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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 (show IRF6 ELISA Kits) through an increase in TLR4 (show TLR4 ELISA Kits), E-selectin (show SELE ELISA Kits), and VCAM-1 (show VCAM1 ELISA Kits) and ultimately through enhanced leukocyte recruitment.
Data suggest BMP9/GDF2 and BMP10 (show BMP10 ELISA Kits) synergize with TNFA (show TNF ELISA Kits) to increase monocyte recruitment to vascular endothelial cells; process appears to be mediated mainly via ALK2/ACVR1 (show ACRV1 ELISA Kits) (which exhibits protein kinase (show CDK7 ELISA Kits) activity). These studies used in vitro flow monocyte adhesion assay. (BMP9 = growth differentiation factor 2; BMP10 (show BMP10 ELISA Kits) = bone morphogenetic protein 10 (show BMP10 ELISA Kits); TNFA (show TNF ELISA Kits) = tumor necrosis factor alpha (show TNF ELISA Kits); ALK2/ACVR1 (show ACRV1 ELISA Kits) = activin A receptor type 1 (show ACRV1 ELISA Kits))
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.
circulating levels significantly decreased in type 2 diabetes mellitus patients and associated with glucose homoeostasis and insulin (show INS ELISA Kits) sensitivity
the data identify MxA (show MX1 ELISA Kits) as a novel stimulator of BMP4 (show BMP4 ELISA Kits) and BMP9 transcriptional signaling, and suggest it to be a candidate IFN-alpha (show IFNA ELISA Kits)-inducible mechanism that might have a protective role against development of pulmonary arterial hypertension and other vascular diseases.
BMP9 inhibited the proliferation and migration of the A549 cells.
his study shows that BMP9 inhibition is associated with Osteosarcoma (OS) development and that enhanced expression of BMP9 may be a potential treatment method for OS
IGF1 (show IGF1 ELISA Kits) can enhance BMP9-induced osteogenic differentiation in 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 (show NOTCH1 ELISA Kits) signaling may play an important role in BMP9-induced osteogenesis and angiogenesis. It's conceivable that simultaneous activation of the BMP9 and Notch (show NOTCH1 ELISA Kits) pathways should efficiently couple osteogenesis and angiogenesis of MSCs for successful bone tissue engineering.
Western blot analysis demonstrated that following BMP2 (show BMP2 ELISA Kits) and BMP7 (show BMP7 ELISA Kits) cotransfection of MC3T3E1 cells, the protein expression levels of BMP2 (show BMP2 ELISA Kits), BMP4 (show BMP4 ELISA Kits), BMP6 (show BMP6 ELISA Kits), BMP7 (show BMP7 ELISA Kits), BMP9 and Wnt3a (show WNT3A ELISA Kits) 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 (show ACVRL1 ELISA Kits) receptor on the cell surface, and inhibiting the ERK1/2 (show MAPK1/3 ELISA Kits) signaling pathways in the cell
that Dkk1 (show DKK1 ELISA Kits) negatively regulates BMP9-induced osteogenic differentiation.
Data show athat beta-catenin (show CTNNB1 ELISA Kits) can be activated by bone morphogenetic protein 9 (BMP9) and the activation of beta-catenin (show CTNNB1 ELISA Kits) 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 (show RUNX2 ELISA Kits) gene, acting as a suppressor.
We have established a producer line that stably expresses a high level of active BMP9 protein. Such producer line should be a valuable resource for generating biologically active BMP9 protein for studying BMP9 signaling
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