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Human BMP4 Protein expressed in Escherichia coli (E. coli) - ABIN413086
Riesco, Valcarce, Alfonso, Herráez, Robles: In vitro generation of zebrafish PGC-like cells. in Biology of reproduction 2014
We detected a haplotype-based interaction for BMP4 and IRF6 (show IRF6 Proteins) genes for expression of the orofacial cleft phenotype. Although the MDR methods indicate that the effect of interaction between these genes appears to be mild, the presence of specific haplotype combinations conferring a higher risk for NSCL (show NHLH1 Proteins)/P reveals the possible combined role of these genes in the pathogenesis of this prevalent birth defect.
Data show that bone morphogenetic protein 4 (BMP4) expression is associated and favored type II macrophage differentiation.
MiR (show MLXIP Proteins)-876-5p suppresses epithelial-mesenchymal transition of lung cancer by directly down-regulating BMP-4.
endothelial BMP4 controls leukocyte recruitment through a VE-cadherin (show CDH5 Proteins)-dependent mechanism and BMP4-induced inflammation might be involved in the pathogenesis of endothelial cell damage following successful resuscitation after cardiac arrest.
Studied serum levels of bone morphogenic protein-4 (BMP-4) and matrix Gla protein (MGP (show MGP Proteins)) in patients who were admitted to emergency department with the diagnosis of acute coronary syndrome (ACS (show PLA2G15 Proteins)) and underwent primary percutaneous coronary intervention. MGP (show MGP Proteins) and BMP-4 levels were significantly elevated when compared to subjects with normal coronary arteries.
BMP4 inhibits epithelial-mesenchymal transition of the retinal pigment epithelium.
Potentially functional and tagging SNPs of BMP2 (show BMP2 Proteins) (rs170986, rs1979855, rs1980499, rs235768, rs3178250) and BMP4 (rs17563, rs4898820, rs762642) were genotyped in NSCLC.
BMP4 polymorphic site rs4901474 (T>C) had an effect on hypertension; CC genotype carriers had a 1.48-fold risk for hypertension at the age of 50 years when compared with T-allele carriers
High serum BMP4 levels are associated with postmenopausal osteoporosis.
results indicate that the BMP4 rs17563 variant is likely to confer a protective effect against the occurrence of Non-Syndromic Cleft Lip with or without Cleft Palate in a sample of the southeast Iranian population.
we demonstrated that the anterior and posterior phenotypes observed in Bmp4 heterozygous animals showed a strong propensity to co-occur, suggesting a common, non-cell autonomous source for these defects.
p73 is required for appropriate BMP-induced mesenchymal-to-epithelial transition during somatic cell reprogramming.
BMP4 inhibits type 2 epithelial cells (AT2s) proliferation, whereas antagonists (follistatin, noggin) promote AT2 self-renewal at the expense of differentiation. Gain- and loss-of-function genetic manipulation reveals that reduced BMP signaling in AT2s after PNX allows self-renewal but reduces differentiation
this study shows that negative autoregulation of BMP4 dependent transcription by SIN3B (show SIN3B Proteins) splicing reveals a role for RBM39 (show RBM39 Proteins)
Gene expression profiling showed that MuSK (show MUSK Proteins) was required for the BMP4-induced expression of a subset of genes in myoblasts, including regulator of G protein signaling 4 (Rgs4 (show RGS4 Proteins)).
differentiated cells exhibited contracting masses. These results suggest that BMP4-mediated somatic stem cell reprogramming may become an alternative approach for cell therapy
Bmp4 promotes a brown to white-like adipocyte shift.
results suggest that bone morphogenetic protein 4 promotes the generation of male germ cells from induced pluripotent stem (iPS (show SLC27A4 Proteins)) cells
These results suggest how BMP4 regulates adipocyte recruitment in subcutaneous (SC) white adipose tissue, and thus promote its beneficial metabolic effects.
Structures of Bmp2a (show BMP2 Proteins), Bmp2b, Bmp4 and Bmp16 were found to be remarkably similar; with residues involved in receptor binding being highly conserved.
FGF signaling in establishment of the developmental hematopoietic stem cell niche occurs via inhibition of bmp4 transcription, and activation of bmp antagonists, nog2 and grem1a (show GREM1 Proteins).
we identify a previously unappreciated role for the Nodal-transcription factor FoxH1 in mediating cell responsiveness to Bmp further linking the control of these two pathways in the heart
Results show that BMP4 down-regulates fshr (show FSHR Proteins) while up-regulating lhr (show LHCGR Proteins) expression.
These data reveal a novel role for LRP1 (show LRP1 Proteins) in the regulation of Bmp4 signaling by regulating receptor complex endocytosis.
Id2a and Bmp4 misexpression resulted in similar ectomesenchyme defects;misexpression of Bmp4 in migrating Cranial neural crest cells inhibits ectomesenchyme formation.
Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling is both sufficient and required for the induction of BMP4 and Tbx2b expression in the AVC
identify Npnt (show NPNT Proteins) as a novel upstream regulator of Bmp4-Has2 (show HAS2 Proteins) signaling that plays a crucial role in AV canal differentiation
immature AVC expansion in wkm mutants is rescued by depleting Bmp4, indicating that Tmem2 (show TMEM2 Proteins) restricts bmp4 expression to delimit the AVC primordium during cardiac development
Elimination of function of bmp2b and bmp4 singly and in combination did not prevent the formation of mature, attached teeth.
Data indicate that bone morphogenetic protein (BMP) signaling is essential for erythroid differentiation, and in the absence of BMP signaling, precursor cells adopt an endothelial cell (EC) fate.
Osr1 (show OSR1 Proteins)/Osr2 normally repress bmp4 expression in the lateral plate mesoderm prior to respiratory specification.
The results suggest that DeltaNp63 is an essential gene in early epidermal specification under the control of BMP4.
PIAS (show PIAS1 Proteins) proteins have differential ability to regulate signals from the growth factors activin, bone morphogenetic protein 4 (BMP4), and Wnt8 (show WNT8A Proteins).
Data show that PV.1A undergoes combinatorial regulation during early Xenopus development as both the direct target of BMP-4 signaling and as the direct and indirect target of positive and negative regulatory factors.
BMP inhibition is sufficient for neural induction in vivo, and that in the absence of ventral BMPs, Spemann organizer signals are not required for brain formation.
Data suggest that the feedback inhibitors BAMBI (show BAMBI Proteins), SMAD6 (show SMAD6 Proteins), and SMAD7 (show SMAD7 Proteins) expand the dynamic BMP4 signaling range essential for proper embryonic patterning and reduce interindividual phenotypic and molecular variability in Xenopus embryos.
limits homeobox (show PRRX1 Proteins) gene expression in the organiser/non-organiser direction
X-epilectin expression is down-regulated by Noggin (show NOG Proteins) and tBR and that this effect is inhibited by BMP4 over-expression
BMP4-dependent expression of Xenopus Grainyhead-like 1 (show GRHL1 Proteins) has a critical role in epidermal differentiation
High BMP4 expression is associated with cystic ovarian disease.
Bone morphogenetic protein 4 and retinoic acid trigger bovine VASA homolog (show DDX4 Proteins) expression in differentiating bovine induced pluripotent stem cells.
The BMP2/4 ligand and receptor system presides within bovine trophectoderm prior to uterine attachment. BMP4 negatively impacts CT1 (show SLC6A8 Proteins) cell growth
BMP4 during maturation increased the proportion of Oct-4 (show POU5F1 Proteins) positive cells in parthenogenic embryos. BMP4 is implicated in bovine oocytes maturation and embryo development.
analysis of polymorphic CA microsatellites in the third exon of the bovine BMP4 gene
concluded that a bone morphogenetic protein (BMP)-signaling system, consisting of BMP2, BMP4, type II and I receptors, is present in bovine antral follicles and plays a role in development and functioning of follicles rather than in oocyte maturation
Data report that BMP-7 (show BMP7 Proteins) suppresses granulosa cell apoptosis by inhibiting the release of caspase-activated DNase (CAD (show DFFB Proteins)) via a mechanism which does not appear to be associated with the mitochondrial pathway, whereas BMP-4 inhibits the release of CAD.
Heat shock protein 70 (show HSP70 Proteins) enhances vascular bone morphogenetic protein-4 signaling by binding matrix Gla protein (show MGP Proteins).
The TM-induced characteristic changes in the expression pattern of Hoxa11 (show HOXA11 Proteins) and Bmp4 on GDs (show PAEP Proteins) 10 and/or 11 were not noted.
BMP4 is expressed peripherally in hypoblast and epiblast and in the mesoderm at the posterior pole of the embryonic disc.
Data show that BMP-2 (show BMP2 Proteins), BMP-4, and BMP-7 (show BMP7 Proteins), noggin (show NOG Proteins), and chordin (show CHRD Proteins) were colocalized in rimming osteoblasts, osteoclasts, and chondrocytes.
Both of the adenovirus-containing bone morphogenetic protein transduced MSCs expressed BMP4 mRNA and protein and underwent osteogenic differentiation.
BMP4 signaling plays a role in the regulation of terminal differentiation of primary equine trophoblast cells via activation of the SMAD1 (show SMAD1 Proteins)/5 pathway
paracrine signals from the embryo, represented by FGF4 (show FGF4 Proteins) and BMP4, induce a response in the trophoblast prior to the extensive elongation.
The structure of porcine BMP4 gene is highly conservative with other mammalian BMP4 genes, but some differences may be present in the regulation of gene expression.
Altered shear stress stimulates upregulation of endothelial VCAM-1 (show VCAM1 Proteins) and ICAM-1 (show ICAM1 Proteins) in a BMP-4- and TGF-beta1 (show TGFB1 Proteins)-dependent pathway.
A microsatellite (ACn (show ACIN1 Proteins)) was identified in the 3' UTR of BMP4 gene.Prolificacy associated microsatellite (AC19 (show POLR1D Proteins)) was detected in Indian goats.
The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.
, bone morphogenetic protein 2B
, bone morphogenetic protein-4
, bone morphogenetic protein 4
, bone morphogenetic protein 4, isoform 3
, Bone morphogenetic protein 4
, bone morphogenetic protein 4-like