Regulation of osteoprotegerin and RANKL gene expression by Wnt/β-catenin and bone morphogenetic protein-2 in C2C12 cells

2008 ◽  
pp. 173-178
Author(s):  
Mari Sato ◽  
Aiko Nakashima ◽  
Masayuki Nashimoto ◽  
Yasutaka Yawaka ◽  
Masato Tamura
Keyword(s):  
Gene Expression ◽  
Bone Morphogenetic Protein ◽  
C2c12 Cells ◽  
Bone Morphogenetic Protein 2 ◽  
Morphogenetic Protein

Gene Expression During Autograft Lumbar Spine Fusion and the Effect of Bone Morphogenetic Protein 2

1998 ◽  
Vol 351 ◽  
pp. 252???265 ◽  
Author(s):  
Michael A. Morone ◽  
Scott D. Boden ◽  
Gregory Hair ◽  
George J. Martin ◽  
Michele Racine ◽  
...  
Keyword(s):  
Gene Expression ◽  
Lumbar Spine ◽  
Bone Morphogenetic Protein ◽  
Spine Fusion ◽  
Bone Morphogenetic Protein 2 ◽  
Lumbar Spine Fusion ◽  
Morphogenetic Protein

scholarly journals Differential Regulation of the Two Principal Runx2/Cbfa1 N-Terminal Isoforms in Response to Bone Morphogenetic Protein-2 during Development of the Osteoblast Phenotype

Endocrinology ◽  
2001 ◽  
Vol 142 (9) ◽  
pp. 4026-4039 ◽  
Author(s):  
Chaitali Banerjee ◽  
Amjad Javed ◽  
Je-Yong Choi ◽  
Jack Green ◽  
Vicki Rosen ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Osteoblast Differentiation ◽  
Mesenchymal Cell ◽  
Cellular Protein ◽  
C2c12 Cells ◽  
Bone Morphogenetic Protein 2 ◽  
Type I ◽  
Type Ii ◽  
Specific Expression ◽  
Morphogenetic Protein

Abstract Cbfa1/Runx2 is a transcription factor essential for bone formation and osteoblast differentiation. Two major N-terminal isoforms of Cbfa1, designated type I/p56 (PEBP2aA1, starting with the sequence MRIPV) and type II/p57 (til-1, starting with the sequence MASNS), each regulated by distinct promoters, are known. Here, we show that the type I transcript is constitutively expressed in nonosseous mesenchymal tissues and in osteoblast progenitor cells. Cbfa1 type I isoform expression does not change with the differentiation status of the cells. In contrast, the type II transcript is increased during differentiation of primary osteoblasts and is induced in osteoprogenitors and in premyoblast C2C12 cells in response to bone morphogenetic protein-2. The functional equivalence of the two isoforms in activation and repression of bone-specific genes indicates overlapping functional roles. The presence of the ubiquitous type I isoform in nonosseous cells and before bone morphogenetic protein-2 induced expression of the type II isoform suggests a regulatory role for Cbfa1 type I in early stages of mesenchymal cell development, whereas type II is necessary for osteogenesis and maintenance of the osteoblast phenotype. Our data indicate that Cbfa1 function is regulated by transcription, cellular protein levels, and DNA binding activity during osteoblast differentiation. Taken together, our studies suggest that developmental timing and cell type- specific expression of type I and type II Cbfa isoforms, and not necessarily molecular properties or sequences that reside in the N-terminus of Cbfa1, are the principal determinants of the osteogenic activity of Cbfa1.

Refolding and Purification of rhBMP-2 Expressed as Inclusion Bodies in E.COLI with Hydroxyapatite Chromatography

2005 ◽  
Vol 288-289 ◽  
pp. 661-664 ◽  
Author(s):  
Shaohua Yao ◽  
Ling Li Zhang ◽  
Steven Y. Cheng ◽  
Xing Dong Zhang
Keyword(s):  
Biological Activity ◽  
Bone Morphogenetic Protein ◽  
Efficient Method ◽  
Recombinant Plasmid ◽  
Inclusion Bodies ◽  
C2c12 Cells ◽  
Bone Morphogenetic Protein 2 ◽  
Morphogenetic Protein ◽  
Alkaline Phosphate ◽  
High Level

The objective of this study was to develop an efficient method for the production of bioactive bone morphogenetic protein 2 (BMP-2). A recombinant plasmid encoding mature human BMP-2 was transferred and expressed at a high level in E.coli. Most of the aimed proteins existed in inclusion bodies. The non-active recombinant human BMP-2 (rhBMP-2) monomer in inclusion bodies was refolded and simultaneously purified using hydroxyapatite (HA) chromatography. After oxidization of the monomer, the rhBMP-2 dimmer showed biological activity by the induction of alkaline phosphate activity in C2C12 cells. The refolding yield was about 30% and the purity was about 90% just by one chromatography process.

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