Retinoic acid receptors and muscle b-HLH proteins: partners in retinoid-induced myogenesis

Froeschle, Anne; Alric, Séverine; Kitzmann, Magali; Carnac, Gilles; Aurade, Frédéric; Rochette‐Egly, Cécile; Bonnieu, Anne

doi:10.1038/sj.onc.1201894

Cited by 40 publications

(32 citation statements)

References 55 publications

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“…It is particularly interesting that these growth factors and RA, which are known to be expressed in the vicinity of condensing mesenchymal cells and limb buds during early developmental stages (54 -57), modulate betaglycan expression. Interestingly, it has been described that RA induces differentiation only in MyoD-expressing muscle cells by the formation of the RA receptor-MyoD complex (58). Other growth factors such as FGF-2, BMP-2, or HGF did not significantly affect the promoter activity.…”

Section: Figmentioning

confidence: 97%

Betaglycan Expression Is Transcriptionally Up-regulated during Skeletal Muscle Differentiation

López‐Casillas¹,

Riquelme²,

Pérez-Kato³

et al. 2003

Journal of Biological Chemistry

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Betaglycan is a membrane-anchored proteoglycan coreceptor that binds transforming growth factor ␤ (TGF-␤) via its core protein and basic fibroblast growth factor through its glycosaminoglycan chains. In this study we evaluated the expression of betaglycan during the C 2 C 12 skeletal muscle differentiation. Betaglycan expression, as determined by Northern and Western blot, was up-regulated during the conversion of myoblasts to myotubes. The mouse betaglycan gene promoter was cloned, and its sequence showed putative binding sites for SP1, Smad3, Smad4, muscle regulatory factor elements such as MyoD and MEF2, and retinoic acid receptor. Transcriptional activity of the mouse betaglycan promoter reporter was also up-regulated in differentiating C 2 C 12 cells. We found that MyoD, but not myogenin, stimulated this transcriptional activity even in the presence of high serum. Betaglycan promoter activity was increased by RA and inhibited by the three isoforms of TGF-␤. On the other hand, basic fibroblast growth factor, BMP-2, and hepatocyte growth factor/scatter factor, which are inhibitors of myogenesis, had little effect. In myotubes, up-regulated betaglycan was also detectable by TGF-␤ affinity labeling and immunofluorescence microscopy studies. The latter indicated that betaglycan was localized both on the cell surface and in the ECM. Forced expression of betaglycan in C 2 C 12 myoblasts increases their responsiveness to TGF-␤2, suggesting that it performs a TGF-␤ presentation function in this cell lineage. These results indicate that betaglycan expression is up-regulated during myogenesis and that MyoD and RA modulate its expression by a mechanism that is independent of myogenin.Skeletal muscle myoblasts are the precursors to skeletal muscle fibers. During development these cells are maintained in a proliferative and undifferentiated state until appropriate signals cause them to undergo conversion into multinucleated myotubes.A network of muscle regulatory factors (MRFs), 1 some of which have been identified and characterized, governs this process. When myogenesis begins, myogenic regulatory genes encoding factors of the MyoD family are activated (myogenin, MRF4, and MRF5). These factors bind to specific DNA consensus sites called E boxes, which function as transcriptional enhancers of muscle differentiation genes (for review see Ref.

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Section: Figmentioning

confidence: 97%

Betaglycan Expression Is Transcriptionally Up-regulated during Skeletal Muscle Differentiation

López‐Casillas¹,

Riquelme²,

Pérez-Kato³

et al. 2003

Journal of Biological Chemistry

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“…Nuclear receptor related 1 activates the human dopamine transporter gene by a novel mechanism independent of its nerve growth factor-induced protein I-B response element-like sites (46). Even more relevant to CAR and the OA synergistic response is the ability of its heterodimerization partner RXR and the nuclear receptor RAR to interact with the bHLH protein myogenic factor 3 and to reciprocally activate nuclear receptor half-sites and E box motifs (CANNTG), by co-activating each others' DNA binding-dependent gene activation (16). Hepatocyte nuclear factor 4␣ has been reported to be critical for maximal activation of CYP3A4 and CYP3A23 by CAR or pregnane X receptor.…”

Section: Discussionmentioning

confidence: 99%

“…It is possible that CAR interacts with other factors in the nucleus that are the target of phosphorylation because direct phosphorylation of CAR has not, as yet, been reported. Indirect mechanisms of gene induction by nuclear receptors, including the retinoic acid receptor (RAR), RXR, and the glucocorticoid receptor, independent of nuclear receptor half-site activation, have been reported previously (16,17) but no such mechanism has been reported for CAR at present.…”

mentioning

confidence: 99%

Novel CAR-mediated Mechanism for Synergistic Activation of Two Distinct Elements within the Human Cytochrome P450 2B6 Gene in HepG2 Cells

Swales

Kakizaki

Yamamoto

et al. 2005

Journal of Biological Chemistry

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The constitutive active receptor (CAR) regulates the induction of the cytochrome P450 2B6 (CYP2B6) gene by phenobarbital-type inducers, such as 1,4 bis[2-(3,5-dichloropyridyloxy)]benzene (TCPOBOP) via the distal phenobarbital-responsive enhancer module (PBREM, at ؊1732/؊1685 bp). Activation of the PBREM by TCPOBOP generated a 10-fold induction of CYP2B6 mRNA in HepG2 cells stably expressing mouse CAR (Ym17). Co-treatment with the protein phosphatase inhibitor okadaic acid (OA) synergistically increased this induction over 100-fold without directly activating CAR or the PBREM. Although OA synergy required the presence of PBREM, deletion assays delineated the OA-responsive activity to a proximal 24-bp (؊256/؊233) sequence (OARE) in the CYP2B6 promoter. CAR did not directly bind to the OARE in electrophoretic mobility shift assays. However, both DNA affinity and chromatin immunoprecipitation assays showed a significant increase in CAR association with the OARE after co-treatment with TCPOBOP and OA, indicating the indirect binding of CAR to the OARE. The two cis-acting elements, the distal PBREM and the proximal OARE, within the chromatin structure are both regulated by CAR in response to TCPOBOP and OA, respectively, to maximally induce the CYP2B6 promoter. This functional interaction between the two sites expands the current understanding of the mechanism of CAR-mediated inducible transcription.

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“…50g of total proteins diluted in 1x Laemmli buffer (100mM Tris-HCl, pH 6.8, 4% SDS, 20% glycerol, 200mM DTT, bromophenol blue) were transferred to nitrocellulose membranes (Schleicher and Schull Bioscience, Dassel, Germany). Western blots were performed as previously described (Froeschle et al, 1998 …”

Section: Western Blotmentioning

confidence: 99%

Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli

Hayot

Rodriguez

Vernus

et al. 2011

Molecular and Cellular Endocrinology

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Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli, Molecular and Cellular Endocrinology (2010), doi:10.1016/j.mce.2010 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Version postprintComment citer ce document : Hayot, M., Rodriguez, J., Vernus, B., Carnac, G., Jean, E., Allen, D., Goret, L., Obert, P., Candau, R., A c c e p t e d M a n u s c r i p t 2 ABSTRACTMyostatin and hypoxia signalling pathways are able to induce skeletal muscle atrophy, but whether a relationship between these two pathways exists is currently unknown. Here, we tested the hypothesis that a potential mechanism for hypoxia effect on skeletal muscle may be through regulation of myostatin. We reported an induction of myostatin expression in muscles of rats exposed to chronic hypoxia. Interestingly, we also demonstrated increased skeletal muscle myostatin protein expression in skeletal muscle of hypoxemic patients with severe Keywords : hypoxic stimulus, myostatin, skeletal muscle atrophy, COPD, myotubes Version postprintComment citer ce document : Hayot, M., Rodriguez, J., Vernus, B., Carnac, G., Jean, E., Allen, D., Goret, L., Obert, P., Candau, R., Bonnieu, A. (2011). Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli.

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Retinoic acid receptors and muscle b-HLH proteins: partners in retinoid-induced myogenesis

Cited by 40 publications

References 55 publications

Betaglycan Expression Is Transcriptionally Up-regulated during Skeletal Muscle Differentiation

Betaglycan Expression Is Transcriptionally Up-regulated during Skeletal Muscle Differentiation

Novel CAR-mediated Mechanism for Synergistic Activation of Two Distinct Elements within the Human Cytochrome P450 2B6 Gene in HepG2 Cells

Myostatin up-regulation is associated with the skeletal muscle response to hypoxic stimuli

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