scholarly journals 25-hydroxyvitamin D upregulates L6 muscle cell differentiation induced by mononuclear cells via the Notch signaling pathway

2021 ◽  
Author(s):  
Carla Domingues-Faria ◽  
Stéphanie Rougé ◽  
Véronique Patrac ◽  
Jérôme Salles ◽  
Stéphane Walrand ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Mrna Expression ◽  
Muscle Cell ◽  
Immune Cells ◽  
Mononuclear Cells ◽  
Notch Pathway ◽  
Muscle Differentiation ◽  
Notch Signaling Pathway ◽  
Muscle Cell Differentiation

Abstract During muscle regeneration, myoblasts engage in cross-talk with immune cells to achieve optimal proliferation and differentiation. In this process, cytokines secreted by immune cells are described to modulate the kinetic of muscle differentiation. Taking into account that immune and muscle cells are both targets of vitamin D, we investigated in vitro the impact of 25-hydroxyvitamin D (25(OH)D) on the transcriptional response of muscle cells in presence of mononuclear cells. To address this objective, an in vitro model of co-culture using L6 myogenic cell line and peripheral blood mononuclear cell (PBMC) isolated from rat was used and compared to L6 cultured alone. Cells were treated with 25(OH)D (125 nM) during the 6 days of differentiation. Gene expression of 25(OH)D metabolism actors, muscle differentiation and metabolism markers, and of Notch signaling pathway effectors were studied in L6 cells by qPCR. In mono-cultured L6 cells, a 25(OH)D treatment induced a 3-fold increase (p < 0.05) in VDR mRNA expression at 24 h while no change in mRNA expression of the muscle differentiation markers i.e. Myog, Myh2 and Des was observed. In the presence of PBMCs, the mRNA expression of these markers was enhanced (27.5 times for myogenin, p < 0.05) resulting in an overexpression of the Notch pathway effectors (Dll: 6.8-fold and Hes1: x3.8-fold, p < 0.05). The 25(OH)D counteracted these effects of the PBMCs on L6 gene expression with the exception of the interleukin 6 transcript and protein. In the present study, our in vitro approach demonstrates the importance of immune cells in stimulating muscle cell differentiation. Taken as a whole, the data show that 25(OH)D attenuates in vitro the Notch pathway-dependent effects of immune cells on muscle cell differentiation and energy metabolism.

scholarly journals USP19 deubiquitinating enzyme inhibits muscle cell differentiation by suppressing unfolded-protein response signaling

2015 ◽  
Vol 26 (5) ◽  
pp. 913-923 ◽  
Author(s):  
Benjamin Wiles ◽  
Miao Miao ◽  
Erin Coyne ◽  
Louise Larose ◽  
Andrey V. Cybulsky ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Unfolded Protein Response ◽  
Muscle Cell ◽  
Deubiquitinating Enzyme ◽  
Muscle Cell Differentiation ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

USP19 deubiquitinating enzyme has two isoforms, cytoplasmic and endoplasmic reticulum (ER) localized. The ER-localized isoform specifically suppresses muscle cell differentiation in vitro and appears to do so by inhibiting the unfolded-protein response that occurs during such differentiation. In vivo, loss of USP19 promotes muscle regeneration following injury.

scholarly journals Smad7 Promotes and Enhances Skeletal Muscle Differentiation

2006 ◽  
Vol 26 (16) ◽  
pp. 6248-6260 ◽  
Author(s):  
Helen D. Kollias ◽  
Robert L. S. Perry ◽  
Tetsuaki Miyake ◽  
Arif Aziz ◽  
John C. McDermott
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Muscle Cell ◽  
Muscle Differentiation ◽  
Skeletal Muscle Cell ◽  
Proximal Promoter ◽  
Cytokine Signaling ◽  
Skeletal Muscle Differentiation ◽  
Muscle Cell Differentiation ◽  
Tgf Β1

ABSTRACT Transforming growth factor β1 (TGF-β1) and myostatin signaling, mediated by the same Smad downstream effectors, potently repress skeletal muscle cell differentiation. Smad7 inhibits these cytokine signaling pathways. The role of Smad7 during skeletal muscle cell differentiation was assessed. In these studies, we document that increased expression of Smad7 abrogates myostatin- but not TGF-β1-mediated repression of myogenesis. Further, constitutive expression of exogenous Smad7 potently enhanced skeletal muscle differentiation and cellular hypertrophy. Conversely, targeting of endogenous Smad7 by small interfering RNA inhibited C2C12 muscle cell differentiation, indicating an essential role for Smad7 during myogenesis. Congruent with a role for Smad7 in myogenesis, we observed that the muscle regulatory factor (MyoD) binds to and transactivates the Smad7 proximal promoter region. Finally, we document that Smad7 directly interacts with MyoD and enhances MyoD transcriptional activity. Thus, Smad7 cooperates with MyoD, creating a positive loop to induce Smad7 expression and to promote MyoD driven myogenesis. Taken together, these data implicate Smad7 as a fundamental regulator of differentiation in skeletal muscle cells.

scholarly journals Smooth Muscle Cell Differentiation In Vitro

2011 ◽  
Vol 31 (7) ◽  
pp. 1485-1494 ◽  
Author(s):  
Changqing Xie ◽  
Raquel P. Ritchie ◽  
Huarong Huang ◽  
Jifeng Zhang ◽  
Y. Eugene Chen
Keyword(s):  
Smooth Muscle ◽  
Cell Differentiation ◽  
Smooth Muscle Cell ◽  
Muscle Cell ◽  
Muscle Cell Differentiation ◽  
Smooth Muscle Cell Differentiation

Regulation of the muscle-specific expression and function of an ascidian T-box gene, As-T2

Development ◽  
2001 ◽  
Vol 128 (19) ◽  
pp. 3717-3728
Author(s):  
Yasuo Mitani ◽  
Hiroki Takahashi ◽  
Nori Satoh
Keyword(s):  
Cell Differentiation ◽  
Muscle Cell ◽  
Muscle Differentiation ◽  
Precursor Cells ◽  
Paraxial Mesoderm ◽  
Specific Expression ◽  
Binding Motifs ◽  
T Box ◽  
Muscle Cell Differentiation ◽  
Endodermal Cells

The Tbx6 T-box genes are expressed in somite precursor cells of vertebrate embryos and are essential for the differentiation of paraxial mesoderm. However, it is unclear how spatial regulation of the gene expression is controlled and how the genes function to promote muscle differentiation. The Tbx6-related gene As-T2 of the ascidian Halocynthia roretzi is first expressed very transiently in endodermal cells around the 32-∼44-cell stage, is then expressed distinctly and continuously in muscle precursor cells, and later in epidermal cells situated in the distal tip region of the elongating tail. We now show that inhibition of As-T2-mediated transcriptional activation by microinjection of As-T2/EnR into one-cell embryos resulted in suppression of the expression of the muscle-specific actin gene (HrMA4) and myosin heavy chain gene (HrMHC), but the injection did not affect the differentiation of endodermal cells or tail tip cells, suggesting that the primary function of As-T2 is associated with muscle cell differentiation. The 5′ flanking region of As-T2 contains two promoter modules that regulate its specific expression: a distal module that responsible for its specific expression in the tail, and a proximal module required for its muscle-specific expression. Around the proximal module, there are two putative T protein-binding motifs (TTCACACTT). Co-injection of an As-T2/lacZ construct with or without the T-binding motifs together with As-T2 mRNA revealed that these motifs are essential for autoregulatory activation of the gene itself. In addition, we found that the minimal promoter regions of HrMA4 and HrMHC contain T-binding motifs. Co-injection of HrMA4/lacZ or HrMHC/lacZ containing the T-binding motifs along with As-T2 mRNA revealed that As-T2 protein binds to these motifs to upregulate the gene activity. Taking into account the recent finding of maternal molecules for muscle differentiation, we propose a model for a genetic cascade that includes As-T2 as a regulator of muscle cell differentiation in the ascidian embryo.

scholarly journals SRF is a nonhistone methylation target of KDM2B and SET7 in the regulation of skeletal muscle differentiation

2021 ◽  
Vol 53 (2) ◽  
pp. 250-263
Author(s):  
Duk-Hwa Kwon ◽  
Joo-Young Kang ◽  
Hosouk Joung ◽  
Ji-Young Kim ◽  
Anna Jeong ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Cell Differentiation ◽  
Muscle Cell ◽  
Transcriptional Activation ◽  
Serum Response Factor ◽  
Muscle Differentiation ◽  
Skeletal Muscle Differentiation ◽  
Muscle Cell Differentiation ◽  
Lysine Residues ◽  
Serum Response

AbstractThe demethylation of histone lysine residues, one of the most important modifications in transcriptional regulation, is associated with various physiological states. KDM2B is a demethylase of histones H3K4, H3K36, and H3K79 and is associated with the repression of transcription. Here, we present a novel mechanism by which KDM2B demethylates serum response factor (SRF) K165 to negatively regulate muscle differentiation, which is counteracted by the histone methyltransferase SET7. We show that KDM2B inhibited skeletal muscle differentiation by inhibiting the transcription of SRF-dependent genes. Both KDM2B and SET7 regulated the balance of SRF K165 methylation. SRF K165 methylation was required for the transcriptional activation of SRF and for the promoter occupancy of SRF-dependent genes. SET7 inhibitors blocked muscle cell differentiation. Taken together, these data indicate that SRF is a nonhistone target of KDM2B and that the methylation balance of SRF as maintained by KDM2B and SET7 plays an important role in muscle cell differentiation.

scholarly journals A novel isoform of MAP4 organises the paraxial microtubule array required for muscle cell differentiation

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Binyam Mogessie ◽  
Daniel Roth ◽  
Zainab Rahil ◽  
Anne Straube
Keyword(s):  
Cell Differentiation ◽  
Cell Fusion ◽  
Muscle Cell ◽  
Cell Elongation ◽  
Myogenic Differentiation ◽  
Muscle Cells ◽  
Microtubule Array ◽  
Muscle Cell Differentiation ◽  
Microtubule Transport

The microtubule cytoskeleton is critical for muscle cell differentiation and undergoes reorganisation into an array of paraxial microtubules, which serves as template for contractile sarcomere formation. In this study, we identify a previously uncharacterised isoform of microtubule-associated protein MAP4, oMAP4, as a microtubule organising factor that is crucial for myogenesis. We show that oMAP4 is expressed upon muscle cell differentiation and is the only MAP4 isoform essential for normal progression of the myogenic differentiation programme. Depletion of oMAP4 impairs cell elongation and cell–cell fusion. Most notably, oMAP4 is required for paraxial microtubule organisation in muscle cells and prevents dynein- and kinesin-driven microtubule–microtubule sliding. Purified oMAP4 aligns dynamic microtubules into antiparallel bundles that withstand motor forces in vitro. We propose a model in which the cooperation of dynein-mediated microtubule transport and oMAP4-mediated zippering of microtubules drives formation of a paraxial microtubule array that provides critical support for the polarisation and elongation of myotubes.

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