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Growth differentiation factor 2

BMP-9, bone morphogenetic protein-9
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ALK-1, CAN, Smad1, SFRP1, V1a
Papers using BMP-9 antibodies
Misexpression of chick Vg1 in the marginal zone induces primitive streak formation
Dodd Jane et al., In Neural Development, 1996
... corresponding to C-terminal amino acids 133 through 144 in the mature coding sequence of mouse BMP9 (Covance Research Products, Inc., Denver, PA, USA) ...
Papers on BMP-9
Recombinant Human Bone Morphogenetic Protein 9 (rhBMP9) Induced Osteoblastic Behaviour on a Collagen Membrane Compared With rhBMP2.
Miron et al., Bern, Switzerland. In J Periodontol, Feb 2016
BACKGROUND: Bone morphogenetic protein 9 (BMP9) has previously been characterized as one of the most osteogenic growth factors of the BMP-family, however, up until now, these experiments have only been demonstrated using adenovirus-transfection experiments (gene therapy).
Putative hormone with anti-obesogenic and insulin-sensitizing effect.
Grubesic et al., Rijeka, Croatia. In Int J Immunopathol Pharmacol, Jan 2016
UNASSIGNED: It was confirmed that bone morphogenetic protein-9 (BMP-9), like insulin, improves glycemia in diabetic mice and regulates glucose metabolism in hepatocytes, which is why it is proposed as a candidate for the hepatic insulin-sensitizing substance (HISS).
Rapid activation of bone morphogenic protein 9 by receptor-mediated displacement of pro-domains.
Lorenz et al., Germany. In J Biol Chem, Jan 2016
In case of bone morphogenic protein 9 (BMP9), however, the pro-domains do not inhibit the bioactivity of the growth factor, and the BMP9-pro-domain complexes have equivalent biological activities as the BMP9 mature ligand dimers.
Modulation of MAPK signalling by immobilized adhesive peptides: Effect on stem cell response to BMP-9-derived peptides.
Faucheux et al., Sherbrooke, Canada. In Acta Biomater, Jan 2016
We have analyzed the influence of polycaprolactone (PCL) films, functionalized with adhesive peptides derived from fibronectin (pFibro) or bone sialoprotein (pBSP), on the response of murine multipotent C3H10T1/2 cells to bone morphogenetic protein-9 (BMP-9) and its derived peptides (pBMP-9 and SpBMP-9).
Soluble endoglin, hypercholesterolemia and endothelial dysfunction.
Nachtigal et al., Hradec Králové, Czech Republic. In Atherosclerosis, Dec 2015
We also addressed a potential interaction of sEng with TGF-β/eNOS or BMP-9 signaling.
Epigenetic Regulation of GDF2 Suppresses Anoikis in Ovarian and Breast Epithelia.
Mythreye et al., Durham, United States. In Neoplasia, Nov 2015
The protein encoded by GDF2 is BMP9 and is a member of the bone morphogenetic protein family and the transforming growth factor (TGF) β superfamily with emerging yet controversial roles in carcinogenesis.
Selective enhancement of endothelial BMPR-II with BMP9 reverses pulmonary arterial hypertension.
Morrell et al., Basel, Switzerland. In Nat Med, Jul 2015
Here, we identify BMP9 as the preferred ligand for preventing apoptosis and enhancing monolayer integrity in both pulmonary arterial endothelial cells and blood outgrowth endothelial cells from subjects with PAH who bear mutations in the gene encoding BMPR-II, BMPR2.
Brown adipose tissue activity as a target for the treatment of obesity/insulin resistance.
Rohner-Jeanrenaud et al., Genève, Switzerland. In Front Physiol, 2014
Endocrine factors, such as fibroblast growth factor 21 (FGF21) and bone morphogenic protein factor-9 (BMP-9), predominantly produced in the liver, were shown to lead to activation of BAT thermogenesis, as well as to "browning" of WAT.
VEGF, Notch and TGFβ/BMPs in regulation of sprouting angiogenesis and vascular patterning.
Jakobsson et al., Stockholm, Sweden. In Biochem Soc Trans, 2014
For example, the pro-angiogenic VEGFA is secreted by cells in need of oxygen, presented to the basal side of the endothelium, whereas BMP9 and BMP10 are supplied via the bloodstream in constant interaction with the apical side to suppress angiogenesis.
The promise of recombinant BMP ligands and other approaches targeting BMPR-II in the treatment of pulmonary arterial hypertension.
Morrell et al., Cambridge, United Kingdom. In Glob Cardiol Sci Pract, 2014
Of these, supplementation of endothelial BMP9/10 signalling with exogenous recombinant ligand has been shown to hold considerable promise as a novel large molecule biopharmaceutical therapy.
TGF-β & BMP receptors endoglin and ALK1: overview of their functional role and status as antiangiogenic targets.
Jonker, Carlisle, United Kingdom. In Microcirculation, 2014
Members of the TGF-β superfamily, TGF-β1, TGF-β3, and BMP9, are key propagators of both inhibition and initiation of angiogenesis.
Potential roles of BMP9 in liver fibrosis.
Ge et al., Shanghai, China. In Int J Mol Sci, 2013
Bone morphogenetic protein 9 (BMP9) is the most recently discovered member of the BMP family.
BMP9 induces EphrinB2 expression in endothelial cells through an Alk1-BMPRII/ActRII-ID1/ID3-dependent pathway: implications for hereditary hemorrhagic telangiectasia type II.
Hughes et al., Irvine, United States. In Angiogenesis, 2012
in an in vitro model of HHT2, loss of Alk1 blocks BMP9 signaling, resulting in reduced EphrinB2 expression, enhanced VEGFR2 expression, and misregulated EC sprouting and anastomosis
Platelet activation receptor CLEC-2 regulates blood/lymphatic vessel separation by inhibiting proliferation, migration, and tube formation of lymphatic endothelial cells.
Ozaki et al., Japan. In J Biol Chem, 2012
platelets regulate blood/lymphatic vessel separation by inhibiting the proliferation, migration, and tube formation of LECs, mainly because of the release of BMP-9 upon activation by CLEC-2/podoplanin in
BMP9 and BMP10 are critical for postnatal retinal vascular remodeling.
Bailly et al., Grenoble, France. In Blood, 2012
BMP9 and BMP10 are important in postnatal vascular remodeling of the retina and BMP10 can substitute for BMP9.
Anti-human activin receptor-like kinase 1 (ALK1) antibody attenuates bone morphogenetic protein 9 (BMP9)-induced ALK1 signaling and interferes with endothelial cell sprouting.
ten Dijke et al., Leiden, Netherlands. In J Biol Chem, 2012
data suggest that both the VEGF/VEGF receptor and the BMP9/ALK1 pathways are essential for stimulating angiogenesis, and targeting both pathways simultaneously may be an attractive strategy to overcome resistance to antiangiogenesis therapy
Crossveinless 2 regulates bone morphogenetic protein 9 in human and mouse vascular endothelium.
Boström et al., Los Angeles, United States. In Blood, 2012
Mutual regulation by BMP-9 and CV2 is essential in regulating the development of the vascular endothelium.
Lack of the bone morphogenetic protein BMP6 induces massive iron overload.
Roth et al., Toulouse, France. In Nat Genet, 2009
Expression of hepcidin, a key regulator of intestinal iron absorption, can be induced in vitro by several bone morphogenetic proteins (BMPs), including BMP2, BMP4 and BMP9 (refs.
An integrated functional genomics screening program reveals a role for BMP-9 in glucose homeostasis.
Birse et al., Rockville, United States. In Nat Biotechnol, 2003
Bone morphogenetic protein-9 (BMP-9) gave a positive response in two independent assays: reducing phosphoenolpyruvate carboxykinase (PEPCK) expression in hepatocytes and activating Akt kinase in differentiated myotubes.
Induction and maintenance of the neuronal cholinergic phenotype in the central nervous system by BMP-9.
Blusztajn et al., Boston, United States. In Science, 2000
A member of this family, BMP-9, was found to be highly expressed in the embryonic mouse septum and spinal cord, indicating a possible role in regulating the cholinergic phenotype.
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