Modulation of embryonic and muscle-specific enolase gene products in the developing mouse hindlimb

Lucas, Marguerite; Goblet, C.; Keller, Andreas; Lamandé, Noël; Gros, François; Whalen, Robert G.; Lazar, Monique

doi:10.1111/j.1432-0436.1992.tb00674.x

Cited by 26 publications

(33 citation statements)

References 29 publications

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“…We and others have observed a large increase in the level of p-enolase gene products during the fetal stage of muscle formation Keller et al, 1992;Lucas et al, 1992). In the developing hindlimb, the accumulation of p-enolase subunit appears to be closely correlated to the level of the corresponding mRNA .…”

Section: Introductionmentioning

confidence: 85%

Transcriptional up‐regulation of the mouse gene for the muscle‐specific subunit of enolase during terminal differentiation of myogenic cells

Lamandé

Brosset

Lucas

et al. 1995

Molecular Reproduction Devel

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The glycolytic enzyme enolase (EC 4.2.1.11) exists as dimers formed from three structurally related subunits alpha, beta, and gamma, encoded by separate genes. The gene encoding the beta-subunit is expressed only in striated muscles. We have previously shown that the beta-enolase gene belongs to a small subset of muscle-specific genes showing transcriptional activity in cultured myoblasts, prior to withdrawal from the cell cycle. An increase in the level of beta-enolase mRNA occurs during terminal differentiation of myoblasts. To investigate the mechanisms underlying this increase, we have simultaneously estimated, under steady state conditions, the rate of synthesis and the stability of beta-enolase mRNA in proliferating C2.7 myoblasts as well as in differentiating myotubes. The method used is based on the isolation of newly synthesized RNA from the total RNA pool, following pulse-labeling of intact cells in the presence of 4-thiouridine. The results described here demonstrate a coordinate increase in newly synthesized and total beta-enolase mRNA, while the mRNA half-life, about 4 hr, remains unchanged in the course of terminal differentiation. The expression of the gene for insulin-like growth factor-II (IGF-II), a major positive regulator of myogenesis, was analyzed using the same approach. It is concluded that the up-regulation of beta-enolase as well as IGF-II gene expression in differentiating muscle cells reflects an increased rate of entry of newly synthesized mRNAs into the general pool of transcripts without changes in their respective half-lives.

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Section: Introductionmentioning

confidence: 85%

Transcriptional up‐regulation of the mouse gene for the muscle‐specific subunit of enolase during terminal differentiation of myogenic cells

Lamandé

Brosset

Lucas

et al. 1995

Molecular Reproduction Devel

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“…For Western blot studies, the anti-MCK serum was diluted 1\250 and the anti-α and -γ-enolase sera were diluted respectively 1\5000 and 1\1000. The anti-β-enolase serum was affinity-purified and used at the dilution 1\300 [10]. Peroxidasecoupled secondary antibody was anti-goat IgG in the case of β-enolase, anti-rabbit IgG in the case of α-and γ-enolase and antichicken IgG in the case of MCK (BIOSYS, Compie' gne, France).…”

Section: Immunological Reagentsmentioning

confidence: 99%

“…In the mouse embryo, β-enolase transcripts are detected in cardiac tube and newly formed myotomes. The gene is further up-regulated at various stages of muscle development, and appears to be under innervational and hormonal control [9][10][11]. At the adult stage, β-enolase transcript and subunit accumulate preferentially in fasttwitch fibres of hindlimb muscles, where the ββ isoenzyme accounts for more than 90 % of total enolase activity [9,[11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins

Меркулова

Lucas

Jabet

et al. 1997

Biochemical Journal

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The glycolytic enzyme enolase (EC 4.2.1.11) is active as dimers formed from three subunits encoded by different genes. The embryonic αα isoform remains distributed in many adult cell types, whereas a transition towards ββ and γγ isoforms occurs in striated muscle cells and neurons respectively. It is not understood why enolase exhibits tissue-specific isoforms with very close functional properties. We approached this problem by the purification of native ββ-enolase from mouse hindlimb muscles and by raising specific antibodies of high titre against this protein. These reagents have been useful in revealing a heterogeneity of the β-enolase subunit that changes with in i o and in itro maturation. A basic carboxypeptidase appears to be involved in generating an acidic β-enolase variant, and may regulate plasminogen binding by this subunit. We show for the

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“…Enolase genes from a wide variety of eucaryotic cells exist as a gene family whose members encode isozymes that are developmentally regulated (28,33,48). Three isozymes that display tissue-specific expression are found in mammalian cells (28,43,44).…”

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confidence: 99%

Genetic organization and mRNA expression of enolase genes of Candida albicans

Postlethwait

Sundstrom

1995

J Bacteriol

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In previous work, we cloned a Candida albicans cDNA for the glycolytic enzyme enolase and found a single, abundant enolase transcript on Northern (RNA) blots and a single protein on immunoblots, using antiserum raised against a recombinant enolase fusion protein. Because C. albicans enolase is abundantly produced during infection and elicits strong host immune responses, the mechanisms regulating enolase production are important for understanding the growth of C. albicans in vivo. To obtain more information on enolase gene expression by C. albicans, we used the enolase cDNA clone to investigate the genetic organization of enolase genes and the steady-state levels of enolase mRNA under several growth conditions. Gene disruption techniques in combination with Southern blot analyses of genomic DNA showed the presence of two enolase gene loci that could be distinguished by the locations of ClaI and MnlI sites in their 3 flanking regions. Enolase steady-state mRNA levels were greatest during the middle phase of the logarithmic growth curve and were low during stationary phase. Minimal differences in enolase mRNA levels between yeast cells and hyphae were found. Propagation of C. albicans in glucose did not cause increased enolase mRNA levels compared with growth in a nonfermentable carbon source (pyruvate). It was concluded that two gene loci exist for C. albicans enolase and that enolase mRNA is constitutively produced at high levels during active metabolism.

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Modulation of embryonic and muscle-specific enolase gene products in the developing mouse hindlimb

Cited by 26 publications

References 29 publications

Transcriptional up‐regulation of the mouse gene for the muscle‐specific subunit of enolase during terminal differentiation of myogenic cells

Transcriptional up‐regulation of the mouse gene for the muscle‐specific subunit of enolase during terminal differentiation of myogenic cells

Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins

Genetic organization and mRNA expression of enolase genes of Candida albicans

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