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The binding free energies indicate that ALK-3 (zeige BMPR1A Proteine) preferably binds to BMP-2 (zeige BMP2 Proteine) instead of BMP-9. The structural analysis shows that ALK-3 (zeige BMPR1A Proteine) binding with BMP-2 (zeige BMP2 Proteine) occurs in a perfectly symmetry pathway, whereas this symmetry is lost for possible ALK-3 (zeige BMPR1A Proteine) interactions with BMP-9
The BMP9-induced phosphorylation of Smad1 (zeige GARS Proteine)/5/8 was increased with the overexpression of RUNX3 (zeige RUNX3 Proteine), and yet was decreased with the knockdown of RUNX3 (zeige RUNX3 Proteine). Collectively, our findings suggest that RUNX3 (zeige RUNX3 Proteine) is an essential modulator of the BMP9-induced osteoblast lineage differentiation of mesenchymal stem cells (MSCs).
BMP9 is overexpressed in hepatic stellate cells in a cohort of liver fibrosis patients.
our study indicates that BMP9 can inhibit the growth and metastasis of breast cancer cells, which may be related to interaction between pre-adipocytes/adipocytes and MDA-MB-231 cells via leptin (zeige LEP Proteine) signaling pathway.
BMP9 interacts with a hydrophobic surface of the N-terminal orphan domain of ENG (zeige ENG Proteine), which adopts a new duplicated fold generated by circular permutation.
this is the first study that accurately identifies BMP9 as a profibrotic factor in fibroblasts.
the combination of BMP-9 and MC-GAG stimulates chondrocytic and osteogenic differentiation of hMSCs.
The results demonstrate that although BMP9 alone does not influence leukocyte recruitment, it primes the vascular endothelium to mount a more intense response when challenged with LPS (zeige IRF6 Proteine) through an increase in TLR4 (zeige TLR4 Proteine), E-selectin (zeige SELE Proteine), and VCAM-1 (zeige VCAM1 Proteine) and ultimately through enhanced leukocyte recruitment.
Data suggest BMP9/GDF2 and BMP10 (zeige BMP10 Proteine) synergize with TNFA (zeige TNF Proteine) to increase monocyte recruitment to vascular endothelial cells; process appears to be mediated mainly via ALK2/ACVR1 (zeige ACRV1 Proteine) (which exhibits protein kinase (zeige CDK7 Proteine) activity). These studies used in vitro flow monocyte adhesion assay. (BMP9 = growth differentiation factor 2; BMP10 (zeige BMP10 Proteine) = bone morphogenetic protein 10 (zeige BMP10 Proteine); TNFA (zeige TNF Proteine) = tumor necrosis factor alpha (zeige TNF Proteine); ALK2/ACVR1 (zeige ACRV1 Proteine) = activin A receptor type 1 (zeige ACRV1 Proteine))
These results suggest that BMP9-transduced calvarial mesenchymal progenitor cells seeded in a PPCN-g thermoresponsive scaffold is capable of inducing bone formation in vivo and is an effective means of creating tissue engineered bone for critical sized defects.
These results suggest that RUNX1 (zeige RUNX1 Proteine) may be an essential modulator in BMP9- induced osteogenic differentiation of mesenchymal stem cells.
results provide a better understanding into how BMP-9 induces osteoblast differentiation and its synergy with IGF-2 at the signaling level.
Our findings provide a clearer understanding of the cellular pathways utilized by BMP-9 for chondrogenesis that may help improve current therapies for regenerative cartilage repair.
Constitutive expression of low levels of BMP-9 stabilises hepatocyte function in the healthy liver. High levels of BMP-9 cause enhanced damage upon acute or chronic injury.
Notch (zeige NOTCH1 Proteine) signaling may play an important role in BMP9-induced osteogenesis and angiogenesis. It's conceivable that simultaneous activation of the BMP9 and Notch (zeige NOTCH1 Proteine) pathways should efficiently couple osteogenesis and angiogenesis of MSCs for successful bone tissue engineering.
Western blot analysis demonstrated that following BMP2 (zeige BMP2 Proteine) and BMP7 (zeige BMP7 Proteine) cotransfection of MC3T3E1 cells, the protein expression levels of BMP2 (zeige BMP2 Proteine), BMP4 (zeige BMP4 Proteine), BMP6 (zeige BMP6 Proteine), BMP7 (zeige BMP7 Proteine), BMP9 and Wnt3a (zeige WNT3A Proteine) were increased compared with control cells
he results of the present study demonstrated that BMP9 promoted the osteoclast differentiation of osteoclast precursors via binding to the ALK1 receptor on the cell surface, and inhibiting the ERK1/2 signaling pathways in the cell
that Dkk1 (zeige DKK1 Proteine) negatively regulates BMP9-induced osteogenic differentiation.
Data show athat beta-catenin (zeige CTNNB1 Proteine) can be activated by bone morphogenetic protein 9 (BMP9) and the activation of beta-catenin (zeige CTNNB1 Proteine) plays an important role in the differentiation of C3H10T1/2 cells into cardiomyocyte-like cells induced by BMP9.
miR23b inhibits BMP9induced C2C12 myoblast osteogenesis via targeting of the Runx2 (zeige RUNX2 Proteine) gene, acting as a suppressor.
The protein encoded by this gene is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Studies in rodents suggest that this protein plays a role in the adult liver and in differentiation of cholinergic central nervous system neurons.
bone morphogenetic protein 9
, growth/differentiation factor 2