Nectandrin A Enhances the BMP-Induced Osteoblastic Differentiation and Mineralization by Activation of p38 MAPK-Smad Signaling Pathway
The Korean Journal of Physiology and Pharmacology
; : 447-453, 2013.
Article
in English
| WPRIM (Western Pacific)
| ID: wpr-727497
Responsible library:
WPRO
ABSTRACT
Osteoblastic activity of nectandrin A was examined in C2C12 cells. Nectandrin A enhances the BMP-induced osteoblastic differentiation and mineralization, manifested by the up-regulation of differentiation markers (alkaline phosphatase and osteogenic genes) and increased calcium contents. In C2C12 cells co-transfected with expression vector encoding Smad4 and Id1-Luc reporter, nectandrin A increased Id1 luciferase activity in a concentration-dependent manner, when compared to that in BMP-2 treated cells, indicating that Smad signaling pathway is associated with nectandrin A-enhanced osteoblastic differentiation in C2C12 cells. In addition, nectandrin A activated p38 mitogen-activated protein kinase (MAPK) in time- and concentration-dependent manners, and phosphorylated form of pSmad1/5/8 and alkaline phosphatase activity were both decreased when the cells were pretreated with SB203580, a p38 MAPK inhibitor, suggesting that p38 MAPK might be an upstream kinase for Smad signaling pathway. Taken together, nectandrin A enhances the BMP-induced osteoblastic differentiation and mineralization of C2C12 cells via activation of p38 MAPK-Smad signaling pathway, and it has a therapeutic potential for osteoporosis by promoting bone formation.
Full text:
Available
Database:
WPRIM (Western Pacific)
Main subject:
Osteoblasts
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Osteogenesis
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Osteoporosis
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Phosphotransferases
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Protein Kinases
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Pyridines
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Antigens, Differentiation
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Up-Regulation
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Calcium
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P38 Mitogen-Activated Protein Kinases
Language:
English
Journal:
The Korean Journal of Physiology and Pharmacology
Year:
2013
Document type:
Article