scholarly journals Continuous release of bone morphogenetic protein-2 through nano-graphene oxide-based delivery influences the activation of the NF-κB signal transduction pathway

2017 ◽  
Vol Volume 12 ◽  
pp. 1215-1226 ◽  
Author(s):  
Cheng Zhong ◽  
Jun Feng ◽  
Xiangjin Lin ◽  
Qi Bao
Keyword(s):  
Signal Transduction ◽  
Graphene Oxide ◽  
Bone Morphogenetic Protein ◽  
Signal Transduction Pathway ◽  
Bone Morphogenetic Protein 2 ◽  
Transduction Pathway ◽  
Nf Kappa B ◽  
Continuous Release ◽  
Morphogenetic Protein ◽  
Nano Graphene

Hemojuvelin Acts as a Bone Morphogenetic Protein Co-Receptor To Regulate Hepcidin Expression.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 511-511 ◽  
Author(s):  
Franklin W. Huang ◽  
Jodie L. Babitt ◽  
Diedra M. Wrighting ◽  
Tarek A. Samad ◽  
Yin Xia ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Bone Morphogenetic Protein ◽  
Signal Transduction Pathway ◽  
Bmp Signaling ◽  
Dominant Negative ◽  
Transduction Pathway ◽  
Reporter Construct ◽  
Hepcidin Expression ◽  
Morphogenetic Protein ◽  
Juvenile Hemochromatosis

Abstract Juvenile hemochromatosis is a severe iron overload disorder resulting from mutations in the hemojuvelin (HJV) gene. To understand its pathogenesis, we developed Hjv−/− mice. Similar to human patients, Hjv−/− animals accumulate excess iron in the liver, pancreas and heart early in life. Tissue macrophages are iron-depleted. Hjv−/− mice express very low levels of hepcidin mRNA and, likely as a consequence, have elevated expression of the iron transporter ferroportin in enterocytes and macrophages. These results suggested that Hjv plays a role in regulating hepcidin expression. Two known Hjv homologs, Rgma and Rgmb, have previously been shown to act as bone morphogenetic protein (BMP) co-receptors. We hypothesized that Hjv regulates hepcidin expression through a BMP signal transduction pathway. We found that Hjv binds radiolabeled BMP, supporting the contention that it is a BMP co-receptor. Transfection of HepG2 cells with Hjv cDNA activated a BMP-responsive reporter construct and augmented its response to exogenous BMP. Both an anti-BMP neutralizing antibody and the natural BMP antagonist Noggin blocked this response, as did co-expressed dominant negative BMP receptor proteins. When cells were transfected with a construct carrying an Hjv mutation known to cause human disease, BMP reporter activation was significantly reduced in the presence and absence of exogenous BMP. Treatment with BMP stimulated hepcidin production in hepatoma cells and activated a reporter construct containing a fragment of the hepcidin promoter. To extend these results, we studied tissues from Hjv−/− mice. BMP signals are transduced through phosphorylation of Smad proteins. We found that Smads 1, 5 and 8 were hypophosphorylated in Hjv−/− liver, consistent with impaired BMP signaling. BMP treatment of wild type and Hjv−/− primary hepatocytes induced hepcidin expression, but induction was blunted in cells from Hjv−/− animals. Taken together, these data suggest that the normal hepatic function of Hjv is to serve as a BMP co-receptor, modulating a signal transduction pathway that culminates in hepcidin expression. [Note - Jodie L. Babitt is the first author of this abstract, but it will be presented by Franklin W. Huang, the second author]

scholarly journals A Kinase Domain-truncated Type I Receptor Blocks Bone Morphogenetic Protein-2-induced Signal Transduction in C2C12 Myoblasts

1997 ◽  
Vol 272 (35) ◽  
pp. 22046-22052 ◽  
Author(s):  
Mana Namiki ◽  
Shuichi Akiyama ◽  
Takenobu Katagiri ◽  
Atsushi Suzuki ◽  
Naoto Ueno ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Bone Morphogenetic Protein ◽  
Kinase Domain ◽  
Bone Morphogenetic Protein 2 ◽  
Type I ◽  
C2c12 Myoblasts ◽  
Morphogenetic Protein ◽  
Induced Signal

scholarly journals Immobilization of Bone Morphogenetic Protein on DOPA- or Dopamine-Treated Titanium Surfaces to Enhance Osseointegration

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Jeonghwa Kang ◽  
Seiichi Tada ◽  
Takashi Kitajima ◽  
Tae Il Son ◽  
Toshiro Aigaki ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Bone Morphogenetic Protein ◽  
Coupling Reaction ◽  
Bone Morphogenetic Protein 2 ◽  
Surface Immobilization ◽  
Amino Groups ◽  
High Ph ◽  
Specific Signal ◽  
Morphogenetic Protein ◽  
Differentiation Marker

Titanium was treated with 3,4-dihydroxy-L-phenylalanine (DOPA) or dopamine to immobilize bone morphogenetic protein-2 (BMP2), a biomolecule. DOPA and dopamine solutions turned into suspensions, and precipitates were produced at high pH. Both treatments produced a brown surface on titanium that was thicker at high pH than low pH. Dopamine produced a thicker layer than DOPA. The hydrophobicity of the surfaces increased after treatment with dopamine independent of pH. Furthermore, there were more amino groups in the layers formed at pH 8.5 than pH 4.5 in both treatments. Dopamine treatment produced more amino groups in the layer than DOPA. BMP2 was immobilized on the treated surfaces via a coupling reaction using carbodiimide. More BMP2 was immobilized on surfaces treated at pH 8.5 than pH 4.5 in both treatments. The immobilized BMP induced specific signal transduction and alkali phosphatase, a differentiation marker. Thus, the present study demonstrates that titanium treated with DOPA or dopamine can become bioactive via the surface immobilization of BMP2, which induces specific signal transduction.

Sign in / Sign up

Export Citation Format

Share Document