Ishige sinicola extract stimulates osteoblast proliferation and differentiation via the bone morphogenetic protein 2/runt-related gene 2 signalling pathway

2019 ◽  
Vol 74 (7-8) ◽  
pp. 167-174
Author(s):  
Mihyang Kim ◽  
Jeong Hyeon Kang ◽  
Geun Hye Oh ◽  
Mi Hwa Park
Keyword(s):  
Cell Proliferation ◽  
Bone Formation ◽  
Bone Morphogenetic Protein ◽  
Bone Diseases ◽  
Signalling Pathway ◽  
Bone Morphogenetic Protein 2 ◽  
Dependent Manner ◽  
Alizarin Red ◽  
Alp Activity ◽  
Morphogenetic Protein

Abstract Osteoporosis is one of the most common bone diseases, occurring due to an imbalance between bone formation and bone resorption. The aim of this study was to investigate the effects of Ishige sinicola, a brown alga, on osteoblast differentiation through the activation of the bone morphogenetic protein 2 (BMP-2)/runt-related transcription factor 2 (Runx2) signalling pathway in MC3T3-E1 cells. A cell proliferation assay, alkaline phosphatase (ALP) activity assay, alizarin red staining, and expression analysis of osteoblastic genes were carried out to assess MC3T3-E1 cell proliferation and osteoblastic differentiation. We found that I. sinicola extract (ISE) increased cell proliferation in a dose-dependent manner. Ishige sinicola extract markedly promoted ALP activity and mineralization. Alizarin red S staining demonstrated that ISE treatment tended to increase extracellular matrix calcium accumulation. Moreover, ISE up-regulated the osteoprotegerin/receptor activator of nuclear factor κB ligand ratio. Ishige sinicola extract also increased the protein expression levels of type 1 collagen, ALP, osteocalcin, osterix, BMP-2, and Runx2. Therefore, ISE showed potential in stimulating osteoblastic bone formation, and it might be useful for the prevention and treatment of osteoporosis.

Bone formation promoted by bone morphogenetic protein-2 plasmid-loaded porous silica nanoparticles with the involvement of autophagy

Nanoscale ◽  
2019 ◽  
Vol 11 (45) ◽  
pp. 21953-21963 ◽  
Author(s):  
Xiaowei Xu ◽  
Maolei Sun ◽  
Dandan Wang ◽  
Wenhuan Bu ◽  
Zilin Wang ◽  
...  
Keyword(s):  
Bone Formation ◽  
Osteogenic Differentiation ◽  
Silica Nanoparticles ◽  
Bone Morphogenetic Protein ◽  
Porous Silica ◽  
Bone Morphogenetic Protein 2 ◽  
Calcium Deposition ◽  
Morphogenetic Protein

Bone morphogenetic protein-2 plasmid was encapsulated by polyethylenimine-modified porous silica nanoparticles, which promoted osteogenic differentiation and increased calcium deposition with the involvement of autophagy.

Transient Production of Bone Morphogenetic Protein 2 by Allogeneic Transplanted Transduced Cells Induces Bone Formation

2000 ◽  
Vol 11 (1) ◽  
pp. 205-211 ◽  
Author(s):  
Thomas Engstrand ◽  
Aaron Daluiski ◽  
Matthew E. Bahamonde ◽  
Hakan Melhus ◽  
Karen M. Lyons
Keyword(s):  
Bone Formation ◽  
Bone Morphogenetic Protein ◽  
Bone Morphogenetic Protein 2 ◽  
Morphogenetic Protein

scholarly journals Statin-induced Ras Activation Integrates the Phosphatidylinositol 3-Kinase Signal to Akt and MAPK for Bone Morphogenetic Protein-2 Expression in Osteoblast Differentiation

2006 ◽  
Vol 282 (7) ◽  
pp. 4983-4993 ◽  
Author(s):  
Nandini Ghosh-Choudhury ◽  
Chandi Charan Mandal ◽  
Goutam Ghosh Choudhury
Keyword(s):  
Bone Morphogenetic Protein ◽  
Osteoblast Differentiation ◽  
Dominant Negative ◽  
Bone Morphogenetic Protein 2 ◽  
Regulatory Subunit ◽  
Type I ◽  
Dependent Manner ◽  
Phosphatidylinositol 3 Kinase ◽  
Morphogenetic Protein ◽  
Phosphatidylinositol 3

Lovastatin promotes osteoblast differentiation by increasing bone morphogenetic protein-2 (BMP-2) expression. We demonstrate that lovastatin stimulates tyrosine phosphorylation of the p85 regulatory subunit of phosphatidylinositol 3-kinase (PI3K), leading to an increase in its kinase activity in osteoblast cells. Inhibition of PI3K ameliorated expression of the osteogenic markers alkaline phosphatase, type I collagen, osteopontin, and BMP-2. Expression of dominant-negative PI3K and PTEN, an inhibitor of PI3K signaling, significantly attenuated lovastatin-induced transcription of BMP-2. Akt kinase was also activated in a PI3K-dependent manner. However, our data suggest involvement of an additional signaling pathway. Lovastatin-induced Erk1/2 activity contributed to BMP-2 transcription. Inhibition of PI3K abrogated Erk1/2 activity in response to lovastatin, indicating the presence of a signal relay between them. We provide, as a mechanism of this cross-talk, the first evidence that lovastatin stimulates rapid activation of Ras, which associates with and activates PI3K in the plasma membrane, which in turn regulates Akt and Erk1/2 to induce BMP-2 expression for osteoblast differentiation.

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