Activin Receptors: Receptors for ACTIVINS are membrane protein kinases belonging to the family of PROTEIN-SERINE-THREONINE KINASES, thus also named activin receptor-like kinases (ALK's). Activin receptors also bind TRANSFORMING GROWTH FACTOR BETA. As those transmembrane receptors of the TGF-beta superfamily (RECEPTORS, TRANSFORMING GROWTH FACTOR BETA), ALK's consist of two different but related protein kinases, Type I and Type II. Activins initiate cellular signal transduction by first binding to the type II receptors (ACTIVIN RECEPTORS, TYPE II ) which then recruit and phosphorylate the type I receptors (ACTIVIN RECEPTORS, TYPE I ) with subsequent activation of the type I kinase activity.Activin Receptors, Type II: One of the two types of ACTIVIN RECEPTORS. They are membrane protein kinases belonging to the family of PROTEIN-SERINE-THREONINE KINASES. The major type II activin receptors are ActR-IIA and ActR-IIB.Activins: Activins are produced in the pituitary, gonads, and other tissues. By acting locally, they stimulate pituitary FSH secretion and have diverse effects on cell differentiation and embryonic development. Activins are glycoproteins that are hetero- or homodimers of INHIBIN-BETA SUBUNITS.Activin Receptors, Type I: One of the two types of ACTIVIN RECEPTORS or activin receptor-like kinases (ALK'S). There are several type I activin receptors. The major active ones are ALK-2 (ActR-IA) and ALK-4 (ActR-IB).Inhibins: Glycoproteins that inhibit pituitary FOLLICLE STIMULATING HORMONE secretion. Inhibins are secreted by the Sertoli cells of the testes, the granulosa cells of the ovarian follicles, the placenta, and other tissues. Inhibins and ACTIVINS are modulators of FOLLICLE STIMULATING HORMONE secretions; both groups belong to the TGF-beta superfamily, as the TRANSFORMING GROWTH FACTOR BETA. Inhibins consist of a disulfide-linked heterodimer with a unique alpha linked to either a beta A or a beta B subunit to form inhibin A or inhibin B, respectivelyInhibin-beta Subunits: They are glycopeptides and subunits in INHIBINS and ACTIVINS. Inhibins and activins belong to the transforming growth factor beta superfamily.Follistatin: A broadly distributed protein that binds directly to ACTIVINS. It functions as an activin antagonist, inhibits FOLLICLE STIMULATING HORMONE secretion, regulates CELL DIFFERENTIATION, and plays an important role in embryogenesis. Follistatin is a single glycosylated polypeptide chain of approximately 37-kDa and is not a member of the inhibin family (INHIBINS). Follistatin also binds and neutralizes many members of the TRANSFORMING GROWTH FACTOR BETA family.Receptors, Growth Factor: Cell surface receptors that bind growth or trophic factors with high affinity, triggering intracellular responses which influence the growth, differentiation, or survival of cells.Myostatin: A growth differentiation factor that is a potent inhibitor of SKELETAL MUSCLE growth. It may play a role in the regulation of MYOGENESIS and in muscle maintenance during adulthood.Smad2 Protein: A receptor-regulated smad protein that undergoes PHOSPHORYLATION by ACTIVIN RECEPTORS, TYPE I. It regulates TRANSFORMING GROWTH FACTOR BETA and ACTIVIN signaling.Receptors, Transforming Growth Factor beta: Cell-surface proteins that bind transforming growth factor beta and trigger changes influencing the behavior of cells. Two types of transforming growth factor receptors have been recognized. They differ in affinity for different members of the transforming growth factor beta family and in cellular mechanisms of action.Nodal Protein: The founding member of the nodal signaling ligand family of proteins. Nodal protein was originally discovered in the region of the mouse embryo primitive streak referred to as HENSEN'S NODE. It is expressed asymmetrically on the left side in chordates and plays a critical role in the genesis of left-right asymmetry during vertebrate development.Transforming Growth Factor beta: A factor synthesized in a wide variety of tissues. It acts synergistically with TGF-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. TGF-beta has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. TGF-beta is found mostly as homodimer forms of separate gene products TGF-beta1, TGF-beta2 or TGF-beta3. Heterodimers composed of TGF-beta1 and 2 (TGF-beta1.2) or of TGF-beta2 and 3 (TGF-beta2.3) have been isolated. The TGF-beta proteins are synthesized as precursor proteins.Bone Morphogenetic Proteins: Bone-growth regulatory factors that are members of the transforming growth factor-beta superfamily of proteins. They are synthesized as large precursor molecules which are cleaved by proteolytic enzymes. The active form can consist of a dimer of two identical proteins or a heterodimer of two related bone morphogenetic proteins.Smad Proteins: A family of proteins that are involved in the translocation of signals from TGF-BETA RECEPTORS; BONE MORPHOGENETIC PROTEIN RECEPTORS; and other surface receptors to the CELL NUCLEUS. They were originally identified as a class of proteins that are related to the mothers against decapentaplegic protein, Drosophila and sma proteins from CAENORHABDITIS ELEGANS.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Growth Differentiation Factors: A family of BONE MORPHOGENETIC PROTEIN-related proteins that are primarily involved in regulation of CELL DIFFERENTIATION.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Mesoderm: The middle germ layer of an embryo derived from three paired mesenchymal aggregates along the neural tube.Smad3 Protein: A receptor-regulated smad protein that undergoes PHOSPHORYLATION by ACTIVIN RECEPTORS, TYPE I. Activated Smad3 can bind directly to DNA, and it regulates TRANSFORMING GROWTH FACTOR BETA and ACTIVIN signaling.Bone Morphogenetic Protein Receptors, Type I: A subtype of bone morphogenetic protein receptors with high affinity for BONE MORPHOGENETIC PROTEINS. They can interact with and undergo PHOSPHORYLATION by BONE MORPHOGENETIC PROTEIN RECEPTORS, TYPE II. They signal primarily through RECEPTOR-REGULATED SMAD PROTEINS.Smad4 Protein: A signal transducing adaptor protein and tumor suppressor protein. It forms a complex with activated RECEPTOR-REGULATED SMAD PROTEINS. The complex then translocates to the CELL NUCLEUS and regulates GENETIC TRANSCRIPTION of target GENES.Embryonic Induction: The complex processes of initiating CELL DIFFERENTIATION in the embryo. The precise regulation by cell interactions leads to diversity of cell types and specific pattern of organization (EMBRYOGENESIS).Growth Substances: Signal molecules that are involved in the control of cell growth and differentiation.Xenopus Proteins: Proteins obtained from various species of Xenopus. Included here are proteins from the African clawed frog (XENOPUS LAEVIS). Many of these proteins have been the subject of scientific investigations in the area of MORPHOGENESIS and development.Protein-Serine-Threonine Kinases: A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.Gene Expression Regulation, Developmental: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action during the developmental stages of an organism.Myositis Ossificans: A disease characterized by bony deposits or the ossification of muscle tissue.In Situ Hybridization: A technique that localizes specific nucleic acid sequences within intact chromosomes, eukaryotic cells, or bacterial cells through the use of specific nucleic acid-labeled probes.Xenopus: An aquatic genus of the family, Pipidae, occurring in Africa and distinguished by having black horny claws on three inner hind toes.Bone Morphogenetic Protein Receptors, Type II: A subtype of bone morphogenetic protein receptors with low affinity for BONE MORPHOGENETIC PROTEINS. They are constitutively active PROTEIN-SERINE-THREONINE KINASES that can interact with and phosphorylate TYPE I BONE MORPHOGENETIC PROTEIN RECEPTORS.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Trans-Activators: Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.Granulosa Cells: Supporting cells for the developing female gamete in the OVARY. They are derived from the coelomic epithelial cells of the gonadal ridge. Granulosa cells form a single layer around the OOCYTE in the primordial ovarian follicle and advance to form a multilayered cumulus oophorus surrounding the OVUM in the Graafian follicle. The major functions of granulosa cells include the production of steroids and LH receptors (RECEPTORS, LH).Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Embryo, Nonmammalian: The developmental entity of a fertilized egg (ZYGOTE) in animal species other than MAMMALS. For chickens, use CHICK EMBRYO.Ovary: The reproductive organ (GONADS) in female animals. In vertebrates, the ovary contains two functional parts: the OVARIAN FOLLICLE for the production of female germ cells (OOGENESIS); and the endocrine cells (GRANULOSA CELLS; THECA CELLS; and LUTEAL CELLS) for the production of ESTROGENS and PROGESTERONE.Reverse Transcriptase Polymerase Chain Reaction: A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.Body Patterning: The processes occurring in early development that direct morphogenesis. They specify the body plan ensuring that cells will proceed to differentiate, grow, and diversify in size and shape at the correct relative positions. Included are axial patterning, segmentation, compartment specification, limb position, organ boundary patterning, blood vessel patterning, etc.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Follicle Stimulating Hormone, beta Subunit: The beta subunit of follicle stimulating hormone. It is a 15-kDa glycopolypeptide. Full biological activity of FSH requires the non-covalently bound heterodimers of an alpha and a beta subunit. Mutation of the FSHB gene causes delayed puberty, or infertility.Proteoglycans: Glycoproteins which have a very high polysaccharide content.Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents.Goosecoid Protein: Goosecoid protein is a homeodomain protein that was first identified in XENOPUS. It is found in the SPEMANN ORGANIZER of VERTEBRATES and plays an important role in neuronal CELL DIFFERENTIATION and ORGANOGENESIS.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Receptors, Cell Surface: Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.

Activin and TGFbeta limit murine primordial germ cell proliferation. (1/240)

Mammalian primordial germ cells (PGCs) proliferate as they migrate from their initial location in the extraembryonic mesoderm to the genital ridge, the gonadal anlage. Once in the genital ridge, PGCs cease dividing and differentiate according to their gender. To identify ligands that might limit PGC proliferation, we analyzed growth factor receptors encoded in RNA obtained from purified germ cells shortly after their arrival in the genital ridge. Receptors for two members of the TGFbeta superfamily were found, TGFbeta1 and activin. As the signal-transducing domains of both receptor systems are highly conserved, the effects of both TGFbeta1 and activin on PGCs would be expected to be similar. We found that both ligands limited the accumulation of germ cells in primary PGC cultures. BrdU incorporation assays demonstrated that either ligand inhibits PGC proliferation. These results suggest that these signal transduction pathways are important elements of the mechanism that determines germ cell endowment.  (+info)

Expression of inhibin/activin subunits and their receptors and binding proteins in human preimplantation embryos. (2/240)

PURPOSE: Our purpose was to study the role of inhibin/activin during embryogenesis. METHODS: Transcripts of inhibin/activin subunits (alpha, beta A, beta B), activin receptors (types I and II), and follistatin were detected by a reverse transcriptase-polymerase chain reaction in human reproductive cells and preembryos cultured alone or co-cultured with human endometrial cells. RESULTS: Transcripts of alpha, beta A, beta B subunits were all detected in granulosa luteal cells, but only beta A units were detected in endometrial stromal and decidualized cells. In human preimplantation embryos, none of these subunits were detected in embryos from the four-cell to the morula stage and only beta A subunits were detectable in blastocyst embryos. Activin receptors were detectable in all of the studied embryos and cells. Transcripts of beta A, activin receptors, and follistatin were differentially expressed in human preimplantation embryos cultured in vitro and their expressions were significantly enhanced with the presence of endometrial stromal cells. CONCLUSIONS: Our data suggest that there is a possible endometrium-embryo interaction via endometrial activins and preimplantation embryo receptors and that the embryonic expressions of these activins, their receptors, and binding proteins are dependent on embryonic stage.  (+info)

Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1. (3/240)

Germ line mutations in one of two distinct genes, endoglin or ALK-1, cause hereditary hemorrhagic telangiectasia (HHT), an autosomal dominant disorder of localized angiodysplasia. Both genes encode endothelial cell receptors for the transforming growth factor beta (TGF-beta) ligand superfamily. Endoglin has homology to the type III receptor, betaglycan, although its exact role in TGF-beta signaling is unclear. Activin receptor-like kinase 1 (ALK-1) has homology to the type I receptor family, but its ligand and corresponding type II receptor are unknown. In order to identify the ligand and type II receptor for ALK-1 and to investigate the role of endoglin in ALK-1 signaling, we devised a chimeric receptor signaling assay by exchanging the kinase domain of ALK-1 with either the TGF-beta type I receptor or the activin type IB receptor, both of which can activate an inducible PAI-1 promoter. We show that TGF-beta1 and TGF-beta3, as well as a third unknown ligand present in serum, can activate chimeric ALK-1. HHT-associated missense mutations in the ALK-1 extracellular domain abrogate signaling. The ALK-1/ligand interaction is mediated by the type II TGF-beta receptor for TGF-beta and most likely through the activin type II or type IIB receptors for the serum ligand. Endoglin is a bifunctional receptor partner since it can bind to ALK-1 as well as to type I TGF-beta receptor. These data suggest that HHT pathogenesis involves disruption of a complex network of positive and negative angiogenic factors, involving TGF-beta, a new unknown ligand, and their corresponding receptors.  (+info)

Bone morphogenetic proteins regulate the developmental program of human hematopoietic stem cells. (4/240)

The identification of molecules that regulate human hematopoietic stem cells has focused mainly on cytokines, of which very few are known to act directly on stem cells. Recent studies in lower organisms and the mouse have suggested that bone morphogenetic proteins (BMPs) may play a critical role in the specification of hematopoietic tissue from the mesodermal germ layer. Here we report that BMPs regulate the proliferation and differentiation of highly purified primitive human hematopoietic cells from adult and neonatal sources. Populations of rare CD34(+)CD38(-)Lin- stem cells were isolated from human hematopoietic tissue and were found to express the BMP type I receptors activin-like kinase (ALK)-3 and ALK-6, and their downstream transducers SMAD-1, -4, and -5. Treatment of isolated stem cell populations with soluble BMP-2, -4, and -7 induced dose-dependent changes in proliferation, clonogenicity, cell surface phenotype, and multilineage repopulation capacity after transplantation in nonobese diabetic/severe combined immunodeficient (NOD/SCID) mice. Similar to transforming growth factor beta, treatment of purified cells with BMP-2 or -7 at high concentrations inhibited proliferation yet maintained the primitive CD34(+)CD38(-) phenotype and repopulation capacity. In contrast, low concentrations of BMP-4 induced proliferation and differentiation of CD34(+) CD38(-)Lin- cells, whereas at higher concentrations BMP-4 extended the length of time that repopulation capacity could be maintained in ex vivo culture, indicating a direct effect on stem cell survival. The discovery that BMPs are capable of regulating repopulating cells provides a new pathway for controlling human stem cell development and a powerful model system for studying the biological mechanism of BMP action using primary human cells.  (+info)

A quantitative analysis of signal transduction from activin receptor to nucleus and its relevance to morphogen gradient interpretation. (5/240)

Previous work has shown that Xenopus blastula cells sense activin concentration by assessing the absolute number of occupied receptors per cell (100 and 300 molecules of bound activin activate Xbra and Xgsc transcription, respectively; a difference of only 3-fold). We now ask how quantitative differences in the absolute number of occupied receptors lead to the qualitatively distinct gene responses in the nucleus through SMAD2, a transducer of concentration-dependent gene responses to activin. We show that the injection of 0.2 or 0.6 ng of Smad2 mRNA activates Xbra or Xgsc transcription, respectively, involving, again, only a 3-fold difference. Furthermore, Xbra transcription is down-regulated by overexpression of SMAD2 as it is after activin signaling. We have developed a method to isolate nuclei from animal cap cells and subsequently have quantified the amount of nuclear SMAD2 protein. We find that the injection of 0.2 or 0.6 ng of Smad2 mRNA into an egg leads to only a 3-fold difference in the amount of SMAD2 protein in the nuclei of the blastula cells that express Xbra or Xgsc. We conclude that a 3-fold difference in the absolute number of occupied activin receptors can be maintained only as a 3-fold difference in the level of nuclear SMAD2 protein. Therefore, in this example of morphogen action, there appears to be no amplification of a key cytoplasmic transduction response, and a small but developmentally important change in extracellular signal concentration is relayed directly to the nucleus.  (+info)

Activin family members in the developing chick retina: expression patterns, protein distribution, and in vitro effects. (6/240)

We have investigated whether the activin family of growth factors is involved in the regulation of retinal cell differentiation. Immunocytochemistry and in situ hybridization have shown that activin/inhibin subunits alpha, betaA, and betaB; receptors II and IIB; follistatin; and a follistatin-like gene are expressed in different regions of the chick embryo retina in developmentally regulated patterns. When tested in dissociated retinal cultures, activin did not appear to affect cell survival or proliferation, but it exerted marked inhibitory effects on the differentiation of photoreceptors, while stimulating the differentiation of nonphotoreceptor neurons; both effects were concentration-dependent and follistatin-sensitive. The results are consistent with the possibility that activin family members play significant roles in the regulation of retinal development.  (+info)

Smad3 inhibits transforming growth factor-beta and activin signaling by competing with Smad4 for FAST-2 binding. (7/240)

Transcriptional regulation by transforming growth factor-beta and activin is mediated by interaction of Smad2 and Smad3 with specific transcription factors and/or DNA elements. However, Smad3 behaves differently from Smad2 in regulating transcription by a winged-helix transcription factor, FAST-2, on an activin-responsive element (ARE) in the Xenopus Mix.2 promoter. Smad3 alone was able to stimulate the ARE through FAST-2, but inhibited the ARE transactivation mediated by Smad2/Smad4 following receptor activation. We characterized the functional domains that are involved in these two activities of Smad3. Deletion of the MH1 domain as well as mutations of four lysine residues in the MH1 domain abrogated the inhibitory activity of Smad3, but did not compromise the self-stimulatory function. In contrast, deletion of the MH2 domain or a point mutation of glycine 379 within this domain obliterated the self-stimulatory activity of Smad3, but not the inhibitory activity. In an electrophoretic mobility shift assay, we found that Smad3 was able to associate with the FAST-2.ARE complex and that this association was dependent on FAST-2. In addition, Smad3 was not able to directly bind the ARE in a DNase I protection assay, in which FAST-2 binds the ARE around a motif (TGTGTATT) previously characterized to associate with the human FAST-1 protein. Interestingly, Smad4 was also able to directly associate with the FAST-2.ARE complex through binding with FAST-2. In a gel shift assay, the association of FAST-2 with Smad4 was mutually exclusive from the association with Smad3. Taken together, these data indicate that Smad3 exerts the inhibitory activity by competitive association with FAST-2.  (+info)

Human activin-A is expressed in the atherosclerotic lesion and promotes the contractile phenotype of smooth muscle cells. (8/240)

Activin is a member of the transforming growth factor-beta superfamily, and it modulates the proliferation and differentiation of various target cells. In this study, we investigated the role of activin in the initiation and progression of human atherosclerosis. The expression of activin, its physiological inhibitor follistatin, and activin receptors were assayed in human vascular tissue specimens that represented various stages of atherogenesis. In situ hybridization experiments revealed activin mRNA in endothelial cells and macrophages and a strong induction of activin expression in neointimal smooth muscle cells from the early onset of atherogenesis. We developed an "in situ free-activin binding assay" by using biotinylated follistatin, which allowed us to detect bioactive activin at specific sites in atherosclerotic lesions. The mRNAs encoding the activin receptors are expressed similarly in normal and atherosclerotic tissue, which indicates that activin-A signaling in atherogenesis is most likely dependent on changes in growth factor concentrations rather than on receptor levels. In vitro, activin induces the contractile, nonproliferative phenotype in cultured smooth muscle cells, as is reflected by increased expression of smooth muscle-specific markers (SMalpha-actin and SM22alpha). Our data provide evidence that activin induces redifferentiation of neointimal smooth muscle cells, and we hypothesize that activin is involved in plaque stabilization.  (+info)

TGF-β 3 superfamily is a group of multifunctional cytokines that affect cell growth, differentiation, apoptosis, and morphogenesis (1, 2, 3) . This family consists of ,40 family members, including TGF-βs, activins, and BMPs. TGF-β superfamily ligands induce heteromeric complex formation of cognate type II and type I serine/threonine kinase receptors. Type II receptor kinases then phosphorylate serine and threonine residues in the GS domain of type I receptors, which results in the activation of type I receptor kinases (4) . Activated type I receptors signal into cytoplasm through phosphorylation of Smad proteins. Thus far, eight mammalian Smad proteins have been identified. Smad1, Smad2, Smad3, Smad5, and Smad8 are R-Smads, which are directly phosphorylated by type I receptors. Smad2 and Smad3 are activated by the TGF-β type I receptor and the activin type IB receptor, whereas Smad1, Smad5, and Smad8 are activated by BMP type I receptors and activin receptor-like kinase 1. Smad4 is a Co-Smad ...
8.0 8.1 Bauer, H et al. (2001) The type I serine/threonine kinase receptor Alk8/Lost-a-fin is required for Bmp2b/7 signal transduction during dorsoventral patterning of the zebrafish embryo. Development 128 849-58 PubMed GONUTS page ...
rat Habrec1 receptor: a TGF-beta type I serine/threonine kinase receptor with a partially unique pattern of expression in the developing organism and adult; amino acid sequence given in first source
On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6.
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BACKGROUND: Bone morphogenetic proteins (BMPs) are key regulators in the embryonic development and postnatal tissue homeostasis in all animals. Loss of function or dysregulation of BMPs results in severe diseases or even lethality. Like transforming growth factors beta (TGF-betas), activins, growth and differentiation factors (GDFs) and other members of the TGF-beta superfamily, BMPs signal by assembling two types of serine/threonine-kinase receptor chains to form a hetero-oligomeric ligand-receptor complex. BMP ligand receptor interaction is highly promiscuous, i.e. BMPs bind more than one receptor of each subtype, and a receptor bind various ligands. The activin type II receptors are of particular interest, since they bind a large number of diverse ligands. In addition they act as high-affinity receptors for activins but are also low-affinity receptors for BMPs. ActR-II and ActR-IIB therefore represent an interesting example how affinity and specificity might be generated in a promiscuous ...
Type I receptor for TGF-beta family ligands BMP9/GDF2 and BMP10 and important regulator of normal blood vessel development. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. May bind activin as well.
On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP-7, BMP-2 and, less efficiently, BMP-4. Binding is weak but enhanced by the presence of type I receptors for BMPs ...
Supplier: ProMab Technologies Type of Product: Monoclonal Antibody Description: The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activi
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TY - JOUR. T1 - RAP-011, an activin receptor ligand trap, increases hemoglobin concentration in hepcidin transgenic mice. AU - Langdon, Jacqueline M.. AU - Barkataki, Sangjucta. AU - Berger, Alan E.. AU - Cheadle, Chris. AU - Xue, Qian Li. AU - Sung, Victoria. AU - Roy, Cindy N.. PY - 2015/1/1. Y1 - 2015/1/1. N2 - Over expression of hepcidin antimicrobial peptide is a common feature of iron-restricted anemia in humans. We investigated the erythroid response to either erythropoietin or RAP-011, a "murinized" ortholog of sotatercept, in C57BL/6 mice and in hepcidin antimicrobial peptide 1 over expressing mice. Sotatercept, a soluble, activin receptor type IIA ligand trap, is currently being evaluated for the treatment of anemias associated with chronic renal disease, myelodysplastic syndrome, β-thalassemia, and Diamond Blackfan anemia and acts by inhibiting signaling downstream of activin and other Transforming Growth Factor-β superfamily members. We found that erythropoietin and RAP-011 ...
Rabbit Polyclonal Anti-Activin RIA/ALK-2/Activin Receptor Type 1 Antibody. Validated: WB, IHC, IHC-Fr. Tested Reactivity: Mouse, Rat, Human, and more. 100% Guaranteed.
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Activin Receptor Type IIA兔多克隆抗体(ab124072)可与小鼠样本反应并经WB实验严格验证。所有产品均提供质保服务,中国75%以上现货。
References for Abcams Recombinant Human Activin Receptor Type IIA protein (ab114449). Please let us know if you have used this product in your publication
Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally…
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The TGF-beta/activin/BMP superfamily of growth factors signals through heteromeric receptor complexes of type I and type II serine/threonine kinase receptors. The signal originated by TGF-beta-like molecules appears to be transduced by a set of evolutionarily conserved proteins known as SMADs, which upon activation directly translocate to the nucleus where they may activate transcription. Five SMAD proteins have so far been characterized in vertebrates. These factors are related to the mediator of decapentaplegic (dpp) signalling, mothers against dpp (Mad), in Drosophila and to the Sma genes from Caenorhabditis elegans. Smad1 and Smad2 have been shown to mimic the effects of BMP and activin, respectively, both in Xenopus and in mammalian cells, whereas Smad3 (a close homologue of Smad2) and the related protein DPC4, a tumour-suppressor gene product, mediate TGF-beta actions. We report here that DPC4 is essential for the function of Smad1 and Smad2 in pathways that signal mesoderm induction and ...
Signaling by the TGF-β superfamily is important in the regulation of hematopoiesis and is dysregulated in myelodysplastic syndromes (MDSs), contributing to ineffective hematopoiesis and clinical cytopenias. TGF-β, activins, and growth differentiation factors exert inhibitory effects on red cell formation by activating canonical SMAD2/3 pathway signaling. In this Review, we summarize evidence that overactivation of SMAD2/3 signaling pathways in MDSs causes anemia due to impaired erythroid maturation. We also describe the basis for biological activity of activin receptor ligand traps, novel fusion proteins such as luspatercept that are promising as erythroid maturation agents to alleviate anemia and related comorbidities in MDSs and other conditions characterized by impaired erythroid maturation.. ...
Signaling by the TGF-β superfamily is important in the regulation of hematopoiesis and is dysregulated in myelodysplastic syndromes (MDSs), contributing to ineffective hematopoiesis and clinical cytopenias. TGF-β, activins, and growth differentiation factors exert inhibitory effects on red cell formation by activating canonical SMAD2/3 pathway signaling. In this Review, we summarize evidence that overactivation of SMAD2/3 signaling pathways in MDSs causes anemia due to impaired erythroid maturation. We also describe the basis for biological activity of activin receptor ligand traps, novel fusion proteins such as luspatercept that are promising as erythroid maturation agents to alleviate anemia and related comorbidities in MDSs and other conditions characterized by impaired erythroid maturation.. ...
In recent years, a significant amount of research has examined the controversial role of activin A in cancer. Activin A, a member of the transforming growth factor β (TGFβ) superfamily, is best characterized for its function during embryogenesis in mesoderm cell fate differentiation and reproduction. During embryogenesis, TGFβ superfamily ligands, TGFβ, bone morphogenic proteins (BMPs) and activins, act as potent morphogens. Similar to TGFβs and BMPs, activin A is a protein that is highly systemically expressed during early embryogenesis; however, post-natal expression is overall reduced and remains under strict spatiotemporal regulation. Of importance, normal post-natal expression of activin A has been implicated in the migration and invasive properties of various immune cell types, as well as endometrial cells. Aberrant activin A signaling during development results in significant morphological defects and premature mortality. Interestingly, activin A has been found to have both oncogenic and
J:22651 Manova K, De Leon V, Angeles M, Kalantry S, Giarre M, Attisano L, Wrana J, Bachvarova RF, mRNAs for activin receptors II and IIB are expressed in mouse oocytes and in the epiblast of pregastrula and gastrula stage mouse embryos. Mech Dev. 1995 Jan;49(1-2):3-11 ...
ACVR2B antibody to detect human activin receptor type-2B. Validated on up to 12 cell lysates for western blotting. Try a trial size today.
Cripto is an EGF-CFC or epidermal growth factor-CFC, which is encoded by the Cryptic family 1 gene. Cryptic family protein 1B is a protein that in humans is encoded by the CFC1B gene. Cryptic family protein 1B acts as a receptor for the TGF beta signaling pathway. It has been associated with the translation of an extracellular protein for this pathway. The extracellular protein which Cripto encodes plays a crucial role in the development of left and right division of symmetry. Mutations of it could cause congenital heart disease. Crypto is a glycosylphosphatidylinositol-anchored co-receptor that binds nodal and the activin type I ActRIB (ALK)-4 receptor (ALK4). Cripto is composed of two adjacent cysteine-rich motifs: the EGF-like and the CFC of an N-terminal signal peptide and of a C-terminal hydrophobic region attached by a GPI anchor, which makes it a potentially essential element in the signaling pathway directing vertebrate embryo development. NMR data confirm that the CFC domain has a ...
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The "book" length of a punt is not the same as its physical distance. Hal kicked the "baptismal competitive punt" 90 yards in the air, but was only credited with a 40-yard punt. Because the line of scrimmage was Syracuses 40, and Hal kicked the ball through the end zone, the punt is recorded as 40 yards (the distance from the line of scrimmage to the end zone). The ball would be placed at Syracuses 20, so the "net" on the punt would only have been 20 yards. 90-yard punt ...
The IUPHAR/BPS Guide to Pharmacology. activin AB ligand page. Quantitative data and detailed annnotation of the targets of licensed and experimental drugs.
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ACTR1B山羊多克隆抗体(ab13802)可与人样本反应并经WB实验严格验证,被1篇文献引用。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
Activin Receptor Type IA (ACVR1) Antibody (Center N153), Purified Rabbit Polyclonal Antibody (Pab) validated in WB, IHC-P, E (AP7101A), Abgent
There are no specific protocols for Recombinant Human Activin Receptor Type IA protein (Fc Chimera) (ab83922). Please download our general protocols booklet
TY - JOUR. T1 - Loss of Heterozygosity and Mutational Analyses of the ACTRII Gene Locus in Human Colorectal Tumors. AU - Olaru, Andreea. AU - Mori, Yuriko. AU - Yin, Jing. AU - Wang, Suna. AU - Kimos, Martha C.. AU - Perry, Kellie. AU - Xu, Yan. AU - Sato, Fumiaki. AU - Selaru, Florin. AU - Deacu, Elena. AU - Sterian, Anca. AU - Shibata, David. AU - Abraham, John M.. AU - Meltzer, Stephen. PY - 2003/12. Y1 - 2003/12. N2 - The activin type II receptor gene (ACTRII) is mutated in 58.1% of microsatellite-unstable (MSI-H) colorectal cancers and is a close relative of the TGFβ-1 type II receptor, which is known to be involved in both MSI-H and non-MSI-H colorectal carcinogenesis. We therefore sought to determine whether ACTRII was involved in non-MSI-H colorectal cancers. We evaluated ACTRII inactivation by allelic deletion, loss of mRNA expression, or somatic mutation in 51 non-MSI-H colon cancers. Loss of heterozygosity (LOH) at the ACTRII locus (2q23.1) was found in 9 (17.6%) of 51 primary ...
Fig. 4. Hypertrophy response as measured via (A) body weight, (B) muscle weight change from sham group, after 4-wk treatment with ActRIIA-specific Ab, ActRIIB-specific Ab, combination thereof, and bimagrumab in SCID mice (n = 12 per group). Mice were untreated, sham group (white), or treated with weekly s.c. injection of isotype control antibody (20 mg/kg/wk) or of anti-ActRIIA Ab (CSJ089, blue, 6 or 20 mg/kg), an anti-ActRIIB Ab (CQI876, orange, 6 or 20 mg/kg), a combination of CSJ089 and CQI876 (black, 6 or 20 mg/kg of each Ab), or bimagrumab (green, 6 or 20 mg/kg). (C) Invasive muscle contractile function determination in gastrocnemius muscle of sham (white) and bimagrumab (green, 6 and 20 mg/kg)-treated groups, average of three stimulations. Hypertrophy response was measured through gastrocnemius and quadriceps muscle weight changes in SCID mice, (D) after 2-wk treatment with the same antibodies as in A, all dosed at 20 mg/kg, with CQI876 being also dosed at 100 mg/kg (orange crosses), (E) ...
Nodal is a secretory protein that in humans is encoded by the NODAL gene which is located on chromosome 10q22.1. It belongs to the Transforming Growth Factor (TGF-β) superfamily. Like many other members of this superfamily it is involved in cell differentiation in early embryogenesis, playing a key role in signal transfer from the node, in the anterior primitive streak, to lateral plate mesoderm (LPM). Nodal signaling is important very early in development for mesoderm and endoderm formation and subsequent organization of left-right axial structures. In addition, Nodal seems to have important functions in neural patterning, stem cell maintenance and many other developmental processes, including left/right handedness. Nodal can bind type I and type II Serine/Threonine kinase receptors, with Cripto-1 acting as its co-receptor. Signaling through SMAD 2/3 and subsequent translocation of SMAD 4 to the nucleus promotes the expression of genes involved in proliferation and differentiation. Nodal also ...
University at Buffalo researchers have identified a neural pathway that could hold a key to preventing relapse in individuals recovering from cocaine addiction. Their study focused on the activity of Activin receptors in the brain that are located in regions involved in pleasure and reward.. Published online June 1 in Nature Neuroscience, the study authored by Amy Gancarz, PhD, found that the Activin pathway controls the ability of cocaine to alter the connections between various neurons. By manipulating the activity of Activin receptors, researchers were able to change cocaine-taking behavior in animal models.. "Understanding this critical pathway will help us pursue new directions in potential pharmacological and gene therapies to prevent drug relapses," senior author David Dietz, PhD, assistant professor at the university medical schools Department of Pharmacology and Toxicology, said in a June 18 news release.. ...
Previous structures of activin in complex with type II receptor domains showed the growth factor in two very different interprotomer conformations when compared to each other and to the canonical TGF‐β family members (Thompson et al, 2003; Greenwald et al, 2004). The structures presented here further emphasise the flexibility of activin A (Figure 7C). While the uncomplexed activin A is very similar to the activin A in the type II receptor complex structure by Greenwald et al (2004), in the Fs12 complex, the growth factor exhibits a more closed structure. Here, the fingers rotate away from the other protomer, pulling with them the interfacial α‐helix. β‐strands 1 and 2, which show the largest displacement compared to free activin, move by more than 20 Å at the tip of the fingers.. With four independent crystal structures of activin now available, it is likely that the observed conformational divergence from the canonical TGF‐β structures is a reflection of true structural plasticity ...
View mouse Acvr2b Chr9:119402118-119434995 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
4213 Transforming growth factor-? (TGF-?) is a multifunctional cytokine which signals to the nucleus through cell surface transmembrane serine/threonine kinase receptors and cytoplasmic effectors, including Smad2, Smad3 and Smad4 proteins. The role of TGF-? in carcinogenesis is complex with tumor suppressor activities in early stages of disease and pro-oncogenic activities in advanced stages of invasive, metastatic disease. We recently identified a novel modulator of this pathway, TLP (TRAP-1-like protein), which associates with TGF-? receptors constitutively and with the common-mediator Smad4 upon ligand binding. We have shown that TLP regulates formation of Smad3/4 complexes and Smad3-dependent transcriptional responses. Since no inactivating mutations in Smad3 have been observed in human tumors, we hypothesized that proteins that regulate Smad3 function, such as TLP, rather than Smad3 itself might be direct targets of oncogenic change. To assess whether the expression of TLP might be ...
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This gene encodes an activin A type IB receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a hete
FGF signaling is very important to the forming of mesoderm in vertebrates, so when it really is perturbed in manifestation furthermore to its well-characterized part in maintaining manifestation. 1996; Horb and Thomsen, 1997; Zhang et al., 1998; Clements et al., 1999; Kofron et al., 1999; Xanthos et al., 2001). Many studies show that these indicators are essential for mesoderm development in Xenopus. Dominant unfavorable Activin receptors or inhibitory mRNA inhibit mesoderm development (Hemmati-Brivanlou and Melton, 1992; Chang et al., 1997; Bhushan et al., 1998; Casellas and Brivanlou, 1998). Likewise, inhibition of TGF ligands with non-cleavable precursors or by manifestation of nodal antagonists also prevent mesoderm development (Sunlight et al., 1999; Agius et al., 2000; Cheng et al., 2000; Tanegashima et al., 2000; Eimon and Harland, 2002; White et al., 2002). While nodal signaling is vital, FGF signaling also takes on a crucial GW 5074 part GW 5074 in mesoderm development, and an FGF ...
Anaemia is a clinical syndrome of blood characterized by decrease in the haemoglobin content in the red blood cells resulting in the marked reduction ..
Human Activin A is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays. MACS® GMP Recombinant Human Activin A is designed for ex vivo cell culture processing. No animal- or human-derived materials were used for the manufacture of this product, unless otherwise stated in the respective Certificate of Origin. The product is lyophilized without carrier protein or preservatives. - Sverige
Recombinant Activin A Receptor, Type IB (ACVR1B) Protein. Species: Mouse. Source: Escherichia coli (E. coli). Order product ABIN6301671.
... is a receptor in the TGF beta signaling pathway. It is also known as activin receptor-like kinase 1, or ALK1. This gene ... "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity". ... "Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors". ... "Entrez Gene: ACVRL1 activin A receptor type II-like 1". Olivieri C, Mira E, Delù G, Pagella F, Zambelli A, Malvezzi L, ...
2007). "Activin subunit and receptor expression in normal and cleft human fetal palate tissues". Pediatr. Dev. Pathol. 10 (6): ... 2005). "The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding". Dev. ... Walsh S, Metter EJ, Ferrucci L, Roth SM (2007). "Activin-type II receptor B (ACVR2B) and follistatin haplotype associations ... In the blood, activin and follistatin are both known to be involved in the inflammatory response following tissue injury or ...
Activin receptor type-2B is a protein that in humans is encoded by the ACVR2B gene. ACVR2B is an activin type 2 receptor. ... This gene encodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A type ... Schneider-Kolsky ME, Manuelpillai U, Waldron K, Dole A, Wallace EM (2002). "The distribution of activin and activin receptors ... II activin receptor genes during differentiation of human K562 cells and cDNA cloning of the human type IIB activin receptor". ...
... is an activin type 2 receptor. This gene encodes activin A type II receptor. Activins are dimeric growth and ... "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells". ... "Variations in activin receptor, inhibin/activin subunit and follistatin mRNAs in human prostate tumour tissues". Br. J. Cancer ... "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. ...
ACVR1 encodes activin receptor type-1, a BMP type-1 receptor. The mutation causes substitution of codon 206 from arginine to ... "ACVR1R206H receptor mutation causes fibrodysplasia ossificans progressiva by imparting responsiveness to activin A". stm. ... Regeneron announced new insight into the mechanism of disease involving the activation of the ACVR1 receptor by activin A. In ... The ACVR1 gene encodes a bone morphogenic protein (BMP) receptor; this gene is mutated in FOP. This protein is responsible for ...
January 2008). "MicroRNA miR-24 inhibits erythropoiesis by targeting activin type I receptor ALK4". Blood. 111 (2): 588-95. doi ...
"Characterization of type I receptors for transforming growth factor-beta and activin". Science. 264 (5155): 101-4. doi:10.1126/ ... 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 ... whereas type I receptors require their respective type II receptors for ligand binding. The BMPR1B receptor plays a role in the ... Bone morphogenetic protein receptor type-1B also known as CDw293 (cluster of differentiation w293) is a protein that in humans ...
These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members ... 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 ... "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity". ... the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors ...
A two-week treatment of normal mice with soluble activin type IIB receptor, a molecule that is normally attached to cells and ... Myostatin binds to the activin type II receptor, resulting in a recruitment of either coreceptor Alk-3 or Alk-4. This ... is thought that binding of myostatin to the soluble activin receptor prevents it from interacting with the cell-bound receptors ... "Regulation of muscle growth by multiple ligands signaling through activin type II receptors". Proceedings of the National ...
... resulting in phosphorylation of type I receptors by type II receptors. This gene encodes activin A type I receptor which ... Activin A receptor, type I (ACVR1) is a protein which in humans is encoded by the ACVR1 gene; also known as ALK-2 (activin ... ACVR1 encodes activin receptor type-1, a BMP type-1 receptor. The mutation causes the ACVR1 protein to have the amino acid ... "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity". ...
"Identification and characterization of a PDZ protein that interacts with activin type II receptors". J Biol Chem. 275 (8): 5485 ... 2003). "PKC regulates the delta2 glutamate receptor interaction with S-SCAM/MAGI-2 protein". Biochem. Biophys. Res. Commun. 301 ... 2001). "beta 1-adrenergic receptor association with the synaptic scaffolding protein membrane-associated guanylate kinase ... inverted-2 (MAGI-2). Differential regulation of receptor internalization by MAGI-2 and PSD-95". J. Biol. Chem. 276 (44): 41310- ...
2003). "Inhibin, activin, follistatin, activin receptors and beta-glycan gene expression in the placental tissue of patients ... Mathews LS, Vale WW (1991). "Expression cloning of an activin receptor, a predicted transmembrane serine kinase". Cell. 65 (6 ... 2003). "Activin betaC-subunit heterodimers provide a new mechanism of regulating activin levels in the prostate". Endocrinology ... 2001). "Localization of activin beta(A)-, beta(B)-, and beta(C)-subunits in humanprostate and evidence for formation of new ...
This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. ... Lebrun JJ, Takabe K, Chen Y, Vale W (January 1999). "Roles of pathway-specific and inhibitory Smads in activin receptor ... This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA ... O'Neill TJ, Zhu Y, Gustafson TA (April 1997). "Interaction of MAD2 with the carboxyl terminus of the insulin receptor but not ...
It is a TGFβ type 1 receptor antagonist. It blocks TGFβ1 and activin associating with the receptor, blocking access to SMAD2. ... By occupying type I receptors for Activin and bone morphogenetic protein (BMP), it also plays a role in negative feedback of ... Lebrun JJ, Takabe K, Chen Y, Vale W (January 1999). "Roles of pathway-specific and inhibitory Smads in activin receptor ... "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation". J. Biol ...
1997). "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells ... Mathews LS, Vale WW (1991). "Expression cloning of an activin receptor, a predicted transmembrane serine kinase". Cell. 65 (6 ... From these receptors β-glycan (the TGFß type III receptor) and InhBP/p120 (a membrane-tethered proteoglycan) were identified as ... 2001). "Localization of activin beta(A)-, beta(B)-, and beta(C)-subunits in humanprostate and evidence for formation of new ...
"The Interpretation of Position in a Morphogen Gradient as Revealed by Occupancy of Activin Receptors". Cell. 93: 557-568. doi: ... The low receptor occupancy permits increases in receptor occupancy which alter the cell fate, but the high receptor affinity ... Receptors which initiate cell fate transduction cascades, in early embryo development, exhibit a ratchet effect in response to ...
2001). "The orphan receptor ALK7 and the Activin receptor ALK4 mediate signaling by Nodal proteins during vertebrate ... The activin A receptor also known as ACVR1C or ALK-7 is a protein that in humans is encoded by the ACVR1C gene. ACVR1C is a ... 2006). "Activin receptor-like kinase 7 induces apoptosis through up-regulation of Bax and down-regulation of Xiap in normal and ... 2004). "Activin receptor-like kinase-7 induces apoptosis through activation of MAPKs in a Smad3-dependent mechanism in hepatoma ...
"Determination of type I receptor specificity by the type II receptors for TGF-beta or activin". Science. 262 (5135): 900-2. doi ... Oh SP, Seki T, Goss KA, Imamura T, Yi Y, Donahoe PK, Li L, Miyazono K, ten Dijke P, Kim S, Li E (March 2000). "Activin receptor ... It can also decrease the expression levels of cytokine receptors, such as the IL-2 receptor to down-regulate the activity of ... Many cells synthesize TGF-β and almost all of them have specific receptors for this peptide. TGF-β1, TGF-β2, and TGF-β3 all ...
BMP influences AV node development through Alk3 receptor (Activin receptor-like kinase 3). Abnormalities seen in BMP and Alk3 ... and Morphology in the Atrioventricular Node of Mice With Atrioventricular Canal-Targeted Deletion of Alk3/Bmpr1a Receptor". ...
In the cell surface Dapper2 tightly binds to the active form of the activin type 1 receptors and targets the receptor for ... Activation of the Nodal pathway involves nodal binding to activin and activin-like receptors which leads to phosphorylation of ... The binding of Nodal proteins to activin or activin-like serine/threonine kinase receptors results in the phosphorylation of ... Somehow the reduction of activin receptors would lead to the decrease in activity of different TGFb pathways. Smad proteins are ...
... and activin type II receptors balance BMP9 signals mediated by activin receptor-like kinase-1 in human pulmonary artery ... The physiological receptor of GDF2 is thought to be activin receptor-like kinase 1, ALK1 (also called ACVRL1), an endothelial- ... also known has Activin A receptor, type I (ACVR1), and the other type II receptors BMPRII and ActRIIA. GDF2 and BMP10 are the ... Endoglin, a type I membrane glycoprotein that forms the TGF-beta receptor complex, is a co-receptor of ALK1 for GDF2/BMP-9 ...
ACVRL1: activin A receptor type II-like 1. *CBX5: chromobox homolog 5 ... PTPN11: protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1). *KRAS: V-Ki-ras2 Kirsten rat sarcoma viral ...
Feijen A, Goumans MJ, van den Eijnden-van Raaij AJ (December 1994). "Expression of activin subunits, activin receptors and ... Feijen A, Goumans MJ, van den Eijnden-van Raaij AJ (December 1994). "Expression of activin subunits, activin receptors and ... TGF-β family receptors most commonly use the Smad signaling pathway to tranduce signals. Type 2 receptors are responsible for ... TGF-β receptors induce the MAPK signaling pathways of ERK, JNK and p38. BMP4 is also known to activate the ERK, JNK and p38 ...
... resulting in phosphorylation of type I receptors by type II receptors. This gene encodes activin A type IB receptor, composed ... "Truncated activin type I receptor Alk4 isoforms are dominant negative receptors inhibiting activin signaling". Mol. Endocrinol ... ACVR1B or ALK-4 acts as a transducer of activin or activin like ligands (e.g., inhibin) signals. Activin binds to either ACVR2A ... "The role of activin type I receptors in activin A-induced growth arrest and apoptosis in mouse B-cell hybridoma cells". Cell. ...
A truncated activin receptor inhibits mesoderm induction and formation of axial structures in Xenopus embryos. Nature 359:609 - ... Using dominant negative Activin receptors in Xenopus animal caps, it has been shown that FGF signaling is crucial for mesoderm ... Upon FGF binding to its receptor, FGFR, the receptor pair dimerizes and is transphosphorylated, enabling it to recruit proteins ... Members of the TGF-β superfamily, Activin and Nodal, are essential for mesodermal induction, while FGF and Wnt are in charge of ...
T4 and T3 bind to thyroid receptor proteins in the cell nucleus and cause metabolic effects through the control of DNA ...
Buy our Recombinant Human Activin Receptor Type IIB protein. Ab125577 is a protein fragment produced in Baculovirus infected ... Recombinant Human Activin Receptor Type IIB protein. See all Activin Receptor Type IIB proteins and peptides. ... Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD ... On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. ...
... transforms ACVR1 into an activin-responsive receptor.. (A) Activin signals via the type I receptors ACVR1B/1C and Smad2/3 ... Identification of human activin and TGFβ type I receptors that form heteromeric kinase complexes with type II receptors. Cell ... Anti-activin A blocking mAb blocks the activity of inhibin A-containing activins but not activin B. ... the receptor required stimulation by the endogenous ligand activin. Small sponges soaked with activin ossified after they were ...
... "Identification of a Novel Mutation in Activin Receptor Type 1 (ACVR1) in a Fibrodysplasia Ossificans Progressiva (FOP) Patient ... "Identification of a Novel Mutation in Activin Receptor Type 1 (ACVR1) in a Fibrodysplasia Ossificans Progressiva (FOP) Patient ... Identification of a novel mutation in activin receptor type 1 (ACVR1) in a fibrodysplasia ossificans progressiva (FOP) patient ...
2007). "Activin subunit and receptor expression in normal and cleft human fetal palate tissues". Pediatr. Dev. Pathol. 10 (6): ... 2005). "The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding". Dev. ... Walsh S, Metter EJ, Ferrucci L, Roth SM (2007). "Activin-type II receptor B (ACVR2B) and follistatin haplotype associations ... In the blood, activin and follistatin are both known to be involved in the inflammatory response following tissue injury or ...
Smad2 and Smad3 are activated by the TGF-β type I receptor and the activin type IB receptor, whereas Smad1, Smad5, and Smad8 ... Smad2 is a receptor-regulated Smad that participates specifically in TGF-β and activin signaling. Targeted disruption of Smad2 ... Smad2 is a receptor-regulated Smad that is activated specifically by transforming growth factor β and activin signaling. We ... Type II receptor kinases then phosphorylate serine and threonine residues in the GS domain of type I receptors, which results ...
The seven members of the BMP type-I receptor family, activin receptor-like kinase (ALK) 1-7, play critical roles in human ... In turn, the improper activation of these receptor pathways is responsible for a wide range of disease conditions. ... type-I receptor family, ALK2. La Jolla recently entered a worldwide, exclusive license agreement with Vanderbilt University ...
They transduce their signal via three different type I receptors, termed activin receptor-like kinase 2 (Alk2), Alk3, or bone ... They transduce their signal via three different type I receptors, termed activin receptor-like kinase 2 (Alk2), Alk3, or bone ... They transduce their signal via three different type I receptors, termed activin receptor-like kinase 2 (Alk2), Alk3, or bone ... They transduce their signal via three different type I receptors, termed activin receptor-like kinase 2 (Alk2), Alk3, or bone ...
7b, respectively), and the myostatin receptor, activin receptor type IIB (AcvR2B) (152%, P , 0.0005, Fig. 7e and 82%, P , 0.01 ... Mature myostatin (26 kDa), premature myostatin (52 kDa), and activin receptor type IIB (AcvR2B) protein levels were increased ... antibody for Activin Receptor Type IIB. Proteins were visualized by horseradish peroxidase-conjugated IgG antibodies (Santa ... growth hormone receptor gene disruption on mouse hindlimb muscle fiber type composition. Growth Hormon IGF Res. 2008;18:479-86. ...
Fst from 2mg/Vial Freeze-Dried Polypeptide Powder Follistatin 344 Activin-Binding Protein - Shanghai Shucan Industrial Co., Ltd ... China 2mg/Vial Freeze-Dried Polypeptide Powder Follistatin 344 Activin-Binding Protein, Find details about China Follistatin ... based on activin receptor type IIB (ActRIIB). The molecule inhibits signaling via the ActRIIB receptor binding ... FS is a high-affinity activin-binding protein that can act as an activin antagonist. Two alternatively spliced ...
GO:0032926 negative regulation of activin receptor signaling pathway GO:0048185 activin binding GO:0051798 positive regulation ... As well as activin, FST interacts with and inhibits other members of the transforming growth factor beta (TGF-beta) superfamily ... originally identified as an antagonist of activin and suppressor of follicle stimulating hormone (FSH) synthesis/secretion.. ...
Arteriovenous malformations in mice lacking activin receptor-like kinase-1. Nat Genet. 2000;26(3):328-331.. View this article ... or β3-adrenergic receptors (n = 5). SCR, scrambled siRNA. (L-N) Expression of (L) β1-, (M) β2-, or (N) β3-adrenergic receptors ... or β3-adrenergic receptors (n = 5). Data shown in H-J and L-N were analyzed by Students t test. Data shown in E, F, K, and O ... Constitutively active Notch4 receptor elicits brain arteriovenous malformations through enlargement of capillary-like vessels. ...
ACVR1R206H receptor mutation causes fibrodysplasia ossificans progressiva by imparting responsiveness to activin A. Sci Transl ... This neofunction of Activin-A raised the possibility that the inhibition of Activin-A signaling by Activin-A-specific- ... Characterization of the ligand binding functionality of the extracellular domain of activin receptor type IIb. J Biol Chem. ... del Re E, Sidis Y, Fabrizio DA, Lin HY, Schneyer A. Reconstitution and analysis of soluble inhibin and activin receptor ...
ACVR1 encodes activin receptor type-1, a BMP type-1 receptor. The mutation causes substitution of codon 206 from arginine to ... A mutation in the gene ACVR1 (also known as activin-like kinase 2 [ALK-2]) is responsible for the disease. ...
Patients with FOP harbor point mutations in ACVR1, a type I receptor for BMPs. Although mutated ACVR1 (FOP-ACVR1) has been ... test compared with the DMSO treatment control with Activin-A (. B. -. D. ).Representative data of n. =3. Scale bar: 200 μm (. E ... Although Activin-A evokes enhanced chondrogenesis in vitro and heterotopic ossification (HO) in vivo, the underlying mechanisms ... Activin-A enhances mTOR signaling to promote aberrant chondrogenesis in fibrodysplasia ossificans progressiva. ...
Although Activin-A evokes enhanced chondrogenesis in vitro and heterotopic ossification (HO) in vivo, the underlying mechanisms ... Patients with FOP harbor point mutations in ACVR1, a type I receptor for BMPs. Although mutated ACVR1 (FOP-ACVR1) has been ... Activin-A enhances mTOR signaling to promote aberrant chondrogenesis in fibrodysplasia ossificans progressiva. ... Activin-A enhances mTOR signaling to promote aberrant chondrogenesis in fibrodysplasia ossificans progressiva. ...
Selective, inducible deletion of the PTH receptor in Sox9-cre cells demonstrated that PTH receptor expression is required for ... Although Activin-A evokes enhanced chondrogenesis in vitro and heterotopic ossification (HO) in vivo, the underlying mechanisms ... Patients with FOP harbor point mutations in ACVR1, a type I receptor for BMPs. Although mutated ACVR1 (FOP-ACVR1) has been ... Activin-A enhances mTOR signaling to promote aberrant chondrogenesis in fibrodysplasia ossificans progressiva. ...
... inhibin/activin betaA and betaB and the activin type II and inhibin beta-glycan receptors in the developing human testis". ... A ligand binds to a type 2 receptor, which recruits and trans-phosphorylates a type I receptor. The type I receptor recruits a ... There are two activin type two receptors: ACVR2A and ACVR2B. Despite the large amount of processes that these ligands regulate ... The activin type 2 receptors modulate signals for ligands belonging to the transforming growth factor beta superfamily of ...
There are three type I Activin receptors: ACVR1, ACVR1B, and ACVR1C. Each bind to a specific type II receptor-ligand complex. ... A ligand binds to a Type two receptor, which recruits and trans-phosphorylate a type I receptor. The type I receptor recruits a ... The Activin type I receptors transduce signals for a variety of members of the Transforming growth factor beta superfamily of ... This family of cytokines and hormones include activin, Anti-müllerian hormone (AMH), bone morphogenetic proteins (BMPs), and ...
Activin receptor-like kinase 2 can mediate atrioventricular cushion transformation.. Lai YT1, Beason KB, Brames GP, ... we cloned and characterized the chicken homologues of two mammalian activin receptor-like kinases (ALK), ALK2 and ALK5, and ... These data establish that ChALK2 and ChALK5 are the chicken homologues of the mammalian receptors ALK2 and ALK5. Both ChALK2 ... To investigate the expression and function of specific Type I TGFbeta receptors during AV cushion transformation, ...
Regulation of muscle growth by multiple ligands signaling through activin type II receptors. Se-Jin Lee, Lori A. Reed, Monique ... Here we describe a potent myostatin inhibitor, a soluble form of the activin type IIB receptor (ACVR2B), which can cause ... Previous studies have demonstrated that myostatin is capable of binding the two activin type II receptors, ACVR2B and, to a ... Finally, we provide genetic evidence that these ligands signal through both activin type II receptors, ACVR2 and ACVR2B, to ...
J:1073 Matzuk MM, et al., Structure of the mouse activin receptor type II gene. Biochem Biophys Res Commun. 1992 May 29;185(1): ...
J:245961 Goh BC, et al., Activin receptor type 2A (ACVR2A) functions directly in osteoblasts as a negative regulator of bone ... J:11226 Mathews LS, et al., Expression cloning of an activin receptor, a predicted transmembrane serine kinase. Cell. 1991 Jun ...
Rabbit polyclonal Activin Receptor Type IIA antibody. Validated in WB, ICC/IF and tested in Human. Cited in 1 publication(s). ... Anti-Activin Receptor Type IIA antibody. See all Activin Receptor Type IIA primary antibodies. ... All lanes : Anti-Activin Receptor Type IIA antibody (ab96793) at 1/10000 dilution. Lane 1 : HeLa whole cell lysate. Lane 2 : ... Recombinant protein fragment corresponding to a region within amino acids 267 and 509 of Human Activin receptor type IIA ( ...
Biological basis for efficacy of activin receptor ligand traps in myelodysplastic syndromes. Amit Verma,1 Rajasekhar N.V.S. ... We also describe the basis for biological activity of activin receptor ligand traps, novel fusion proteins such as luspatercept ... TGF-β, activins, and growth differentiation factors exert inhibitory effects on red cell formation by activating canonical ...
Activin receptor type-1. Activin receptor type-1, EC 2.7.11.30 (Activin receptor type I, ACTR-I) (Activin receptor-like kinase ... Activin receptor type-1Imported. ,p>Information which has been imported from another database using automatic procedures.,/p> , ... tr,C9J1R3,C9J1R3_HUMAN Activin receptor type-1 (Fragment) OS=Homo sapiens OX=9606 GN=ACVR1 PE=4 SV=1 ... transmembrane receptor protein serine/threonine kinase activity Source: InterPro. View the complete GO annotation on QuickGO ...
  • To this end, we developed a high-throughput screening (HTS) system using FOP patient-derived induced pluripotent stem cells (FOP-iPSCs) to identify pivotal pathways in enhanced chondrogenesis that are initiated by Activin-A. In a screen of 6,809 small-molecule compounds, we identified mTOR signaling as a critical pathway for the aberrant chondrogenesis of mesenchymal stromal cells derived from FOP-iPSCs (FOP-iMSCs). (jci.org)
  • The cells were harvested 3 days ( B ), 7 days ( C ), or 6 days ( D and E ) after chondrogenesis induction was performed, with or without Activin-A and inhibitors (10 μM). (jci.org)
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