scholarly journals Icariin regulates the osteoblast differentiation and cell proliferation of MC3T3‑E1 cells through microRNA‑153 by targeting Runt‑related transcription factor 2

2018 ◽  
Author(s):  
Zengfa Huang ◽  
Cheng Cheng ◽  
Jing Wang ◽  
Xianzhe Liu ◽  
Hui Wei ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Transcription Factor ◽  
Osteoblast Differentiation ◽  
Related Transcription Factor

scholarly journals The ETS Protein MEF Is Regulated by Phosphorylation-Dependent Proteolysis via the Protein-Ubiquitin Ligase SCFSkp2

2006 ◽  
Vol 26 (8) ◽  
pp. 3114-3123 ◽  
Author(s):  
Yan Liu ◽  
Cyrus V. Hedvat ◽  
Shifeng Mao ◽  
Xin-Hua Zhu ◽  
Jinjuan Yao ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Proliferation ◽  
Transcription Factor ◽  
Ubiquitin Ligase ◽  
Nk Cell ◽  
Retinoic Acid Receptor ◽  
Hematopoietic Stem ◽  
C Terminus ◽  
Related Transcription Factor ◽  
Retinoic Acid Receptor Α

ABSTRACT MEF is an ETS-related transcription factor with strong transcriptional activating activity that affects hematopoietic stem cell behavior and is required for normal NK cell and NK T-cell development. The MEF (also known as ELF4) gene is repressed by several leukemia-associated fusion transcription factor proteins (PML-retinoic acid receptor α and AML1-ETO), but it is also activated by retroviral insertion in several cancer models. We have previously shown that cyclin A-dependent phosphorylation of MEF largely restricts its activity to the G1 phase of the cell cycle; we now show that MEF is a short-lived protein whose expression level also peaks during late G1 phase. Mutagenesis studies show that the rapid turnover of MEF in S phase is dependent on the specific phosphorylation of threonine 643 and serine 648 at the C terminus of MEF by cdk2 and on the Skp1/Cul1/F-box (SCF) E3 ubiquitin ligase complex SCFSkp2, which targets MEF for ubiquitination and proteolysis. Overexpression of MEF drives cells through the G1/S transition, thereby promoting cell proliferation. The tight regulation of MEF levels during the cell cycle contributes to its effects on regulating cell cycle entry and cell proliferation.

scholarly journals Effects of PIN on Osteoblast Differentiation and Matrix Mineralization through Runt-Related Transcription Factor

2020 ◽  
Vol 21 (24) ◽  
pp. 9579
Author(s):  
Kyung-Ran Park ◽  
SooHyun Kim ◽  
MyoungLae Cho ◽  
Sang Wook Kang ◽  
Hyung-Mun Yun
Keyword(s):  
Transcription Factor ◽  
Cell Migration ◽  
Protein Level ◽  
Osteoblast Differentiation ◽  
Signaling Molecules ◽  
Dependent Manner ◽  
Alizarin Red ◽  
Matrix Mineralization ◽  
Related Transcription Factor ◽  
Dose Dependent

Styrax Japonica Sieb. et Zucc. has been used as traditional medicine in inflammatory diseases, and isolated compounds have shown pharmacological activities. Pinoresinol glucoside (PIN) belonging to lignins was isolated from the stem bark of S. Japonica. This study aimed to investigate the biological function and mechanisms of PIN on cell migration, osteoblast differentiation, and matrix mineralization. Herein, we investigated the effects of PIN in MC3T3-E1 pre-osteoblasts, which are widely used for studying osteoblast behavior in in vitro cell systems. At concentrations ranging from 0.1 to 100 μM, PIN had no cell toxicity in pre-osteoblasts. Pre-osteoblasts induced osteoblast differentiation, and the treatment of PIN (10 and 30 μM) promoted the cell migration rate in a dose-dependent manner. At concentrations of 10 and 30 μM, PIN elevated early osteoblast differentiation in a dose-dependent manner, as indicated by increases in alkaline phosphatase (ALP) staining and activity. Subsequently, PIN also increased the formation of mineralized nodules in a dose-dependent manner, as indicated by alizarin red S (ARS) staining, demonstrating positive effects of PIN on late osteoblast differentiation. In addition, PIN induced the mRNA level of BMP2, ALP, and osteocalcin (OCN). PIN also upregulated the protein level of BMP2 and increased canonical BMP2 signaling molecules, the phosphorylation of Smad1/5/8, and the protein level of Runt-related transcription factor 2 (RUNX2). Furthermore, PIN activated non-canonical BMP2 signaling molecules, activated MAP kinases, and increased β-catenin signaling. The findings of this study indicate that PIN has biological roles in osteoblast differentiation and matrix mineralization, and suggest that PIN might have anabolic effects in bone diseases such as osteoporosis and periodontitis.

scholarly journals The PERK-EIF2α-ATF4 signaling branch regulates osteoblast differentiation and proliferation by PTH

2019 ◽  
Vol 316 (4) ◽  
pp. E590-E604 ◽  
Author(s):  
Kefan Zhang ◽  
Miaomiao Wang ◽  
Yingjiang Li ◽  
Chunping Li ◽  
Shaidi Tang ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Endoplasmic Reticulum ◽  
Transcription Factor ◽  
Er Stress ◽  
Signaling Pathway ◽  
Osteoblast Differentiation ◽  
Type I ◽  
Matrix Mineralization ◽  
Related Peptide ◽  
Differentiation And Proliferation

Parathyroid hormone (PTH) and its related peptide (PTH-related peptide 1–34) are two of the Food and Drug Administration-approved bone-promoting drugs for age-related osteoporosis. Treatment with PTH stimulates bone formation. However, the molecular mechanisms of PTH-mediated osteoblast differentiation and cell proliferation are still not completely understood. In this study, we showed that PTH induced endoplasmic reticulum (ER) stress in osteoblasts through the PKR-like endoplasmic reticulum kinase (PERK)-eukaryotic initiation factor 2α (EIF2α)-activating transcription factor 4 (ATF4)-signaling pathway. After separately blocking PERK-EIF2α-ATF4 signaling with two different inhibitors [AMG’44 and integrated stress response inhibitor (ISRIB)] or specific small interfering RNA for PERK and ATF4, the following targets were all downregulated: expression of osteoblast differentiation markers [runt-related transcription factor 2 (Runx2), alkaline phosphatase (Alp), type I collagen (Col1a1), and osteocalcin (Ocn)], cell proliferation markers (CyclinE, CyclinD, and CDC2), amino acid import (Glyt1), and metabolism-related genes (Asns). Additionally, Alp-positive staining cells, Alp activity, matrix mineralization, Ocn secretion, and cell proliferation indexes were inhibited. Interestingly, we found that salubrinal enhanced PTH-induced osteoblast differentiation and proliferation by maintenance of phosphorylation of EIF2α. Furthermore, we observed that PTH increased the association between heat shock protein 90 (HSP90) and PERK and maintained PERK protein stabilization in the early stages of PTH-induced ER stress. Treatment of MC3T3-E1 cells with geldanamycin, an HSP90 inhibitor, decreased PERK protein expression and inhibited osteoblast differentiation and cell proliferation upon PTH treatment. Taken together, our data demonstrate that PTH regulates osteoblast differentiation and cell proliferation, partly by activating the HSP90-dependent PERK-EIF2α-ATF4 signaling pathway.

scholarly journals The cancer-related transcription factor Runx2 modulates cell proliferation in human osteosarcoma cell lines

2012 ◽  
Vol 228 (4) ◽  
pp. 714-723 ◽  
Author(s):  
Claudia M.J. Lucero ◽  
Oscar A. Vega ◽  
Mariana M. Osorio ◽  
Julio C. Tapia ◽  
Marcelo Antonelli ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Transcription Factor ◽  
Cell Lines ◽  
Osteosarcoma Cell ◽  
Human Osteosarcoma ◽  
Human Osteosarcoma Cell ◽  
Related Transcription Factor

scholarly journals Collagen Hydrolysate Gly-Pro-Hyp on Osteoblastic Proliferation and Differentiation of MC3T3-E1 Cells

2017 ◽  
Vol 1 (3) ◽  
Author(s):  
Geng Min
Keyword(s):  
Alkaline Phosphatase ◽  
Transcription Factor ◽  
Bone Formation ◽  
Osteoblast Differentiation ◽  
Control Medium ◽  
Collagen Hydrolysate ◽  
Alp Activity ◽  
Proliferation And Differentiation ◽  
Related Transcription Factor ◽  
Set Up

Objectives: Bone formation and bone resorption continuouslyoccur in bone tissue to prevent the accumulation of old bone, thisbeing called bone remodeling. Osteoblasts especially play a crucialrole in bone formation through the differentiation and proliferation.Therefore, in this study, we investigated the effects of collagenhydrolysate Glycine-Prolyl-Hydroxyproline (Gly-Pro-Hyp) onosteoblastic proliferation and differentiation in MC3T3-E1 cells.Methods: Four groups including control, Gly-Pro-Hyp 20 μM,100 μM, 500 μM groups were set up in this study. Cells werecultured with blank control medium or Gly-Pro-Hyp of thedifferent dosages for 24 h. CCK 8 assay was analyzed cellproliferation. Assay of Alkaline phosphatase (ALP)activity wasanalyzed osteoblast differentiation. The expression levels of ALP,Col 1, Runx 2 and Osterix in MC3T3-E1 cells were measured byWestern blot. Results: The results indicated the treatment of Gly-Pro-Hyp promoted the proliferation of MC3T3-E1 cells andimproved ALP activity. In addition, cells treated with Gly-Pro-Hypsignificantly upregulated protein expression of ALP, type 1collagen, runt-related transcription factor 2 and osterix.Conclusion: The results demonstrate that Gly-Pro-Hyp promotedifferentiation inducement and proliferation of MC3T3-E1 cells,therefore may help to elucidate the transcriptional mechanism ofbone formation and possibly lead to the development of bone-forming drugs.

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