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C2C12

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

Roland Baron – 1st expert 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 – 2nd expert 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 – 3rd expert 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.