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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
Vrtn binds a bmp2b regulatory sequence and acts as a repressor to inhibit its zygotic transcription.
Study found that BMP-2 is negatively regulated by miR (zeige MYLIP Proteine)-140 during early embryogenesis and bone development in zebra fi sh.
Data show that transcription of organizer-specific bone morphogenetic protein 2b (bmp2b) is directly down-regulated by Nodal and up-regulated by Wnt (zeige WNT2 Proteine) signal.
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).
Organizer-derived Bmp2 is required for the formation of a correct Bmp activity gradient during embryonic development.
BMP2b signaling in zebrafish embryos substantially decreases emergence of lymphatic endothelial cells.
Data show that BMP2B protein is expressed in a gradient as early as blastula stages.
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
The Bmp2b mutants and mosaic loss-of-function experiments reveal that BMP acts as a repressor of eye-field fate through inhibition of its key transcription factor Rx3, thereby protecting the future telencephalon from acquiring eye identity.
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
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
BMP4 levels are increased dramatically in individuals with impaired glucose tolerance and type 2 diabetes.
The results suggest that selective RNA decay via TGF-beta (zeige TGFB1 Proteine) and BMP4 signaling is critical for specifying the developmental fate of specific human embryonic cell lineages.
Expression of bone morphogenetic protein (BMP) 4, an upstream stimulator of SOX9, was upregulated by CG.
Study shows that BMP4 is overexpressed in hepatocellular carcinoma (HCC (zeige FAM126A Proteine)) tissues and BMP4-induced ID2/CDKN1B (zeige CDKN1B Proteine) signaling facilitates the proliferation of HCC (zeige FAM126A Proteine).
Data suggest pituitary cells secrete factor (TSP1) that binds to and inhibits action of BMP2 and BMP4; von Willebrand type C domain of TSP1 is likely responsible for this BMP2/4-binding activity. These studies were initially conducted using cultured cells from ovine pituitary gland and mouse cell line; interactions were confirmed using recombinant human proteins. (TSP1 = thrombospondin-1; BMP = bone morphogenetic protein)
we demonstrate that expression of bone morphogenetic protein 4 (BMP-4) is universally upregulated in human colorectal cancer cells and tissues, resulting in activated BMP signaling
RUNX1T1 (zeige RUNX1T1 Proteine) serves as a common angiogenic driver for vaculogenesis and functionality of endothelial lineage cells
Phosphorylated Smad1/5/8/9 specifically bound to the BREs of Smad8/9 gene. The present study reveals that Smad8/9 is a unique R-Smad regulated through the BMP pathway at the mRNA level.
Meta-analysis to assess the effect of BMP4 rs17563 polymorphism on nonsyndromic cleft lip with or without cleft palate (NSCL (zeige NHLH1 Proteine)/P) suggests that the C allele of BMP4 rs17563 may be a risk factor for NSCL (zeige NHLH1 Proteine)/P among Asians and Caucasians, and may be a protective factor for NSCL (zeige NHLH1 Proteine)/P in Brazilian population.
this study identified BMP-4 as a potential molecular marker for predicting the invasion and progression of papillary thyroid carcinoma
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.
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.
the effect of titanium (Ti) with nanotopography (Nano) on the endogenous expression of BMP-2 (zeige BMP2 Proteine) and BMP-4 and the relevance of this process to the nanotopography-induced osteoblast differentiation.
These data indicate that Foxc1 (zeige FOXC1 Proteine) expression is regulated by BMP4 and FOXC1 (zeige FOXC1 Proteine) functions in the commitment of progenitor cells to the osteoblast fate and its expression is reduced when differentiation proceeds.
Treatment of ES cells with TPO (zeige THPO Proteine) induced the autocrine production of BMP4 with concomitant upregulation of the BMP receptor BMPR1A (zeige BMPR1A Proteine), phosphorylation of SMAD1 (zeige SMAD1 Proteine), 5, 8, and activation of specific BMP4 target genes; this was mediated by TPO (zeige THPO Proteine)-dependent binding of transcription factor HIF-1alpha (zeige HIF1A Proteine) to the BMP4 gene promoter.
Data suggest that ovarian Bmp4 levels are significantly decreased in a mouse model of polycystic ovary syndrome with hyperandrogenism; androgens inhibited Bmp4 expression via activation of androgen receptors; Smad4 (zeige SMAD4 Proteine) signaling rather than p38 MAPK (zeige MAPK14 Proteine) pathway regulates androgen and estrogen formation.
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).
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.
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.
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.
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-4
, bone morphogenetic protein 4
, bone morphogenetic protein 4, isoform 3
, Bone morphogenetic protein 4
, bone morphogenetic protein 4-like
, bone morphogenetic protein 2
, bone morphogenetic protein 2B