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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
endothelial BMP4 controls leukocyte recruitment through a VE-cadherin (zeige CDH5 Proteine)-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 (zeige MGP Proteine)) in patients who were admitted to emergency department with the diagnosis of acute coronary syndrome (ACS (zeige PLA2G15 Proteine)) and underwent primary percutaneous coronary intervention. MGP (zeige MGP Proteine) 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 (zeige BMP2 Proteine) (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.
cardiomyocyte (CM) conditioned medium can trigger the recruitment of pro-inflammatory (M1) macrophages, through a mechanism that involves, in part, CM-derived BMP4.
BMP4 participates in the regulation of invasion and migration by EC109/Taxol cells
Bone morphogenetic protein 4 regulates expression of microRNAs miR (zeige MLXIP Proteine)-494 and miR (zeige MLXIP Proteine)-126-5p to control endothelial cell function in angiogenesis.
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 (zeige SIN3B Proteine) splicing reveals a role for RBM39 (zeige RBM39 Proteine)
Gene expression profiling showed that MuSK (zeige MUSK Proteine) was required for the BMP4-induced expression of a subset of genes in myoblasts, including regulator of G protein signaling 4 (Rgs4 (zeige RGS4 Proteine)).
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 (zeige SLC27A4 Proteine)) cells
These results suggest how BMP4 regulates adipocyte recruitment in subcutaneous (SC) white adipose tissue, and thus promote its beneficial metabolic effects.
RUNX1T1 (zeige RUNX1T1 Proteine) serves as a common angiogenic driver for vaculogenesis and functionality of endothelial lineage cells
Expression of Bmp4 in the ureteric mesenchyme depends on HH signaling and Foxf1 (zeige FOXF1 Proteine), and that exogenous BMP4 rescued cell proliferation and epithelial differentiation in ureters with abrogated HH signaling or FOXF1 (zeige FOXF1 Proteine) function.
Structures of Bmp2a (zeige BMP2 Proteine), 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 (zeige GREM1 Proteine).
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 (zeige FSHR Proteine) while up-regulating lhr (zeige LHCGR Proteine) expression.
These data reveal a novel role for LRP1 (zeige LRP1 Proteine) 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 (zeige WNT2 Proteine)/beta-catenin (zeige CTNNB1 Proteine) signaling is both sufficient and required for the induction of BMP4 and Tbx2b expression in the AVC
identify Npnt (zeige NPNT Proteine) as a novel upstream regulator of Bmp4-Has2 (zeige HAS2 Proteine) signaling that plays a crucial role in AV canal differentiation
immature AVC expansion in wkm mutants is rescued by depleting Bmp4, indicating that Tmem2 (zeige TMEM2 Proteine) 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 (zeige OSR1 Proteine)/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 (zeige PIAS1 Proteine) proteins have differential ability to regulate signals from the growth factors activin, bone morphogenetic protein 4 (BMP4), and Wnt8 (zeige WNT8A Proteine).
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 (zeige BAMBI Proteine), SMAD6 (zeige SMAD6 Proteine), and SMAD7 (zeige SMAD7 Proteine) expand the dynamic BMP4 signaling range essential for proper embryonic patterning and reduce interindividual phenotypic and molecular variability in Xenopus embryos.
limits homeobox (zeige PRRX1 Proteine) gene expression in the organiser/non-organiser direction
X-epilectin expression is down-regulated by Noggin (zeige NOG Proteine) and tBR and that this effect is inhibited by BMP4 over-expression
BMP4-dependent expression of Xenopus Grainyhead-like 1 (zeige GRHL1 Proteine) 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 (zeige DDX4 Proteine) 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 (zeige SLC6A8 Proteine) cell growth
BMP4 during maturation increased the proportion of Oct-4 (zeige POU5F1 Proteine) 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 (zeige BMP7 Proteine) suppresses granulosa cell apoptosis by inhibiting the release of caspase-activated DNase (CAD (zeige DFFB Proteine)) 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 (zeige HSP70 Proteine) enhances vascular bone morphogenetic protein-4 signaling by binding matrix Gla protein (zeige MGP Proteine).
The TM-induced characteristic changes in the expression pattern of Hoxa11 (zeige HOXA11 Proteine) and Bmp4 on GDs (zeige PAEP Proteine) 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 (zeige BMP2 Proteine), BMP-4, and BMP-7 (zeige BMP7 Proteine), noggin (zeige NOG Proteine), and chordin (zeige CHRD Proteine) 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 (zeige SMAD1 Proteine)/5 pathway
paracrine signals from the embryo, represented by FGF4 (zeige FGF4 Proteine) 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 (zeige VCAM1 Proteine) and ICAM-1 (zeige ICAM1 Proteine) in a BMP-4- and TGF-beta1 (zeige TGFB1 Proteine)-dependent pathway.
A microsatellite (ACn (zeige ACIN1 Proteine)) was identified in the 3' UTR of BMP4 gene.Prolificacy associated microsatellite (AC19 (zeige POLR1D Proteine)) 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