scholarly journals The Dentin Sialoprotein (DSP) Domain Regulates Dental Mesenchymal Cell Differentiation through a Novel Surface Receptor

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Chunyan Wan ◽  
Guohua Yuan ◽  
Daoshu Luo ◽  
Lu Zhang ◽  
Heng Lin ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Mesenchymal Cell ◽  
Surface Receptor ◽  
Dentin Sialoprotein

scholarly journals Dentin sialoprotein facilitates dental mesenchymal cell differentiation and dentin formation

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Wentong Li ◽  
Lei Chen ◽  
Zhuo Chen ◽  
Lian Wu ◽  
Junsheng Feng ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Mesenchymal Cell ◽  
Dentin Sialoprotein ◽  
Dentin Formation

Type I collagen induces mesenchymal cell differentiation into myofibroblasts through YAP-induced TGF-β1 activation

Biochimie ◽  
2018 ◽  
Vol 150 ◽  
pp. 110-130 ◽  
Author(s):  
Xiaoling Liu ◽  
Xinyu Long ◽  
Weiwei Liu ◽  
Yeli Zhao ◽  
Toshihiko Hayashi ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Type I Collagen ◽  
Mesenchymal Cell ◽  
Type I ◽  
Tgf Β1

scholarly journals Mesenchymal cell differentiation and diseases: involvement of translin/TRAX complexes and associated proteins

2018 ◽  
Vol 1421 (1) ◽  
pp. 37-45 ◽  
Author(s):  
Masataka Kasai ◽  
Reiko Ishida ◽  
Kazuhiko Nakahara ◽  
Ko Okumura ◽  
Katsunori Aoki
Keyword(s):  
Cell Differentiation ◽  
Mesenchymal Cell ◽  
Associated Proteins

scholarly journals Superoxide Mediates Shock Wave Induction of ERK-dependent Osteogenic Transcription Factor (CBFA1) and Mesenchymal Cell Differentiation toward Osteoprogenitors

2002 ◽  
Vol 277 (13) ◽  
pp. 10931-10937 ◽  
Author(s):  
Feng-Sheng Wang ◽  
Ching-Jen Wang ◽  
Shyr-Ming Sheen-Chen ◽  
Yur-Ren Kuo ◽  
Rong-Fu Chen ◽  
...  
Keyword(s):  
Shock Wave ◽  
Transcription Factor ◽  
Cell Differentiation ◽  
Mesenchymal Cell

Ras modulates commitment and maturation of 10T½ fibroblasts to adipocytes

1992 ◽  
Vol 70 (10-11) ◽  
pp. 1249-1257 ◽  
Author(s):  
Ying Lu ◽  
Steve Anderson ◽  
Michael J. Corbley ◽  
Yu-Chun Zhou ◽  
Hugh Pross ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Human Cancer ◽  
Low Frequency ◽  
Positive Association ◽  
Mesenchymal Cell ◽  
Negative Regulator ◽  
Ras Gene ◽  
Positive Role ◽  
Adipose Conversion ◽  
Differentiating Agent

The positive association of the ras oncogene with human cancer and the recognition that malignancy may, in part, represent the imbalance between cell proliferation and differentiation have generated intense interest in the potential role of ras in cell differentiation. We investigated this possibility utilizing as a model system the differentiation of the mesenchymal cell line C3H 10T½ (10T½) to adipocytes, and a series of transfectants of 10T½ cells in which the level of the ras gene product (p21ras; Ras) can be effectively up- or down-modulated. In agreement with previous reports, we found that 10T½ cultures, propagated in the resting state for several weeks, spontaneously convert to fat cells at a very low frequency. Downmodulation of endogenous p21ras levels, as a consequence of expression of antisense ras, markedly increased the rapidity and frequency of adipose conversion (6- to 10-fold), which was equivalent in magnitude to that effected by the potent differentiating agent 5-azacytidine. Conversely, overexpression of ras completely inhibited cell differentiation. In addition, adipocytes derived from antisense-ras expressing lines were characterized by a decrease in hormone responsiveness, as well as an apparent deficiency in attaining the terminally differentiated state. These findings suggest that Ras may be a negative regulator of the decision-making step of fibroblast differentiation to adipocytes. In addition, Ras may play an essential positive role in the transduction of hormonal signals necessary for full adipocytic maturation during later progression along the differentiation pathway.Key words: ras protooncogene, cell differentiation, signal transduction, insulin, adipocytes.

A Mechanochemical Microarray for Studying Combinatorial Effects on Embryonic Mesenchymal Cell Differentiation

2016 ◽  
Vol 4 (0) ◽  
pp. 1 ◽  
Author(s):  
Basma Hashmi ◽  
Keekyoung Kim ◽  
Jalil Zerdani ◽  
Tadanori Mammoto ◽  
Juani Feliz ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Mesenchymal Cell

scholarly journals Gene expression and protein secretion during human mesenchymal cell differentiation into adipogenic cells

2014 ◽  
Vol 15 (1) ◽  
Author(s):  
Paola Romina Amable ◽  
Marcus Vinicius Telles Teixeira ◽  
Rosana Bizon Vieira Carias ◽  
José Mauro Granjeiro ◽  
Radovan Borojevic
Keyword(s):  
Gene Expression ◽  
Cell Differentiation ◽  
Protein Secretion ◽  
Mesenchymal Cell

scholarly journals A Cdo–Bnip-2–Cdc42 signaling pathway regulates p38α/β MAPK activity and myogenic differentiation

2008 ◽  
Vol 182 (3) ◽  
pp. 497-507 ◽  
Author(s):  
Jong-Sun Kang ◽  
Gyu-Un Bae ◽  
Min-Jeong Yi ◽  
Youn-Joo Yang ◽  
Ji-Eun Oh ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Cell Surface ◽  
Mapk Pathway ◽  
Myogenic Differentiation ◽  
Negative Regulator ◽  
Mitogen Activated Protein Kinase ◽  
Cell Surface Receptor ◽  
Myoblast Differentiation ◽  
Loss Of Function ◽  
Surface Receptor

The p38α/β mitogen-activated protein kinase (MAPK) pathway promotes skeletal myogenesis, but the mechanisms by which it is activated during this process are unclear. During myoblast differentiation, the promyogenic cell surface receptor Cdo binds to the p38α/β pathway scaffold protein JLP and, via JLP, p38α/β itself. We report that Cdo also interacts with Bnip-2, a protein that binds the small guanosine triphosphatase (GTPase) Cdc42 and a negative regulator of Cdc42, Cdc42 GTPase-activating protein (GAP). Moreover, Bnip-2 and JLP are brought together through mutual interaction with Cdo. Gain- and loss-of-function experiments with myoblasts indicate that the Cdo–Bnip-2 interaction stimulates Cdc42 activity, which in turn promotes p38α/β activity and cell differentiation. These results reveal a previously unknown linkage between a cell surface receptor and downstream modulation of Cdc42 activity. Furthermore, interaction with multiple scaffold-type proteins is a distinctive mode of cell surface receptor signaling and provides one mechanism for specificity of p38α/β activation during cell differentiation.

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