Biological Systems with Applications to Molecular Medicine: The Need to Integrate Transcriptomic and Proteomic Approaches

Silvestri

Lombardi

Lange³

et al. 2010

BioMed Research International

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Omics approaches to the study of complex biological systems with potential applications to molecular medicine are attracting great interest in clinical as well as in basic biological research. Genomics, transcriptomics and proteomics are characterized by the lack of an a priori definition of scope, and this gives sufficient leeway for investigators (a) to discern all at once a globally altered pattern of gene/protein expression and (b) to examine the complex interactions that regulate entire biological processes. Two popular platforms in “omics” are DNA microarrays, which measure messenger RNA transcript levels, and proteomic analyses, which identify and quantify proteins. Because of their intrinsic strengths and weaknesses, no single approach can fully unravel the complexities of fundamental biological events. However, an appropriate combination of different tools could lead to integrative analyses that would furnish new insights not accessible through one-dimensional datasets. In this review, we will outline some of the challenges associated with integrative analyses relating to the changes in metabolic pathways that occur in complex pathophysiological conditions (viz. ageing and altered thyroid state) in relevant metabolically active tissues. In addition, we discuss several new applications of proteomic analysis to the investigation of mitochondrial activity.

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Section: Thyroid Hormones and Thyroid Statessupporting

confidence: 79%

Studies of Complex Biological Systems with Applications to Molecular Medicine: The Need to Integrate Transcriptomic and Proteomic Approaches

Silvestri

Lombardi

Lange³

et al. 2010

BioMed Research International

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“…T3 is known to stimulate gluconeogenesis and glucose production in the liver, thereby opposing the action of insulin on hepatic glucose production (Merkulova et al, 2000). Our results extended this knowledge by showing that T3 significantly enhances the level of -enolase, which catalyses the reversible dehydration of 2-phosphoglycerate to phosphoenolpyruvate, thereby participating in glycolysis and gluconeogenesis.…”

Section: Thyroid Hormone Actions: Proteomicssupporting

confidence: 77%

Metabolic Action of Thyroid Hormones: Insights from Functional and Proteomic Studies

Silvestri¹,

Lombardi²,

Lange³

et al. 2008

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3,5,3'-triiodo-L-thyronine (T3) modulates development and growth, and in adult life it exerts a profound effect on basal metabolic rate, increasing respiration rate and simultaneously lowering metabolic efficiency. It mainly acts through the coordinated and synergistic modulation of both nuclear and mitochondrial genome expressions giving rise to a complex network of factors and cellular events not yet completely defined. Thus, understanding the effects of T3 requires investigations at several levels [such as genes and gene transcripts (genome and transcriptome), proteins and metabolites, functions and metabolic assessment (proteome and metabolome)]. As yet, the ultimate effects of T3 on tissue-proteomes remain largely unknown. The proteins are excellent targets in disease diagnostics, prognostics, and therapeutics, and therefore proteomic approaches [such as two-dimensional gel electrophoresis (2D-E), two-dimensional liquid chromatography (2-DL), and mass spectrometry (MS)] represent powerful tools for a) the discovery of novel hormone/drug targets and biomarkers, and b) the study of in vivo and in vitro hormone effects on cellular metabolism and protein expressions. Increasingly proteomic techniques are being adopted, in particular to avoid the limitations inherent in the more classical approaches, to solve analytical problems and obtain a more comprehensive identification and characterization of molecular events associated with patho-physiological conditions.Here, we review the new leads emerging from the application of comparative proteomics to the actions of thyroid hormones, and we overview the technologies that can improve the resolution of proteins differing in hydrophobicity, intracellular location, complex formation, and membrane binding.

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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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Thyroid hormones differentially modulate enolase isozymes during rat skeletal and cardiac muscle development

Cited by 19 publications

References 46 publications

Studies of Complex Biological Systems with Applications to Molecular Medicine: The Need to Integrate Transcriptomic and Proteomic Approaches

Studies of Complex Biological Systems with Applications to Molecular Medicine: The Need to Integrate Transcriptomic and Proteomic Approaches

Metabolic Action of Thyroid Hormones: Insights from Functional and Proteomic Studies

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

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