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Human BMPR2 Protein expressed in Wheat germ - ABIN1346791
Miyagi, Mikawa, Hasegawa, Kobayashi, Sho, Matsuyama, Sato: Bone morphogenetic protein receptor expressions in the adult rat brain. in Neuroscience 2011
bmpr2b mediates BMP signaling and is required to establish left-right asymmetry.
Sequencing of BMPR2, CAV1 (show CAV1 Proteins), and KCNK3 (show KCNK3 Proteins) coding regions did not identify any pathogenic variants in these genes in infants with pulmonary hypoplasia and pulmonary hypertension.
The present study showed that deletion-duplication mutations in the BMPR2 or ACVRL1 (show ACVRL1 Proteins) genes may not be associated with non-regression of Pulmonary arterial hypertension.
BMPR2 mutation carriers are more prone to hemoptysis and that hemoptysis is closely correlated to bronchial arterial remodelling and angiogenesis; in turn, pronounced changes in the systemic vasculature correlate with increased pulmonary venous remodelling, creating a distinctive profile in pulmonary arterial hypertension patients harbouring a BMPR2 mutation.
Studying the methylation pattern of the BMPR2 promoter region in pulmonary arterial hypertension patients and controls revealed a a CpG island, suitable for methylation, in the BMPR2 promoter region, in addition to NIT-2, sex-determining region Y, and heat shock factor transcription factor binding sites.No evidence of methylation was detected in this region in patients and controls.
Mutations in the bone morphogenetic protein receptor type-2 gene (BMPR2) have been identified in patients with pulmonary arterial hypertension.
Affected mutation carriers with heritable pulmonary hypertension have hypermethylation of the BMPR2 promotor compared with their unaffected relatives.
increased BMPR2 signal transduction is linked to fragile X (show FMR1 Proteins) syndrome (FXS) and that the BMPR2-LIMK1 (show LIMK1 Proteins) pathway is a putative therapeutic target in patients with FXS and possibly other forms of autism
A burden of rare variants in BMPR2 significantly contributed to the risk of pulmonary arterial hypertension. In the remaining one family, the patient carried a pathogenic variant in a member of potassium channels, KCNK3 (show KCNK3 Proteins), which was the first replicative finding of channelopathy in an Asian population.
The SMYD2 may promote BMP signaling by directly methylating BMPR2, which, in turn, stimulates BMPR2 kinase activity and activation of the BMP pathway.
This review focuses on recent advances in rescuing BMPRII expression, function or signaling to prevent and reverse pulmonary vascular remodeling in pulmonary arterial hypertension and its feasibility for clinical translation. Furthermore, it summarizes the role of described miRNAs that directly target the BMPR2 gene in blood vessels. [review]
High BMPR2 expression is associated with aberrant synaptic development in mouse and Drosophila models of Fragile X (show FMR1 Proteins) syndrome.
BMPR2 deletion extended survival relative to Pten deletion alone, establishing its promoting role in BMP6 (show BMP6 Proteins)-driven prostate cancer progression
Dual luciferase report assay verified that miR (show MLXIP Proteins)-3065-5p could bind to the 3'UTR of bone morphogenetic protein receptor type II (BMPR2), which dramatically increased in the beginning of odontoblastic differentiation but decreased in the terminal differentiation stage.
Disrupting BMPR2 impairs TGFbeta1 (show TGFB1 Proteins)- and BMP4 (show BMP4 Proteins)-mediated elastic fiber assembly and is of pathophysiologic significance in pulmonary arterial hypertension.
These results suggested that endogenous PTH enhanced BMPR2 expression by a cAMP/PKA/CREB pathway in osteoblasts, and increased RUNX2 expression through transduction of the BMP/pSMAD1/5/8 signaling pathway
Cav-1 (show CAV1 Proteins) depletion, oxidative stress-mediated reduction in BMPRII expression, and enhanced TGF-beta (show TGFB1 Proteins)-driven SMAD-2 (show SMAD2 Proteins)/3 signaling promote pulmonary vascular remodeling in inflamed lungs.
BMPR2 gene transfer reduced TGF-beta effects on Smad2, Smad1/5/8 and Erk1/2 phosphorylation in human pulmonary arterial smooth muscle cells
Deleting Bmpr2 in mouse skeletal progenitor cells impaired activin signaling resulting in an increased bone formation rate and high bone mass.
The findings suggest that the mutant ALK2 (show ACRV1 Proteins) related to Fibrodysplasia ossificans progressiva is enhanced by bone morphogenetic protein type II receptors via the T203-regulated phosphorylation of ALK2 (show ACRV1 Proteins).
Report temporal regulation of BMPR2 mRNA expression in the oocyte, granulosa and theca cells of developing preovulatory follicles in the pig.
Losartan therapy was associated with persistent overexpressions of ANG II (show AGT Proteins), AT2 (show AGTR2 Proteins), ET-1 (show EDN1 Proteins), ETB (show EDNRB Proteins), and angiopoietin-1 (show ANGPT1 Proteins) and with a return to normal of the BMPR-2 expression.
Inhibition of BMPR2 resulted in increased expression of ALK4 (show ACVR1B Proteins) and decreased expression of PTX3 (show PTX3 Proteins), HAS2 (show HAS2 Proteins) and PTGS2 (show PTGS2 Proteins).
These findings are important because Wnt (show WNT2 Proteins), BMPR2, and Akt3 (show AKT3 Proteins) promote neurogenesis and cell survival, processes crucial for lifelong viral latency.
the miR-17-92 cluster is involved in granulosa cell proliferation and differentiation by coordinately targeting the PTEN and BMPR2 genes.
Stimulation of BMPRII promotes normal pulmonary artery endothelial cell function by activating eNOS (show NOS3 Proteins).
This gene encodes a member of the bone morphogenetic protein (BMP) receptor family of transmembrane serine/threonine kinases. The ligands of this receptor are BMPs, which are members of the TGF-beta superfamily. BMPs are involved in endochondral bone formation and embryogenesis. These proteins transduce their signals through the formation of heteromeric complexes of two different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding. Mutations in this gene have been associated with primary pulmonary hypertension, both familial and fenfluramine-associated, and with pulmonary venoocclusive disease.
bone morphogenetic protein receptor type II
, bone morphogenetic protein receptor type-2
, bone morphogenetic protein receptor type II b
, BMP type II receptor
, BMP type-2 receptor
, type II activin receptor-like kinase
, type II receptor for bone morphogenetic protein-4
, bone morphogenic protein receptor, type II (serine/threonine kinase)
, bone morphogenic protein receptor type 2