C2C12

14,000,000 Leading Edge Experts on the ideXlab platform

Scan Science and Technology

Contact Leading Edge Experts & Companies

Scan Science and Technology

Contact Leading Edge Experts & Companies

The Experts below are selected from a list of 23784 Experts worldwide ranked by ideXlab platform

Roland Baron - One of the best experts on this subject based on the ideXlab platform.

  • activation of mitogen activated protein kinase cascades is involved in regulation of bone morphogenetic protein 2 induced osteoblast differentiation in pluripotent C2C12 cells
    Bone, 2001
    Co-Authors: Sylvie Gallea, Francois Lallemand, Azeddine Atfi, Georges Rawadi, Valerie Ramez, S Spinellajaegle, Shinji Kawai, Chi Faucheu, L Huet, Roland Baron
    Abstract:

    Bone morphogenetic protein (BMP)-2, a member of the transforming growth factor-β (TGF-β) superfamily, is able to induce osteoblastic differentiation of C2C12 cells. Both Smad and mitogen-activated protein kinase (MAPK) pathways are essential components of the TGF-β superfamily signaling machinery. Although Smads have been demonstrated to participate in the BMP-2-induced osteoblastic differentiation of C2C12 cells, the role of MAPK has not been addressed. This report shows that BMP-2 activates ERK and p38, but not JNK, in C2C12 cells. Pretreatment of cells with the p38 inhibitor, SB203580, dramatically reduced BMP-2-induced expression of the osteoblast markers alkaline phosphatase (ALP) and osteocalcin (OC). Nevertheless, overexpression of MKK3, a protein kinase that phosphorylates and activates p38, failed to induce ALP or OC expression in the absence of BMP-2, indicating that p38 activation is necessary but not sufficient for the acquisition of the osteoblast phenotype by these cells. Although ALP induction was increased slightly in the presence of PD-98059, a selective inhibitor of the ERK cascade, this compound significantly inhibited both steady-state and BMP-2-induced OC RNA levels. Our results indicate that p38 and ERK cascades play a crucial role in the osteoblast differentiation of C2C12 cells mediated by BMP-2.

Mario Petrini - One of the best experts on this subject based on the ideXlab platform.

  • investigation of interactions between poly l lysine coated boron nitride nanotubes and C2C12 cells up take cytocompatibility and differentiation
    International Journal of Nanomedicine, 2010
    Co-Authors: Gianni Ciofani, Leonardo Ricotti, Serena Danti, Stefania Moscato, Claudia Nesti, Delfo Dalessandro, Dinuccio Dinucci, Federica Chiellini, A Pietrabissa, Mario Petrini
    Abstract:

    Boron nitride nanotubes (BNNTs) have generated considerable interest within the scientific community by virtue of their unique physical properties, which can be exploited in the biomedical field. In the present in vitro study, we investigated the interactions of poly-l-lysine-coated BNNTs with C2C12 cells, as a model of muscle cells, in terms of cytocompatibility and BNNT internalization. The latter was performed using both confocal and transmission electron microscopy. Finally, we investigated myoblast differentiation in the presence of BNNTs, evaluating the protein synthesis of differentiating cells, myotube formation, and expression of some constitutive myoblastic markers, such as MyoD and Cx43, by reverse transcription – polymerase chain reaction and Western blot analysis. We demonstrated that BNNTs are highly internalized by C2C12 cells, with neither adversely affecting C2C12 myoblast viability nor significantly interfering with myotube formation.

  • Investigation of interactions between boron nitride nanotubes and C2C12 cells
    2009 9th IEEE Conference on Nanotechnology (IEEE-NANO), 2009
    Co-Authors: Gianni Ciofani, Leonardo Ricotti, Serena Danti, Stefania Moscato, Claudia Nesti, Arianna Menciassi, Mario Petrini
    Abstract:

    Boron nitride nanotubes are structural analogues of carbon nanotubes with alternating B and N atoms, which entirely substitute for C atoms in a graphitic like sheet. In this study, we investigated the interactions of boron nitride nanotubes with C2C12 cells as model of muscle cells. We demonstrated that they do not affect viability of these cells neither interfere with their differentiation, making these vectors suitable as non-invasive nano-transducers. Boron nitride nanotubes; cytocompatibility; C2C12 ceUs; nanomaterials-cell interactions.

Naoya Yamamoto - One of the best experts on this subject based on the ideXlab platform.

  • smad1 and smad5 act downstream of intracellular signalings of bmp 2 that inhibits myogenic differentiation and induces osteoblast differentiation in C2C12 myoblasts
    Biochemical and Biophysical Research Communications, 1997
    Co-Authors: Takenobu Katagiri, Naoya Yamamoto, Shuichi Akiyama, Mana Namiki, Takahide Kurokawa, Tatsuo Suda
    Abstract:

    Bone morphogenetic protein-2 (BMP-2) inhibits terminal differentiation of C2C12 myoblasts and converts them into osteoblast lineage cells (Katagiri, T., Yamaguchi, A., Komaki, M., Abe, E., Takahashi, N., Ikeda, T., Rosen, V., Wozney, J. M., Fujisawa-Sehara, A., and Suda T. (1994)J. Cell Biol.127, 1755–1766). In the present study, we examined the possible involvement of Smad proteins, vertebrate homologues ofDrosophilaMothers against decapentaplegic, in the BMP effects on the differentiation of C2C12 myoblasts. C2C12 cells expressed Smad1, Smad2, Smad4, and Smad5 mRNAs, and expression levels were not altered by treatment with BMP-2 or TGF-β1. When Smads were transiently transfected into C2C12 cells, both Smad1 and Smad5 induced alkaline phosphatase (ALP) activity and decreased the activity of myogenin promoter/chloramphenicol acetyltransferase (myogenin-CAT) without BMP-2. When C-terminal-truncated Smad1 and Smad5 were transfected into constitutively active BMP receptor type IB (BMPR-IB)-expressing C2C12 cells, BMP signals were blocked, resulting in an increase in myogenin-CAT activity. On the other hand, Smad1 and Smad5 decreased myogenin-CAT activity but did not induce ALP activity in MyoD-transfected NIH3T3 fibroblasts. These results suggest that both Smad1 and Smad5 are involved in the intracellular BMP signals which inhibit myogenic differentiation and induce osteoblast differentiation in C2C12 cells, and that the conversion of the two differentiation pathways is regulated independently at a transcriptional level.

Sylvie Gallea - One of the best experts on this subject based on the ideXlab platform.

  • activation of mitogen activated protein kinase cascades is involved in regulation of bone morphogenetic protein 2 induced osteoblast differentiation in pluripotent C2C12 cells
    Bone, 2001
    Co-Authors: Sylvie Gallea, Francois Lallemand, Azeddine Atfi, Georges Rawadi, Valerie Ramez, S Spinellajaegle, Shinji Kawai, Chi Faucheu, L Huet, Roland Baron
    Abstract:

    Bone morphogenetic protein (BMP)-2, a member of the transforming growth factor-β (TGF-β) superfamily, is able to induce osteoblastic differentiation of C2C12 cells. Both Smad and mitogen-activated protein kinase (MAPK) pathways are essential components of the TGF-β superfamily signaling machinery. Although Smads have been demonstrated to participate in the BMP-2-induced osteoblastic differentiation of C2C12 cells, the role of MAPK has not been addressed. This report shows that BMP-2 activates ERK and p38, but not JNK, in C2C12 cells. Pretreatment of cells with the p38 inhibitor, SB203580, dramatically reduced BMP-2-induced expression of the osteoblast markers alkaline phosphatase (ALP) and osteocalcin (OC). Nevertheless, overexpression of MKK3, a protein kinase that phosphorylates and activates p38, failed to induce ALP or OC expression in the absence of BMP-2, indicating that p38 activation is necessary but not sufficient for the acquisition of the osteoblast phenotype by these cells. Although ALP induction was increased slightly in the presence of PD-98059, a selective inhibitor of the ERK cascade, this compound significantly inhibited both steady-state and BMP-2-induced OC RNA levels. Our results indicate that p38 and ERK cascades play a crucial role in the osteoblast differentiation of C2C12 cells mediated by BMP-2.

Takenobu Katagiri - One of the best experts on this subject based on the ideXlab platform.

  • DRAGON, a GPI-anchored membrane protein, inhibits BMP signaling in C2C12 myoblasts
    Genes to Cells, 2009
    Co-Authors: Kazuhiro Kanomata, Shoichiro Kokabu, Junya Nojima, Toru Fukuda, Takenobu Katagiri
    Abstract:

    Bone morphogenetic proteins (BMPs) induce osteoblastic differentiation of myoblasts via binding to cell surface receptors. Repulsive guidance molecules (RGMs) have been identified as BMP co-receptors. We report here that DRAGON/RGMb, a member of the RGM family, suppressed BMP signaling in C2C12 myoblasts via a novel mechanism. All RGMs were expressed in C2C12 cells that were differentiated into myocytes and osteoblastic cells, but RGMc was not detected in immature cells. In C2C12 cells, only DRAGON suppressed ALP and Id1 promoter activities induced by BMP-4 or by constitutively activated BMP type I receptors. This inhibition by DRAGON was dependent on the secretory form of the von Willbrand factor type D domain. DRAGON even suppressed BMP signaling induced by constitutively activated Smad1. Over-expression of neogenin did not alter the inhibitory capacity of DRAGON. Taken together, these findings indicate that DRAGON may be an inhibitor of BMP signaling in C2C12 myoblasts. We also suggest that a novel molecule(s) expressed on the cell membrane may mediate the signal transduction of DRAGON in order to suppress BMP signaling in C2C12 myoblasts.

  • cross talk between wnt and bone morphogenetic protein 2 bmp 2 signaling in differentiation pathway of C2C12 myoblasts
    Journal of Biological Chemistry, 2005
    Co-Authors: Aiko Nakashima, Takenobu Katagiri, Masato Tamura
    Abstract:

    Abstract Loss of function of the Wnt co-receptor, lipoprotein receptor-related protein 5, decreases bone formation, and a point mutation in this gene results in high bone mass, indicating the importance of this signaling pathway in bone formation. However, the exact mechanism is currently unknown. We examined a potential role for Wnt signaling and functional cross-talk of bone morphogenetic protein 2 (BMP-2) in osteoblast differentiation. To assess the contribution of Wnt, we generated C2C12 cells over-expressing Wnt3a or Wnt5a and treated these with BMP-2. We showed that expression of matrix extracellular phosphoglycoprotein was induced by BMP-2 in Wnt3a over-expressing C2C12 cells but not in Wnt5a over-expressing C2C12 cells. Over-expression of Wnt3a blocked BMP-2-induced inhibition of myotube formation in C2C12 cells when switched to low mitogen medium. In these cultures, expression of inhibitor of DNA binding/differentiation (Id) 1, a helix-loop-helix protein induced by BMP-2, decreased in stable Wnt3a- but not in Wnt5a-expressing cells. This suppression is mediated by a GC-rich region of the BMP-2-responsive element of the Id1 gene promoter, and interaction between Smad1/4 and β-catenin is crucial for Wnt-mediated suppression of the BMP-2 response in C2C12 cells. Over-expression of the inhibitor of canonical Wnt signaling, Dickkopf, inhibits this suppression. In contrast, BMP-2 or Smad1/4 up-regulated Wnt3a or activated β-catenin-induced lymphoid-enhancing factor 1/T cell factor-dependent transcriptional activity. These findings identify functional cross-talk of Id1 expression between Wnt and BMP signaling and demonstrate a novel mechanism for Wnt regulation of the BMP-2 response, linking Id1 expression to Wnt/β-catenin signaling.

  • smad1 and smad5 act downstream of intracellular signalings of bmp 2 that inhibits myogenic differentiation and induces osteoblast differentiation in C2C12 myoblasts
    Biochemical and Biophysical Research Communications, 1997
    Co-Authors: Takenobu Katagiri, Naoya Yamamoto, Shuichi Akiyama, Mana Namiki, Takahide Kurokawa, Tatsuo Suda
    Abstract:

    Bone morphogenetic protein-2 (BMP-2) inhibits terminal differentiation of C2C12 myoblasts and converts them into osteoblast lineage cells (Katagiri, T., Yamaguchi, A., Komaki, M., Abe, E., Takahashi, N., Ikeda, T., Rosen, V., Wozney, J. M., Fujisawa-Sehara, A., and Suda T. (1994)J. Cell Biol.127, 1755–1766). In the present study, we examined the possible involvement of Smad proteins, vertebrate homologues ofDrosophilaMothers against decapentaplegic, in the BMP effects on the differentiation of C2C12 myoblasts. C2C12 cells expressed Smad1, Smad2, Smad4, and Smad5 mRNAs, and expression levels were not altered by treatment with BMP-2 or TGF-β1. When Smads were transiently transfected into C2C12 cells, both Smad1 and Smad5 induced alkaline phosphatase (ALP) activity and decreased the activity of myogenin promoter/chloramphenicol acetyltransferase (myogenin-CAT) without BMP-2. When C-terminal-truncated Smad1 and Smad5 were transfected into constitutively active BMP receptor type IB (BMPR-IB)-expressing C2C12 cells, BMP signals were blocked, resulting in an increase in myogenin-CAT activity. On the other hand, Smad1 and Smad5 decreased myogenin-CAT activity but did not induce ALP activity in MyoD-transfected NIH3T3 fibroblasts. These results suggest that both Smad1 and Smad5 are involved in the intracellular BMP signals which inhibit myogenic differentiation and induce osteoblast differentiation in C2C12 cells, and that the conversion of the two differentiation pathways is regulated independently at a transcriptional level.