Bone Morphogenetic Protein-7 Modifies the Effects of Insulin-Like Growth Factors and Intermittent Parathyroid Hormone (1-34) on Human Periodontal Ligament Cell Physiology In Vitro

2011 ◽  
Vol 82 (6) ◽  
pp. 900-908 ◽  
Author(s):  
Stefan Lossdörfer ◽  
Nuersailike Abuduwali ◽  
Andreas Jäger
Keyword(s):  
Growth Factors ◽  
Parathyroid Hormone ◽  
Bone Morphogenetic Protein ◽  
Periodontal Ligament ◽  
Cell Physiology ◽  
Periodontal Ligament Cell ◽  
Bone Morphogenetic Protein 7 ◽  
Morphogenetic Protein ◽  
Insulin Like Growth Factors

The protective effects of bone morphogenetic protein-7 against epithelial injury and matrix metalloproteases upregulation induced by silica in vitro

2016 ◽  
Vol 36 (9) ◽  
pp. 892-900 ◽  
Author(s):  
D Liang ◽  
G An ◽  
Z Zhu ◽  
Y Wang ◽  
G Yang ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Signaling Pathway ◽  
Western Blotting ◽  
Neutralizing Antibody ◽  
Collagen I ◽  
Bone Morphogenetic Protein 7 ◽  
Smad Signaling ◽  
Morphogenetic Protein ◽  
Smad Signaling Pathway

Objective: We investigate the effects of bone morphogenetic protein-7 (BMP-7) on models with silica-induced and macrophage-mediated fibrosis and its possible mechanisms in vitro. Methods: Rat alveolar II epithelial (RLE-6TN) cells were incubated with the supernatant of mouse macrophage-like cells (RAW264.7) and treated with 0, 25, 50, and 100 μg/mL silica. Using Western blotting, the epithelial markers (surfactant proteins-C and E-cadherin) and the mesenchymal markers (fibronectin (FN) and viminten (Vim)) were detected. After neutralizing the BMP-7, the progress of fibrosis was assessed by the content of hydroxyproline (Hyp) and collagen I, III protein levels as well as the Smad signaling pathway proteins, including phosphorylated Smad1/5(P-Smad1/5) and phosphorylated Smad2/3(P-Smad2/3). Collagen I was also identified by immunofluorescence and pretreated with SB-431542, LDN-193189, or anti-BMP-7-neutralizing antibody. In addition, the levels of matrix metalloproteinase-2 (MMP-2) and MMP-9 were detected using Western blotting. Results: The model of RLE-6TN cells was established successfully, the expressions of Vim, FN, MMP-2, and MMP-9 were upregulated, while the concentration of silica is increased. Neutralizing BMP-7 stimulated the decrease of P-Smad1/5 and the increase of P-Smad2/3, as well as the collagen I, collagen III, FN, and Hyp via Smad signaling pathway. Furthermore, pretreated with LDN-193189 or anti-BMP-7-neutralizing antibody, the expression of collagen I was increased, yet it was decreased with SB-431542 intervention. Conclusion: The activated BMP/Smad and suppressed transforming growth factor-β/Smad pathways could suppress silica-induced fibrosis via a MMP-dependent mechanism. BMP-7 is expected to be the optimized strategy of delaying the interstitial changes.

scholarly journals Bone Morphogenetic Protein 7 (BMP-7) Influences Tendon-Bone Integration In Vitro

PLoS ONE ◽  
2015 ◽  
Vol 10 (2) ◽  
pp. e0116833 ◽  
Author(s):  
Tim Schwarting ◽  
Philipp Lechler ◽  
Johannes Struewer ◽  
Marius Ambrock ◽  
Thomas Manfred Frangen ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Bone Morphogenetic Protein 7 ◽  
Morphogenetic Protein ◽  
Bone Integration

scholarly journals Bone morphogenetic protein-7 prevented epithelial-mesenchymal transition in RLE-6TN cells

2016 ◽  
Vol 5 (3) ◽  
pp. 931-937 ◽  
Author(s):  
Yan Wang ◽  
Di Liang ◽  
Zhonghui Zhu ◽  
Xiaoli Li ◽  
Guoliang An ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Bone Morphogenetic Protein ◽  
Signaling Pathway ◽  
P38 Mapk ◽  
Epithelial Mesenchymal Transition ◽  
Bone Morphogenetic Protein 7 ◽  
Mesenchymal Transition ◽  
Morphogenetic Protein

Silica induced EMT and decreased the expression of BMP-7 in vivo and in vitro, while exogenous BMP-7 promoted MET and inhibited silica-induced EMT associated with inhibition of the p38 MAPK/transcription factor (TF) signaling pathway in RLE-6TN cells.

scholarly journals Characterization of the different oligomeric states of the DAN family antagonists SOSTDC1 and SOST

2020 ◽  
Vol 477 (17) ◽  
pp. 3167-3182
Author(s):  
Gregory R. Gipson ◽  
Chandramohan Kattamuri ◽  
Magdalena Czepnik ◽  
Thomas B. Thompson
Keyword(s):  
Growth Factors ◽  
Bone Morphogenetic Protein ◽  
Extracellular Proteins ◽  
Bmp Signaling ◽  
Differential Screening ◽  
Protein Ligands ◽  
Morphogenetic Protein ◽  
Covalent Dimer

The DAN (differential screening-selected gene aberrative in neuroblastoma) family are a group of secreted extracellular proteins which typically bind to and antagonize BMP (bone morphogenetic protein) ligands. Previous studies have revealed discrepancies between the oligomerization state of certain DAN family members, with SOST (a poor antagonist of BMP signaling) forming a monomer while Grem1, Grem2, and NBL1 (more potent BMP antagonists) form non-disulfide linked dimers. The protein SOSTDC1 (Sclerostin domain containing protein 1) is sequentially similar to SOST, but has been shown to be a better BMP inhibitor. In order to determine the oligomerization state of SOSTDC1 and determine what effect dimerization might have on the mechanism of DAN family antagonism of BMP signaling, we isolated the SOSTDC1 protein and, using a battery of biophysical, biochemical, and structural techniques, showed that SOSTDC1 forms a highly stable non-covalent dimer. Additionally, this SOSTDC1 dimer was shown, using an in vitro cell based assay system, to be an inhibitor of multiple BMP signaling growth factors, including GDF5, while monomeric SOST was a very poor antagonist. These results demonstrate that SOSTDC1 is distinct from paralogue SOST in terms of both oligomerization and strength of BMP inhibition.

Bone Morphogenetic Protein-7 Enhances Cementoblast Function In Vitro

2010 ◽  
Vol 81 (11) ◽  
pp. 1663-1674 ◽  
Author(s):  
Sema S. Hakki ◽  
Brian L. Foster ◽  
Kanako J. Nagatomo ◽  
S. Buket Bozkurt ◽  
Erdogan E. Hakki ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Bone Morphogenetic Protein 7 ◽  
Morphogenetic Protein

scholarly journals Identification of bone morphogenetic protein 7 (BMP7) as an instructive factor for human epidermal Langerhans cell differentiation

2013 ◽  
Vol 210 (12) ◽  
pp. 2597-2610 ◽  
Author(s):  
Nighat Yasmin ◽  
Thomas Bauer ◽  
Madhura Modak ◽  
Karin Wagner ◽  
Christopher Schuster ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Prenatal Development ◽  
Langerhans Cell ◽  
Type I ◽  
Blood Monocytes ◽  
Bone Morphogenetic Protein 7 ◽  
Morphogenetic Protein ◽  
Tgf Β1

Human Langerhans cell (LC) precursors populate the epidermis early during prenatal development and thereafter undergo massive proliferation. The prototypic antiproliferative cytokine TGF-β1 is required for LC differentiation from human CD34+ hematopoietic progenitor cells and blood monocytes in vitro. Similarly, TGF-β1 deficiency results in LC loss in vivo. However, immunohistology studies revealed that human LC niches in early prenatal epidermis and adult basal (germinal) keratinocyte layers lack detectable TGF-β1. Here we demonstrated that these LC niches express high levels of bone morphogenetic protein 7 (BMP7) and that Bmp7-deficient mice exhibit substantially diminished LC numbers, with the remaining cells appearing less dendritic. BMP7 induces LC differentiation and proliferation by activating the BMP type-I receptor ALK3 in the absence of canonical TGF-β1–ALK5 signaling. Conversely, TGF-β1–induced in vitro LC differentiation is mediated via ALK3; however, co-induction of ALK5 diminished TGF-β1–driven LC generation. Therefore, selective ALK3 signaling by BMP7 promotes high LC yields. Within epidermis, BMP7 shows an inverse expression pattern relative to TGF-β1, the latter induced in suprabasal layers and up-regulated in outer layers. We observed that TGF-β1 inhibits microbial activation of BMP7-generated LCs. Therefore, TGF-β1 in suprabasal/outer epidermal layers might inhibit LC activation, resulting in LC network maintenance.

scholarly journals Bone morphogenetic protein 15 and growth differentiation factor 9 co-operate to regulate granulosa cell function in ruminants

Reproduction ◽  
2005 ◽  
Vol 129 (4) ◽  
pp. 481-487 ◽  
Author(s):  
Kenneth P McNatty ◽  
Jennifer L Juengel ◽  
Karen L Reader ◽  
Stan Lun ◽  
Samu Myllymaa ◽  
...  
Keyword(s):  
Growth Factors ◽  
Growth Factor ◽  
Bone Morphogenetic Protein ◽  
Granulosa Cells ◽  
Progesterone Production ◽  
Differentiation Factor ◽  
Morphogenetic Protein ◽  
Growth Differentiation Factor 9 ◽  
Bone Morphogenetic Protein 15

The oocyte-secreted polypeptide growth factors, growth differentiation factor 9 (GDF9) and bone morphogenetic protein 15 (BMP15, also known as GDF9B) have both been shown to be essential for ovarian follicular development and ovulation rate. In addition, it is known from both in vivo and in vitro studies that these factors co-operate in some manner. To date, most studies examining the in vitro effects of these growth factors have used the rodent model. However, the evidence suggests that these growth factors have somewhat different roles between rodents and ruminants. Therefore, the objectives of these studies were to examine the effects of GDF9 and BMP15, alone and together, on the functions of ovine and bovine granulosa cells under in vitro conditions. Ovine (o)BMP15 given together with murine (m)GDF9 or oGDF9 was more potent in stimulating 3H-thymidine incorporation by ovine granulosa cells compared with each growth factor alone. For bovine granulosa cells, there appeared to be little or no co-operativity between oBMP15 and oGDF9 as oBMP15 alone was as potent as any combination of the two growth factors in stimulating 3H-thymidine uptake. The species of origin of GDF9 affected the progesterone response in ovine granulosa cells with mGDF9 stimulating and oGDF9 inhibiting progesterone production. Ovine BMP15 alone had no effect on progesterone production by ovine granulosa cells and these growth factors did not appear to co-operate. FSH-stimulated progesterone production by bovine granulosa cells was most potently inhibited when oBMP15 and murine or ovine GDF9 were administered together. As was observed for progesterone, the species of origin of GDF9 affected inhibin production by ovine granulosa cells where mGDF9 inhibited while oGDF9 stimulated production. Murine GDF9 also inhibited inhibin production from bovine granulosa cells. For both ovine and bovine granulosa cells, BMP15 alone had no effect on inhibin production and there did not appear to be any co-operation between GDF9 and BMP15. These results indicate that the effects of BMP15 and GDF9 varied with respect to the species of origin of the growth factor. Moreover, the effects of GDF9 and BMP15 together were often co-operative and not always the same as those observed for these growth factors alone.

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