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.
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 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.
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).
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, respectively
They are glycopeptides and subunits in INHIBINS and ACTIVINS. Inhibins and activins belong to the transforming growth factor beta superfamily.
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.
Cell surface receptors that bind growth or trophic factors with high affinity, triggering intracellular responses which influence the growth, differentiation, or survival of cells.
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.
A receptor-regulated smad protein that undergoes PHOSPHORYLATION by ACTIVIN RECEPTORS, TYPE I. It regulates TRANSFORMING GROWTH FACTOR BETA and ACTIVIN signaling.
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.
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.
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-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.
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.
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.
A family of BONE MORPHOGENETIC PROTEIN-related proteins that are primarily involved in regulation of CELL DIFFERENTIATION.
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.
The middle germ layer of an embryo derived from three paired mesenchymal aggregates along the neural tube.
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.
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.
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.
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).
Signal molecules that are involved in the control of cell growth and differentiation.
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.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
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.
A disease characterized by bony deposits or the ossification of muscle tissue.
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.
An aquatic genus of the family, Pipidae, occurring in Africa and distinguished by having black horny claws on three inner hind toes.
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.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
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).
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
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.
The developmental entity of a fertilized egg (ZYGOTE) in animal species other than MAMMALS. For chickens, use CHICK EMBRYO.
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.
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.
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.
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.
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.
Established cell cultures that have the potential to propagate indefinitely.
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.
Glycoproteins which have a very high polysaccharide content.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
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 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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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)

Activin receptors are a type of serine/threonine kinase receptor that play a crucial role in various biological processes, including cell growth, differentiation, and apoptosis. They are activated by members of the TGF-β (transforming growth factor-beta) superfamily, particularly activins.

There are two main types of activin receptors: ActR-I and ActR-II. ActR-I exists in two isoforms, ALK2 and ALK4, while ActR-II has two isoforms, ActR-IIA and ActR-IIB. Activation of these receptors leads to the phosphorylation of intracellular signaling molecules, which then translocate to the nucleus and regulate gene expression.

Abnormalities in activin receptor function have been implicated in various diseases, including cancer, fibrosis, and developmental disorders. Therefore, activin receptors are an important target for therapeutic intervention in these conditions.

Activin receptors, type II, are a subgroup of serine/threonine kinase receptors that play a crucial role in signal transduction pathways involved in various biological processes, including cell growth, differentiation, and apoptosis. There are two types of activin receptors, Type IIA (ACVR2A) and Type IIB (ACVR2B), which are single-pass transmembrane proteins with an extracellular domain that binds to activins and a cytoplasmic domain with kinase activity.

Activins are dimeric proteins that belong to the transforming growth factor-β (TGF-β) superfamily, and they play essential roles in regulating developmental processes, reproduction, and homeostasis. Activin receptors, type II, function as primary binding sites for activins, forming a complex with Type I activin receptors (ALK4, ALK5, or ALK7) to initiate downstream signaling cascades.

Once the activin-receptor complex is formed, the intracellular kinase domain of the Type II receptor phosphorylates and activates the Type I receptor, which in turn propagates the signal by recruiting and phosphorylating downstream effectors such as SMAD proteins. Activated SMADs then form a complex and translocate to the nucleus, where they regulate gene expression.

Dysregulation of activin receptors, type II, has been implicated in various pathological conditions, including cancer, fibrosis, and developmental disorders. Therefore, understanding their function and regulation is essential for developing novel therapeutic strategies to target these diseases.

Activins are a type of protein that belongs to the transforming growth factor-beta (TGF-β) superfamily. They are produced and released by various cells in the body, including those in the ovaries, testes, pituitary gland, and other tissues. Activins play important roles in regulating several biological processes, such as cell growth, differentiation, and apoptosis (programmed cell death).

Activins bind to specific receptors on the surface of cells, leading to the activation of intracellular signaling pathways that control gene expression. They are particularly well-known for their role in reproductive biology, where they help regulate follicle stimulation and hormone production in the ovaries and testes. Activins also have been implicated in various disease processes, including cancer, fibrosis, and inflammation.

There are three main isoforms of activin in humans: activin A, activin B, and inhibin A. While activins and inhibins share similar structures and functions, they have opposite effects on the activity of the pituitary gland. Activins stimulate the production of follicle-stimulating hormone (FSH), while inhibins suppress it. This delicate balance between activins and inhibins helps regulate reproductive function and other physiological processes in the body.

Activin receptors, type I are serine/threonine kinase receptors that play a crucial role in the activin signaling pathway. There are two types of activin receptors, Type I (ALK2, ALK4, and ALK7) and Type II (ActRII and ActRIIB). Activin receptors, type I are transmembrane proteins that bind to activins, which are cytokines belonging to the TGF-β superfamily.

Once activated by binding to activins, activin receptors, type I recruit and phosphorylate type II receptors, leading to the activation of downstream signaling pathways, including SMAD proteins. Activated SMAD proteins then translocate to the nucleus and regulate gene expression, thereby mediating various cellular responses such as proliferation, differentiation, apoptosis, and migration.

Mutations in activin receptors, type I have been implicated in several human diseases, including cancer, fibrosis, and developmental disorders. Therefore, understanding the structure and function of activin receptors, type I is essential for developing novel therapeutic strategies to treat these diseases.

Inhibins are a group of protein hormones that play a crucial role in regulating the function of the reproductive system, specifically by inhibiting the production of follicle-stimulating hormone (FSH) in the pituitary gland. They are produced and secreted primarily by the granulosa cells in the ovaries of females and Sertoli cells in the testes of males.

Inhibins consist of two subunits, an alpha subunit, and a beta subunit, which can be further divided into two types: inhibin A and inhibin B. Inhibin A is primarily produced by the granulosa cells of developing follicles in the ovary, while inhibin B is mainly produced by the Sertoli cells in the testes.

By regulating FSH production, inhibins help control the development and maturation of ovarian follicles in females and spermatogenesis in males. Abnormal levels of inhibins have been associated with various reproductive disorders, including polycystic ovary syndrome (PCOS) and certain types of cancer.

Inhibin-β subunits are proteins that combine to form inhibins, which are hormones that play a role in regulating the function of the reproductive system. Specifically, inhibins help to regulate the production of follicle-stimulating hormone (FSH) by the pituitary gland.

There are two main types of Inhibin-β subunits, Inhibin-β A and Inhibin-β B, which combine with a common α subunit to form the inhibins. Inhibin-β A is produced primarily in the granulosa cells of the ovaries, while Inhibin-beta B is produced primarily in the testicular Sertoli cells.

Abnormal levels of Inhibin-β subunits have been associated with various reproductive disorders, such as polycystic ovary syndrome (PCOS) and certain types of cancer. Measurement of Inhibin-β subunits can be used as a biomarker for ovarian function, ovarian reserve and ovarian cancer detection.

Follistatin is a glycoprotein that is naturally produced in various tissues, including the ovaries, pituitary gland, and skeletal muscle. It plays an essential role in regulating the activity of members of the transforming growth factor-β (TGF-β) superfamily, particularly the bone morphogenetic proteins (BMPs) and activins.

Follistatin binds to these signaling molecules with high affinity, preventing them from interacting with their receptors and thereby inhibiting their downstream signaling pathways. By doing so, follistatin helps regulate processes such as follicle stimulation in the ovaries, neurogenesis, muscle growth, and inflammation.

Increased levels of follistatin have been associated with muscle hypertrophy, while its deficiency can lead to impaired fertility and developmental abnormalities.

Growth factor receptors are a type of cell surface receptor that bind to specific growth factors, which are signaling molecules that play crucial roles in regulating various cellular processes such as growth, differentiation, and survival. These receptors have an extracellular domain that can recognize and bind to the growth factor and an intracellular domain that can transduce the signal into the cell through a series of biochemical reactions.

There are several types of growth factors, including fibroblast growth factors (FGFs), epidermal growth factors (EGFs), vascular endothelial growth factors (VEGFs), and transforming growth factors (TGFs). Each type of growth factor has its own specific receptor or family of receptors.

Once a growth factor binds to its receptor, it triggers a cascade of intracellular signaling events that ultimately lead to changes in gene expression, protein synthesis, and other cellular responses. These responses can include the activation of enzymes, the regulation of ion channels, and the modulation of cytoskeletal dynamics.

Abnormalities in growth factor receptor signaling have been implicated in various diseases, including cancer, developmental disorders, and autoimmune diseases. For example, mutations in growth factor receptors can lead to uncontrolled cell growth and division, which is a hallmark of cancer. Therefore, understanding the structure and function of growth factor receptors has important implications for the development of new therapies for these diseases.

Myostatin is a protein that is primarily known for its role in regulating muscle growth. It's also called "growth differentiation factor 8" or GDF-8. Produced by muscle cells, myostatin inhibits the process of muscle growth by preventing the transformation of stem cells into muscle fibers and promoting the breakdown of existing muscle proteins.

In essence, myostatin acts as a negative regulator of muscle mass, keeping it in check to prevent excessive growth. Mutations leading to reduced myostatin activity or expression have been associated with increased muscle mass and strength in both animals and humans, making it a potential target for therapeutic interventions in muscle-wasting conditions such as muscular dystrophy and age-related sarcopenia.

Smad2 protein is a transcription factor that plays a critical role in the TGF-β (transforming growth factor-beta) signaling pathway, which regulates various cellular processes such as proliferation, differentiation, and apoptosis. Smad2 is primarily localized in the cytoplasm and becomes phosphorylated upon TGF-β receptor activation. Once phosphorylated, it forms a complex with Smad4 and translocates to the nucleus where it regulates the transcription of target genes. Mutations in the Smad2 gene have been associated with various human diseases, including cancer and fibrotic disorders.

Transforming Growth Factor beta (TGF-β) receptors are a group of cell surface receptors that bind to TGF-β ligands and transduce signals into the cell. These receptors play crucial roles in regulating various cellular processes, including cell growth, differentiation, apoptosis, and extracellular matrix production.

There are two types of TGF-β receptors: type I and type II. Type I receptors, also known as activin receptor-like kinases (ALKs), have serine/threonine kinase activity and include ALK1, ALK2, ALK3, ALK4, ALK5, and ALK6. Type II receptors are constitutively active serine/threonine kinases and include TGF-β RII, ActRII, and ActRIIB.

When a TGF-β ligand binds to a type II receptor, it recruits and phosphorylates a type I receptor, which in turn phosphorylates downstream signaling molecules called Smads. Phosphorylated Smads form complexes with co-Smad proteins and translocate to the nucleus, where they regulate gene expression.

Abnormalities in TGF-β signaling have been implicated in various human diseases, including fibrosis, cancer, and autoimmune disorders. Therefore, understanding the mechanisms of TGF-β receptor function is essential for developing therapeutic strategies to target these conditions.

A nodal protein, in the context of molecular biology and genetics, refers to a protein that plays a role in signal transmission within a cell at a node or junction point of a signaling pathway. These proteins are often involved in regulatory processes, such as activating or inhibiting downstream effectors in response to specific signals received by the cell. Nodal proteins can be activated or deactivated through various mechanisms, including phosphorylation, ubiquitination, and interactions with other signaling molecules.

In a more specific context, nodal proteins are also known as nodal factors, which are members of the transforming growth factor-beta (TGF-β) superfamily of signaling molecules that play critical roles in embryonic development and tissue homeostasis. Nodal is a secreted protein that acts as a morphogen, inducing different cellular responses depending on its concentration gradient. It is involved in establishing left-right asymmetry during embryonic development and regulates various processes such as cell proliferation, differentiation, and apoptosis.

In summary, nodal proteins can refer to any protein that functions at a node or junction point of a signaling pathway, but they are also specifically known as nodal factors, which are TGF-β superfamily members involved in embryonic development and tissue homeostasis.

Transforming Growth Factor-beta (TGF-β) is a type of cytokine, which is a cell signaling protein involved in the regulation of various cellular processes, including cell growth, differentiation, and apoptosis (programmed cell death). TGF-β plays a critical role in embryonic development, tissue homeostasis, and wound healing. It also has been implicated in several pathological conditions such as fibrosis, cancer, and autoimmune diseases.

TGF-β exists in multiple isoforms (TGF-β1, TGF-β2, and TGF-β3) that are produced by many different cell types, including immune cells, epithelial cells, and fibroblasts. The protein is synthesized as a precursor molecule, which is cleaved to release the active TGF-β peptide. Once activated, TGF-β binds to its receptors on the cell surface, leading to the activation of intracellular signaling pathways that regulate gene expression and cell behavior.

In summary, Transforming Growth Factor-beta (TGF-β) is a multifunctional cytokine involved in various cellular processes, including cell growth, differentiation, apoptosis, embryonic development, tissue homeostasis, and wound healing. It has been implicated in several pathological conditions such as fibrosis, cancer, and autoimmune diseases.

Bone Morphogenetic Proteins (BMPs) are a group of growth factors that play crucial roles in the development, growth, and repair of bones and other tissues. They belong to the Transforming Growth Factor-β (TGF-β) superfamily and were first discovered when researchers found that certain proteins extracted from demineralized bone matrix had the ability to induce new bone formation.

BMPs stimulate the differentiation of mesenchymal stem cells into osteoblasts, which are the cells responsible for bone formation. They also promote the recruitment and proliferation of these cells, enhancing the overall process of bone regeneration. In addition to their role in bone biology, BMPs have been implicated in various other biological processes, including embryonic development, wound healing, and the regulation of fat metabolism.

There are several types of BMPs (BMP-2, BMP-4, BMP-7, etc.) that exhibit distinct functions and expression patterns. Due to their ability to stimulate bone formation, recombinant human BMPs have been used in clinical applications, such as spinal fusion surgery and non-healing fracture treatment. However, the use of BMPs in medicine has been associated with certain risks and complications, including uncontrolled bone growth, inflammation, and cancer development, which necessitates further research to optimize their therapeutic potential.

Smad proteins are a family of intracellular signaling molecules that play a crucial role in the transmission of signals from the cell surface to the nucleus in response to transforming growth factor β (TGF-β) superfamily ligands. These ligands include TGF-βs, bone morphogenetic proteins (BMPs), activins, and inhibins.

There are eight mammalian Smad proteins, which are categorized into three classes based on their function: receptor-regulated Smads (R-Smads), common mediator Smads (Co-Smads), and inhibitory Smads (I-Smads). R-Smads include Smad1, Smad2, Smad3, Smad5, and Smad8/9, while Smad4 is the only Co-Smad. The I-Smads consist of Smad6 and Smad7.

Upon TGF-β superfamily ligand binding to their transmembrane serine/threonine kinase receptors, R-Smads are phosphorylated and form complexes with Co-Smad4. These complexes then translocate into the nucleus, where they regulate the transcription of target genes involved in various cellular processes, such as proliferation, differentiation, apoptosis, migration, and extracellular matrix production. I-Smads act as negative regulators of TGF-β signaling by competing with R-Smads for receptor binding or promoting the degradation of receptors and R-Smads.

Dysregulation of Smad protein function has been implicated in various human diseases, including fibrosis, cancer, and developmental disorders.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Growth differentiation factors (GDFs) are a subfamily of the transforming growth factor-beta (TGF-β) superfamily of cytokines. They play crucial roles in various biological processes, including cell growth, differentiation, and apoptosis. Specifically, GDFs are involved in the development and maintenance of the skeletal, reproductive, and nervous systems. Some members of this family include GDF5, GDF6, and GDF7, which are essential for normal joint formation and cartilage development; GDF8 (also known as myostatin) is a negative regulator of muscle growth; and GDF11 has been implicated in the regulation of neurogenesis and age-related changes.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

In medical and embryological terms, the mesoderm is one of the three primary germ layers in the very early stages of embryonic development. It forms between the ectoderm and endoderm during gastrulation, and it gives rise to a wide variety of cell types, tissues, and organs in the developing embryo.

The mesoderm contributes to the formation of structures such as:

1. The connective tissues (including tendons, ligaments, and most of the bones)
2. Muscular system (skeletal, smooth, and cardiac muscles)
3. Circulatory system (heart, blood vessels, and blood cells)
4. Excretory system (kidneys and associated structures)
5. Reproductive system (gonads, including ovaries and testes)
6. Dermis of the skin
7. Parts of the eye and inner ear
8. Several organs in the urogenital system

Dysfunctions or abnormalities in mesoderm development can lead to various congenital disorders and birth defects, highlighting its importance during embryogenesis.

Smad3 protein is a transcription factor that plays a crucial role in the TGF-β (transforming growth factor-beta) signaling pathway. When TGF-β binds to its receptor, it activates Smad3 through phosphorylation. Activated Smad3 then forms a complex with other Smad proteins and translocates into the nucleus where it regulates the transcription of target genes involved in various cellular processes such as proliferation, differentiation, apoptosis, and migration.

Mutations in the SMAD3 gene or dysregulation of the TGF-β/Smad3 signaling pathway have been implicated in several human diseases, including fibrotic disorders, cancer, and Marfan syndrome. Therefore, Smad3 protein is an important target for therapeutic interventions in these conditions.

Bone morphogenetic protein receptors (BMPRs) are a group of transmembrane serine/threonine kinase receptors that play a crucial role in the signaling pathway of bone morphogenetic proteins (BMPs), which are growth factors involved in various biological processes including cell proliferation, differentiation, and apoptosis.

Type I BMPRs include three subtypes: activin receptor-like kinase 2 (ALK2), ALK3 (also known as BMPR-IA), and ALK6 (also known as BMPR-IB). These receptors form a complex with type II BMPRs upon binding of BMP ligands to their extracellular domains. The activation of the receptor complex leads to the phosphorylation of intracellular signaling molecules, such as SMAD proteins, which then translocate to the nucleus and regulate gene expression.

Mutations in type I BMPRs have been associated with several genetic disorders, including hereditary hemorrhagic telangiectasia (HHT), a vascular dysplasia disorder characterized by the formation of abnormal blood vessels. Additionally, alterations in BMP signaling pathways have been implicated in various human diseases, such as cancer, fibrosis, and bone disorders.

Smad4 protein is a transcription factor that plays a crucial role in the signaling pathways of transforming growth factor-beta (TGF-β), bone morphogenetic proteins (BMPs), and activins. These signaling pathways are involved in various cellular processes, including cell proliferation, differentiation, apoptosis, and migration.

Smad4 is the common mediator of these pathways and forms a complex with Smad2 or Smad3 upon TGF-β/activin stimulation or with Smad1, Smad5, or Smad8 upon BMP stimulation. The resulting complex then translocates to the nucleus, where it regulates gene expression by binding to specific DNA sequences and interacting with other transcription factors.

Smad4 also plays a role in negative feedback regulation of TGF-β signaling by promoting the expression of inhibitory Smads (Smad6 and Smad7), which compete for receptor binding and prevent further signal transduction. Mutations in the Smad4 gene have been associated with various human diseases, including cancer and vascular disorders.

Embryonic induction is a process that occurs during the development of a multicellular organism, where one group of cells in the embryo signals and influences the developmental fate of another group of cells. This interaction leads to the formation of specific structures or organs in the developing embryo. The signaling cells that initiate the process are called organizers, and they release signaling molecules known as morphogens that bind to receptors on the target cells and trigger a cascade of intracellular signals that ultimately lead to changes in gene expression and cell fate. Embryonic induction is a crucial step in the development of complex organisms and plays a key role in establishing the body plan and organizing the different tissues and organs in the developing embryo.

Growth substances, in the context of medical terminology, typically refer to natural hormones or chemically synthesized agents that play crucial roles in controlling and regulating cell growth, differentiation, and division. They are also known as "growth factors" or "mitogens." These substances include:

1. Proteins: Examples include insulin-like growth factors (IGFs), transforming growth factor-beta (TGF-β), platelet-derived growth factor (PDGF), and fibroblast growth factors (FGFs). They bind to specific receptors on the cell surface, activating intracellular signaling pathways that promote cell proliferation, differentiation, and survival.

2. Steroids: Certain steroid hormones, such as androgens and estrogens, can also act as growth substances by binding to nuclear receptors and influencing gene expression related to cell growth and division.

3. Cytokines: Some cytokines, like interleukins (ILs) and hematopoietic growth factors (HGFs), contribute to the regulation of hematopoiesis, immune responses, and inflammation, thus indirectly affecting cell growth and differentiation.

These growth substances have essential roles in various physiological processes, such as embryonic development, tissue repair, and wound healing. However, abnormal or excessive production or response to these growth substances can lead to pathological conditions, including cancer, benign tumors, and other proliferative disorders.

"Xenopus proteins" refer to the proteins that are expressed or isolated from the Xenopus species, which are primarily used as model organisms in biological and biomedical research. The most commonly used Xenopus species for research are the African clawed frogs, Xenopus laevis and Xenopus tropicalis. These proteins play crucial roles in various cellular processes and functions, and they serve as valuable tools to study different aspects of molecular biology, developmental biology, genetics, and biochemistry.

Some examples of Xenopus proteins that are widely studied include:

1. Xenopus Histones: These are the proteins that package DNA into nucleosomes, which are the fundamental units of chromatin in eukaryotic cells. They play a significant role in gene regulation and epigenetic modifications.
2. Xenopus Cyclins and Cyclin-dependent kinases (CDKs): These proteins regulate the cell cycle and control cell division, differentiation, and apoptosis.
3. Xenopus Transcription factors: These proteins bind to specific DNA sequences and regulate gene expression during development and in response to various stimuli.
4. Xenopus Signaling molecules: These proteins are involved in intracellular signaling pathways that control various cellular processes, such as cell growth, differentiation, migration, and survival.
5. Xenopus Cytoskeletal proteins: These proteins provide structural support to the cells and regulate their shape, motility, and organization.
6. Xenopus Enzymes: These proteins catalyze various biochemical reactions in the cell, such as metabolic pathways, DNA replication, transcription, and translation.

Overall, Xenopus proteins are essential tools for understanding fundamental biological processes and have contributed significantly to our current knowledge of molecular biology, genetics, and developmental biology.

Protein-Serine-Threonine Kinases (PSTKs) are a type of protein kinase that catalyzes the transfer of a phosphate group from ATP to the hydroxyl side chains of serine or threonine residues on target proteins. This phosphorylation process plays a crucial role in various cellular signaling pathways, including regulation of metabolism, gene expression, cell cycle progression, and apoptosis. PSTKs are involved in many physiological and pathological processes, and their dysregulation has been implicated in several diseases, such as cancer, diabetes, and neurodegenerative disorders.

Developmental gene expression regulation refers to the processes that control the activation or repression of specific genes during embryonic and fetal development. These regulatory mechanisms ensure that genes are expressed at the right time, in the right cells, and at appropriate levels to guide proper growth, differentiation, and morphogenesis of an organism.

Developmental gene expression regulation is a complex and dynamic process involving various molecular players, such as transcription factors, chromatin modifiers, non-coding RNAs, and signaling molecules. These regulators can interact with cis-regulatory elements, like enhancers and promoters, to fine-tune the spatiotemporal patterns of gene expression during development.

Dysregulation of developmental gene expression can lead to various congenital disorders and developmental abnormalities. Therefore, understanding the principles and mechanisms governing developmental gene expression regulation is crucial for uncovering the etiology of developmental diseases and devising potential therapeutic strategies.

Myositis ossificans is a medical condition characterized by the formation of bone tissue within the soft tissues, particularly in the muscles. It is also known as heterotopic ossification, which means "bone formation in an abnormal location." This condition usually occurs after trauma or injury to the muscle, such as a severe contusion (bruise) or a muscle strain or tear.

In myositis ossificans, the body's repair process goes awry, and instead of healing the muscle with normal scar tissue, bone tissue forms within the muscle. This can cause pain, stiffness, and limited mobility in the affected area. In some cases, the bone tissue may continue to grow and harden over time, leading to further complications.

Myositis ossificans is typically diagnosed through imaging tests such as X-rays, CT scans, or MRI scans, which can show the presence of bone tissue within the muscle. Treatment may include physical therapy, pain management, and in some cases, surgery to remove the excess bone tissue. Preventive measures such as early mobilization and protection of the affected area may help reduce the risk of developing myositis ossificans after an injury.

In situ hybridization (ISH) is a molecular biology technique used to detect and localize specific nucleic acid sequences, such as DNA or RNA, within cells or tissues. This technique involves the use of a labeled probe that is complementary to the target nucleic acid sequence. The probe can be labeled with various types of markers, including radioisotopes, fluorescent dyes, or enzymes.

During the ISH procedure, the labeled probe is hybridized to the target nucleic acid sequence in situ, meaning that the hybridization occurs within the intact cells or tissues. After washing away unbound probe, the location of the labeled probe can be visualized using various methods depending on the type of label used.

In situ hybridization has a wide range of applications in both research and diagnostic settings, including the detection of gene expression patterns, identification of viral infections, and diagnosis of genetic disorders.

"Xenopus" is not a medical term, but it is a genus of highly invasive aquatic frogs native to sub-Saharan Africa. They are often used in scientific research, particularly in developmental biology and genetics. The most commonly studied species is Xenopus laevis, also known as the African clawed frog.

In a medical context, Xenopus might be mentioned when discussing their use in research or as a model organism to study various biological processes or diseases.

Bone morphogenetic protein receptors, type II (BMPR2) are a type of cell surface receptor that bind to bone morphogenetic proteins (BMPs), which are growth factors involved in the regulation of various cellular processes such as cell proliferation, differentiation, and apoptosis. BMPR2 is a serine/threonine kinase receptor and forms a complex with type I BMP receptors upon BMP binding. This complex activation leads to the phosphorylation and activation of downstream signaling molecules, including SMAD proteins, which ultimately regulate gene transcription.

Mutations in the BMPR2 gene have been associated with several genetic disorders, most notably pulmonary arterial hypertension (PAH), a rare but life-threatening condition characterized by increased pressure in the pulmonary arteries that supply blood to the lungs. In addition, BMPR2 mutations have also been linked to Marfan syndrome, a genetic disorder that affects connective tissue and can cause skeletal, cardiovascular, and ocular abnormalities.

Glycoproteins are complex proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbone. These glycans are linked to the protein through asparagine residues (N-linked) or serine/threonine residues (O-linked). Glycoproteins play crucial roles in various biological processes, including cell recognition, cell-cell interactions, cell adhesion, and signal transduction. They are widely distributed in nature and can be found on the outer surface of cell membranes, in extracellular fluids, and as components of the extracellular matrix. The structure and composition of glycoproteins can vary significantly depending on their function and location within an organism.

Gene expression is the process by which the information encoded in a gene is used to synthesize a functional gene product, such as a protein or RNA molecule. This process involves several steps: transcription, RNA processing, and translation. During transcription, the genetic information in DNA is copied into a complementary RNA molecule, known as messenger RNA (mRNA). The mRNA then undergoes RNA processing, which includes adding a cap and tail to the mRNA and splicing out non-coding regions called introns. The resulting mature mRNA is then translated into a protein on ribosomes in the cytoplasm through the process of translation.

The regulation of gene expression is a complex and highly controlled process that allows cells to respond to changes in their environment, such as growth factors, hormones, and stress signals. This regulation can occur at various stages of gene expression, including transcriptional activation or repression, RNA processing, mRNA stability, and translation. Dysregulation of gene expression has been implicated in many diseases, including cancer, genetic disorders, and neurological conditions.

Trans-activators are proteins that increase the transcriptional activity of a gene or a set of genes. They do this by binding to specific DNA sequences and interacting with the transcription machinery, thereby enhancing the recruitment and assembly of the complexes needed for transcription. In some cases, trans-activators can also modulate the chromatin structure to make the template more accessible to the transcription machinery.

In the context of HIV (Human Immunodeficiency Virus) infection, the term "trans-activator" is often used specifically to refer to the Tat protein. The Tat protein is a viral regulatory protein that plays a critical role in the replication of HIV by activating the transcription of the viral genome. It does this by binding to a specific RNA structure called the Trans-Activation Response Element (TAR) located at the 5' end of all nascent HIV transcripts, and recruiting cellular cofactors that enhance the processivity and efficiency of RNA polymerase II, leading to increased viral gene expression.

Granulosa cells are specialized cells that surround and enclose the developing egg cells (oocytes) in the ovaries. They play a crucial role in the growth, development, and maturation of the follicles (the fluid-filled sacs containing the oocytes) by providing essential nutrients and hormones.

Granulosa cells are responsible for producing estrogen, which supports the development of the endometrium during the menstrual cycle in preparation for a potential pregnancy. They also produce inhibin and activin, two hormones that regulate the function of the pituitary gland and its secretion of follicle-stimulating hormone (FSH) and luteinizing hormone (LH).

These cells are critical for female reproductive health and fertility. Abnormalities in granulosa cell function can lead to various reproductive disorders, such as polycystic ovary syndrome (PCOS), premature ovarian failure, and infertility.

Cell differentiation is the process by which a less specialized cell, or stem cell, becomes a more specialized cell type with specific functions and structures. This process involves changes in gene expression, which are regulated by various intracellular signaling pathways and transcription factors. Differentiation results in the development of distinct cell types that make up tissues and organs in multicellular organisms. It is a crucial aspect of embryonic development, tissue repair, and maintenance of homeostasis in the body.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

A nonmammalian embryo refers to the developing organism in animals other than mammals, from the fertilized egg (zygote) stage until hatching or birth. In nonmammalian species, the developmental stages and terminology differ from those used in mammals. The term "embryo" is generally applied to the developing organism up until a specific stage of development that is characterized by the formation of major organs and structures. After this point, the developing organism is referred to as a "larva," "juvenile," or other species-specific terminology.

The study of nonmammalian embryos has played an important role in our understanding of developmental biology and evolutionary developmental biology (evo-devo). By comparing the developmental processes across different animal groups, researchers can gain insights into the evolutionary origins and diversification of body plans and structures. Additionally, nonmammalian embryos are often used as model systems for studying basic biological processes, such as cell division, gene regulation, and pattern formation.

An ovary is a part of the female reproductive system in which ova or eggs are produced through the process of oogenesis. They are a pair of solid, almond-shaped structures located one on each side of the uterus within the pelvic cavity. Each ovary measures about 3 to 5 centimeters in length and weighs around 14 grams.

The ovaries have two main functions: endocrine (hormonal) function and reproductive function. They produce and release eggs (ovulation) responsible for potential fertilization and development of an embryo/fetus during pregnancy. Additionally, they are essential in the production of female sex hormones, primarily estrogen and progesterone, which regulate menstrual cycles, sexual development, and reproduction.

During each menstrual cycle, a mature egg is released from one of the ovaries into the fallopian tube, where it may be fertilized by sperm. If not fertilized, the egg, along with the uterine lining, will be shed, leading to menstruation.

Reverse Transcriptase Polymerase Chain Reaction (RT-PCR) is a laboratory technique used in molecular biology to amplify and detect specific DNA sequences. This technique is particularly useful for the detection and quantification of RNA viruses, as well as for the analysis of gene expression.

The process involves two main steps: reverse transcription and polymerase chain reaction (PCR). In the first step, reverse transcriptase enzyme is used to convert RNA into complementary DNA (cDNA) by reading the template provided by the RNA molecule. This cDNA then serves as a template for the PCR amplification step.

In the second step, the PCR reaction uses two primers that flank the target DNA sequence and a thermostable polymerase enzyme to repeatedly copy the targeted cDNA sequence. The reaction mixture is heated and cooled in cycles, allowing the primers to anneal to the template, and the polymerase to extend the new strand. This results in exponential amplification of the target DNA sequence, making it possible to detect even small amounts of RNA or cDNA.

RT-PCR is a sensitive and specific technique that has many applications in medical research and diagnostics, including the detection of viruses such as HIV, hepatitis C virus, and SARS-CoV-2 (the virus that causes COVID-19). It can also be used to study gene expression, identify genetic mutations, and diagnose genetic disorders.

DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.

The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.

DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.

"Body patterning" is a general term that refers to the process of forming and organizing various tissues and structures into specific patterns during embryonic development. This complex process involves a variety of molecular mechanisms, including gene expression, cell signaling, and cell-cell interactions. It results in the creation of distinct body regions, such as the head, trunk, and limbs, as well as the organization of internal organs and systems.

In medical terminology, "body patterning" may refer to specific developmental processes or abnormalities related to embryonic development. For example, in genetic disorders such as Poland syndrome or Holt-Oram syndrome, mutations in certain genes can lead to abnormal body patterning, resulting in the absence or underdevelopment of certain muscles, bones, or other structures.

It's important to note that "body patterning" is not a formal medical term with a specific definition, but rather a general concept used in developmental biology and genetics.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Follicle-stimulating hormone (FSH) is a glycoprotein hormone produced and released by the anterior pituitary gland. It plays crucial roles in the reproductive system, primarily by promoting the growth and development of follicles in the ovaries or sperm production in the testes.

The FSH molecule consists of two subunits: α (alpha) and β (beta). The α-subunit is common to several glycoprotein hormones, including thyroid-stimulating hormone (TSH), luteinizing hormone (LH), and human chorionic gonadotropin (hCG). In contrast, the β-subunit is unique to each hormone and determines its specific biological activity.

A medical definition of 'Follicle Stimulating Hormone, beta Subunit' refers to the distinct portion of the FSH molecule that is responsible for its particular functions in the body. The β-subunit of FSH enables the hormone to bind to its specific receptors in the gonads and initiate downstream signaling pathways leading to follicular development and spermatogenesis. Any alterations or mutations in the FSH beta subunit can lead to disruptions in reproductive processes, potentially causing infertility or other related disorders.

Proteoglycans are complex, highly negatively charged macromolecules that are composed of a core protein covalently linked to one or more glycosaminoglycan (GAG) chains. They are a major component of the extracellular matrix (ECM) and play crucial roles in various biological processes, including cell signaling, regulation of growth factor activity, and maintenance of tissue structure and function.

The GAG chains, which can vary in length and composition, are long, unbranched polysaccharides that are composed of repeating disaccharide units containing a hexuronic acid (either glucuronic or iduronic acid) and a hexosamine (either N-acetylglucosamine or N-acetylgalactosamine). These GAG chains can be sulfated to varying degrees, which contributes to the negative charge of proteoglycans.

Proteoglycans are classified into four major groups based on their core protein structure and GAG composition: heparan sulfate/heparin proteoglycans, chondroitin/dermatan sulfate proteoglycans, keratan sulfate proteoglycans, and hyaluronan-binding proteoglycans. Each group has distinct functions and is found in specific tissues and cell types.

In summary, proteoglycans are complex macromolecules composed of a core protein and one or more GAG chains that play important roles in the ECM and various biological processes, including cell signaling, growth factor regulation, and tissue structure maintenance.

Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.

Goosecoid protein is not a term that has a specific medical definition. However, it is a biological term related to the field of developmental biology and genetics.

Goosecoid protein is a transcription factor that plays a crucial role in embryonic development, particularly during gastrulation - an early stage of embryogenesis where the three germ layers (ectoderm, mesoderm, and endoderm) are formed. The goosecoid gene encodes this protein, and it is primarily expressed in the Spemann-Mangold organizer, a structure located in the dorsal blastopore lip of amphibian embryos. This organizer region is essential for establishing the body axis and inducing the formation of the central nervous system.

In humans, goosecoid protein homologs have been identified, and they are involved in various developmental processes, including limb development and craniofacial morphogenesis. Dysregulation of goosecoid protein expression or function has been implicated in several congenital disorders and cancer types. However, a direct medical definition focusing on 'Goosecoid Protein' is not available due to its broader biological context.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Cell surface receptors, also known as membrane receptors, are proteins located on the cell membrane that bind to specific molecules outside the cell, known as ligands. These receptors play a crucial role in signal transduction, which is the process of converting an extracellular signal into an intracellular response.

Cell surface receptors can be classified into several categories based on their structure and mechanism of action, including:

1. Ion channel receptors: These receptors contain a pore that opens to allow ions to flow across the cell membrane when they bind to their ligands. This ion flux can directly activate or inhibit various cellular processes.
2. G protein-coupled receptors (GPCRs): These receptors consist of seven transmembrane domains and are associated with heterotrimeric G proteins that modulate intracellular signaling pathways upon ligand binding.
3. Enzyme-linked receptors: These receptors possess an intrinsic enzymatic activity or are linked to an enzyme, which becomes activated when the receptor binds to its ligand. This activation can lead to the initiation of various signaling cascades within the cell.
4. Receptor tyrosine kinases (RTKs): These receptors contain intracellular tyrosine kinase domains that become activated upon ligand binding, leading to the phosphorylation and activation of downstream signaling molecules.
5. Integrins: These receptors are transmembrane proteins that mediate cell-cell or cell-matrix interactions by binding to extracellular matrix proteins or counter-receptors on adjacent cells. They play essential roles in cell adhesion, migration, and survival.

Cell surface receptors are involved in various physiological processes, including neurotransmission, hormone signaling, immune response, and cell growth and differentiation. Dysregulation of these receptors can contribute to the development of numerous diseases, such as cancer, diabetes, and neurological disorders.

The activin type 2 receptors belong to a larger TGF-beta receptor family and modulate signals for transforming growth factor ... 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 ...
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 ...
An Activin receptor is a receptor which binds activin. These proteins are receptor-type kinases of Ser/Thr type, which have a ... Types include: Activin type 1 receptors Activin type 2 receptors ACVR1; ACVR1B; ACVR1C; ACVR2A; ACVR2B; ACVRL1; BMPR1A; BMPR1B ... Activin+receptors at the U.S. National Library of Medicine Medical Subject Headings (MeSH) This article incorporates text from ... Wrana JL, Attisano L, Wieser R, Ventura F, Massague J (1994). "Mechanism of activation of the TGF-beta receptor". Nature. 370 ( ...
... 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, ...
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. ...
It binds to and inhibits activin receptor type-2B. On August 20, 2013, it was announced that bimagrumab had received a ... an activin receptor type II inhibitor, on pituitary neurohormonal axes". Clinical Endocrinology. 88 (6): 908-919. doi:10.1111/ ...
"Characterization of type I receptors for transforming growth factor-beta and activin". Science. 264 (5155): 101-4. Bibcode: ... 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 ... Receptors, Transmembrane receptors, S/T domain, EC 2.7.11). ... Bone morphogenetic protein receptor type-1B also known as ...
... 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 ... "Activin receptor-like kinases: a novel subclass of cell-surface receptors with predicted serine/threonine kinase activity". ... and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a ...
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 ...
2020 scientists reported that suppressing activin type 2 receptors-signalling proteins myostatin and activin A via activin A/ ... 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 ... Treating progeric mice with soluble activin receptor type IIB before the onset of premature ageing signs appear to protects ...
Activin A receptor type 2A (ACVR2A) is a transmembrane receptor that is involved in ligand-binding and mediates the functions ... "ACVR2A activin A receptor type 2A [Homo sapiens (human)] - Gene - NCBI". Gene. Bock, J B; Klumperman, J; Davanger, S; Scheller ... Bone morphogenetic protein receptor type 1A(BMPR1A) is expressed almost exclusively in skeletal muscle and is a transcriptional ... Fibroblast growth factor receptor 2 (FGFR2) plays an essential role in the regulation of osteoblast differentiation, ...
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 ...
ACVR1 encodes activin receptor type-1, a BMP type-1 receptor. The mutation causes substitution of codon 206 from arginine to ... Normally, the ACVR1 gene encodes the activin receptor type-1 transmembrane kinase that bind BMP receptors (Type I BMPR and Type ... Regeneron announced new insight into the mechanism of disease involving the activation of the ACVR1 receptor by activin A. In ... "ACVR1 R206H receptor mutation causes fibrodysplasia ossificans progressiva by imparting responsiveness to activin A". Science ...
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 betaglycan (the TGF-β type III receptor) and InhBP/p120 (a membrane-tethered proteoglycan) were identified ... 2001). "Localization of activin beta(A)-, beta(B)-, and beta(C)-subunits in humanprostate and evidence for formation of new ...
Engelse MA, Arkenbout EK, Pannekoek H, de Vries CJ (November 2003). "Activin and TR3 orphan receptor: two 'atheroprotective' ... The other two members are Nuclear receptor 4A2 (NR4A2) and Nuclear receptor 4A3 (NR4A3). Nuclear receptor 4A1 has a high degree ... The nuclear receptor 4A1 (NR4A1 for "nuclear receptor subfamily 4 group A member 1") also known as Nur77, TR3, and NGFI-B is a ... Nuclear receptor 4A1 has the systematic HUGO gene symbol NR4A1. It belongs to a group of three closely related orphan receptors ...
"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- ...
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 ...
January 2008). "MicroRNA miR-24 inhibits erythropoiesis by targeting activin type I receptor ALK4". Blood. 111 (2): 588-95. doi ...
"The Interpretation of Position in a Morphogen Gradient as Revealed by Occupancy of Activin Receptors". Cell. 93 (4): 557-568. ... 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 ...
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". ...
Lambert-Messerlian G, Eklund E, Pinar H, Tantravahi U, Schneyer AL (2007). "Activin subunit and receptor expression in normal ... Walsh S, Metter EJ, Ferrucci L, Roth SM (June 2007). "Activin-type II receptor B (ACVR2B) and follistatin haplotype ... activin complex reveals antagonism of both type I and type II receptor binding". Developmental Cell. 9 (4): 535-543. doi: ... In the blood, activin and follistatin are both known to be involved in the inflammatory response following tissue injury or ...
"Determination of type I receptor specificity by the type II receptors for TGF-beta or activin". Science. 262 (5135): 900-2. ... 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 ... Chen W, Wahl SM (2002). "TGF-β: Receptors, Signaling Pathways and Autoimmunity". TGF-beta: receptors, signaling pathways and ...
... activin A receptor type II-like kinase, 53kDa) is a membrane-bound TGF beta receptor protein of the TGF-beta receptor family ... "Entrez Gene: TGFBR1 transforming growth factor, beta receptor I (activin A receptor type II-like kinase, 53kDa)". Razani B, ... "Determination of type I receptor specificity by the type II receptors for TGF-beta or activin". Science. 262 (5135): 900-2. ... 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 ...
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 ...
Tan SM, Zhang Y, Connelly KA, Gilbert RE, Kelly DJ (May 2010). "Targeted inhibition of activin receptor-like kinase 5 signaling ... Lho Y, Do JY, Heo JY, Kim AY, Kim SW, Kang SH (April 2021). "Effects of TGF-β1 Receptor Inhibitor GW788388 on the Epithelial to ... GW 788388 is a synthetic compound which acts as a potent and selective inhibitor for TGF beta receptor 1. It has applications ... McMillin M, Grant S, Frampton G, Petrescu AD, Williams E, Jefferson B, DeMorrow S (May 2019). "The TGFβ1 Receptor Antagonist ...
... 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 activin receptor-like kinase 1, ALK1 (also called ACVRL1), an endothelial-specific type I ... 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 ...
... 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. ...
We report that RAP-011, an activin receptor IIA (ActRIIA) ligand trap, improved ineffective erythropoiesis, corrected anemia ... An activin receptor IIA ligand trap corrects ineffective erythropoiesis in β-thalassemia Michael Dussiot 1 , Thiago T Maciel 1 ... An activin receptor IIA ligand trap corrects ineffective erythropoiesis in β-thalassemia Michael Dussiot et al. Nat Med. 2014 ... Modified activin receptor IIB ligand trap mitigates ineffective erythropoiesis and disease complications in murine β- ...
Activin type II receptor (ActRII) ligands have been implicated in muscle wasting in aging and disease. However, the role of ... Activin type II receptor signaling in cardiac aging and heart failure Jason D Roh 1 , Ryan Hobson 1 , Vinita Chaudhari 1 , ... Activin type II receptor signaling in cardiac aging and heart failure Jason D Roh et al. Sci Transl Med. 2019. . ... Activin type II receptor (ActRII) ligands have been implicated in muscle wasting in aging and disease. However, the role of ...
The activin type II receptor (ACVR2) gene is a putative tumor suppressor gene that is frequently mutated in microsatellite- ... Activin type II receptor restoration in ACVR2-deficient colon cancer cells induces transforming growth factor-beta response ... Activin type II receptor restoration in ACVR2-deficient colon cancer cells induces transforming growth factor-beta response ... This observed similarity between the activin and TGF-beta signaling systems suggests that activin may serve as an alternative ...
Small molecule inhibition of activin receptor signaling limits vaccinia virus growth in the skin of a new filaggrin-deficient ... Small molecule inhibition of activin receptor (ALK5) signaling promoted viral clearance from the skin but not disseminated ... We are currently evaluating the role of activin A in shaping innate and adaptive immune responses to skin infection in mice, ... yielded pronounced local and distant viral spread accompanied by elevated levels of the TGF-b family ligand activin A. ...
... and activin-receptor inhibitors the next upcoming drug class, highly effective treatments for obesity are in sight. ... Activin Receptor Inhibitors Bimagrumab. This drug is a monoclonal antibody activin receptor inhibitor that binds to activin ... She then briefly touched on activin receptor inhibitors -"the next [medication] class that I think will be up and coming," she ... With nutrient-stimulated hormone therapies for obesity in phase 3 trials, and activin-receptor inhibitors the next upcoming ...
ACVR1: activin A receptor type 1. *ACVRL1: activin A receptor like type 1 ...
Activin Receptors, Type I. 1. 2019. 143. 0.330. Why? Professional Practice. 1. 2010. 327. 0.320. Why? ...
Activins and the receptor serine kinase superfamily. Gaddy-Kurten D, Tsuchida K, Vale W. Gaddy-Kurten D, et al. Among authors: ... Roles of activin family in pancreatic development and homeostasis. Wiater E, Vale W. Wiater E, et al. Among authors: vale w. ... Modulation of activin and BMP signaling. Harrison CA, Wiater E, Gray PC, Greenwald J, Choe S, Vale W. Harrison CA, et al. Among ... Antagonists of activin signaling: mechanisms and potential biological applications. Harrison CA, Gray PC, Vale WW, Robertson DM ...
activin A receptor, type IB. 1.3. 421986. CXCR4. chemokine (C-X-C motif) receptor 4. 1.3. ... Activation of EGF receptors mediates pulmonary vasoconstriction induced by residual oil fly ash. Exp Lung Res 28(1):19-38. ... These alterations included up-regulation of tissue factor (F3) (2.7-fold) and coagulation factor II receptor-like 2 (F2RL2) ( ... Table 1 Cytokine-cytokine receptor interaction KEGG pathway (p = 0.001) identified with DAVID 2.1 from the list of ...
Antibody Details for Activin Receptor, Type II (actRII) Ab-1. WBI Title. Validation Status. Band Result. Date. Dilution. ...
CDD866 can bind to the receptor and prevent activin A from activating it. CDD866 blocked activin A from causing a drop in ... References: Activin type II receptor signaling in cardiac aging and heart failure. Roh JD, Hobson R, Chaudhari V, Quintero P, ... Previous studies have associated the activin type II receptor (ActRII) pathway with muscle wasting and other aging-related ... One of the proteins that binds to ActRII is called activin A. Older mice had about three times as much activin A in their blood ...
Bone morphogenetic protein (BMP) and activin type II receptors balance BMP9 signals mediated by activin receptor-like kinase-1 ... Activin receptor inhibitors--dalantercept.. Gupta S; Gill D; Pal SK; Agarwal N. Curr Oncol Rep; 2015 Apr; 17(4):14. PubMed ID: ... Anti-human activin receptor-like kinase 1 (ALK1) antibody attenuates bone morphogenetic protein 9 (BMP9)-induced ALK1 signaling ... 3. Activin Receptor-like Kinase 1 Ligand Trap Reduces Microvascular Density and Improves Chemotherapy Efficiency to Various ...
An Activin Receptor IA/Activin-Like Kinase-2 (R206H) Mutation in Fibrodysplasia Ossificans Progressiva. Case Rep Genet. 2013. ... A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva. Nat ... type I receptor ACVR1. Hum Mutat. 2009 Mar. 30(3):379-90. [QxMD MEDLINE Link]. ...
MeSH Terms: Activin Receptors, Type I/genetics; Activin Receptors, Type I/metabolism*; Animals; Chick Embryo; Epithelial Cells/ ... Receptors involved in the EMT process include TGF-beta receptor type II (TBRII), TBRIII, endoglin and the TBRI receptors, ALK2 ... Receptors, Transforming Growth Factor beta/genetics; Receptors, Transforming Growth Factor beta/metabolism*; Transforming ... In the chick, TGF-beta ligands and some receptors have specific functions during EMT. TGF-beta2 mediates endothelial cell-cell ...
ACVR1 is a protein which in humans is encoded by the ACVR1 gene; also known as ALK-2 (activin receptor-like kinase-2); ... Inhibits signals along 3 pathways - Janus kinase (JAK) 1, JAK2, and activin A receptor type 1 (ACVR1) ...
Activin-like kinase type 1 receptor (ALK-1). *. Bone morphogenetic protein receptor type 2 (BMPR2) ... The BMPR2 (bone morphogenic receptor type 2) pathway is targeted by sotatercept, a novel drug. BMPR2 is the most common gene ... The endothelin pathway is targeted by bosentan, ambrisentan, and macitentan, which are oral endothelin-receptor antagonists ( ... Prostacyclin analogs, endothelin-receptor antagonists, and guanylate cyclase stimulators have been studied primarily in ...
... activin receptor-like kinase 5 (ALK5) receptor] and TGF-Beta/Smad signaling pathway in CNT-induced collagen production in human ... In this study, we investigated the activation of transforming growth factor-beta receptor-1 [TGF-Beta R1; i.e., ... Identification of TGF-beta receptor-1 as a key regulator of carbon nanotube-induced fibrogenesis. ...
Luspatercept-aamt is a receptor fusion protein consisting of a modified extracellular domain of the human activin receptor type ...
An additional study has demonstrated that the bone morphogenic protein (BMP) receptor activin-like kinase 3 (Alk3) is elevated ... growth factor receptor (PDGFR) activation after acute obstruction or ischemic insult, (b) pericyte genetic expression changes ( ... cells is driven by acquired cytokine receptor, gain-of-function mutations, most notably in the signal transducer, JAK2. In ...
Inhibition of the TGF? super family member myostatin/GDF-88 (a natural inhibitor of muscle growth) or its receptor (activin ... The specificity of these networks and processes during development may depend on localized ligands that interact with receptors ... Some are capable of forming different receptor/ligand combinations, and some may cause multiple different effects. Furthermore ... What are the most promising anabolic targets (cells, ligands/receptors, intracellular signaling pathways) for diseases and ...
Activin Receptors Entry term(s). Activin Receptor Activin Receptor like Kinase Activin Receptor like Kinases Activin Receptor- ... Activin Receptor. Activin Receptor like Kinase. Activin Receptor like Kinases. Activin Receptor-Like Kinases. Activin Receptor- ... Activin Receptor-like Kinase Kinase, Activin Receptor-like Kinases, Activin Receptor-like Receptor, Activin Receptor-like ... Kinase, Activin Receptor-like. Kinases, Activin Receptor-like. Receptor, Activin. Receptor-like Kinase, Activin. Receptor-like ...
ACTIVIN RECEPT. Entry Term(s). Activin Receptor Activin Receptor-Like Kinases Activin Receptor-like Kinase Receptor, Activin ... Receptor, Activin Term UI T218993. LexicalTag NON. ThesaurusID NLM (2002). Activin Receptor-Like Kinases Term UI T441227. Date ... Activin Receptor Term UI T218994. LexicalTag NON. ThesaurusID NLM (2002). Activin Receptor-like Kinase Term UI T259098. ... ACTIVIN RECEPTORS, TYPE II ) which then recruit and phosphorylate the type I receptors (ACTIVIN RECEPTORS, TYPE I ) with ...
ACTIVIN RECEPT. Entry Term(s). Activin Receptor Activin Receptor-Like Kinases Activin Receptor-like Kinase Receptor, Activin ... Receptor, Activin Term UI T218993. LexicalTag NON. ThesaurusID NLM (2002). Activin Receptor-Like Kinases Term UI T441227. Date ... Activin Receptor Term UI T218994. LexicalTag NON. ThesaurusID NLM (2002). Activin Receptor-like Kinase Term UI T259098. ... ACTIVIN RECEPTORS, TYPE II ) which then recruit and phosphorylate the type I receptors (ACTIVIN RECEPTORS, TYPE I ) with ...
Genetic association of the activin A receptor gene (ACVR2A) and pre-eclampsia. Molecular human reproduction 2009 Mar 15 (3): ... ACVR2A promoter polymorphism rs1424954 in the Activin-A signaling pathway in trophoblasts. Placenta 2015 Apr 36 (4): 345-9. ...
... that arises from gain of function mutations in the Activin Receptor Type 1 protein (ACVR1) gene. ACVR1 encodes for bone ... While some inhibitors of ALK2 receptor kinase (ATP-sensitive) are currently being tested in clinical trials, those drugs are ... morphogenetic protein (BMP) type I receptor ALK2, which is involved in the growth and development of bones. In FOP, muscle or ...
activin inhibitor activity. 0.00274327425429597. GO:0032925. regulation of activin receptor signaling pathway. ... activin receptor signaling pathway. 0.00274327425429597. GO:0046884. follicle-stimulating hormone secretion. ... transmembrane receptor protein serine/threonine kinase signaling pathway. 0.0117226808852989. GO:0051249. regulation of ... transforming growth factor beta receptor binding. 0.00457171996631325. GO:0046888. negative regulation of hormone secretion. ...
An autosomal recessive disorder of connective tissue caused by mutation(s) in the ACVR1 gene, encoding activin receptor type-1 ... C131021 TSHR Gene Mutation Thyroid Stimulating Hormone Receptor Gene Mutation TSH Receptor Defect,Thyrotropin Receptor Defect A ... C120386 Leptin Receptor Deficiency Leptin Receptor Deficiency Deficiency or dysfunction of the leptin receptor associated with ... C120370 Follicle Stimulating Hormone Receptor Deficiency Follicle Stimulating Hormone Receptor Deficiency FSH Receptor ...
Activin receptor-like kinase 1 is associated with immune cell infiltration and regulates CLEC14A transcription in cancer Matteo ... Targeting tumour vasculature by inhibiting activin receptor-like kinase (ALK)1 function Amaya García De Vinuesa, Matteo Bocci, ... Bone morphogenetic protein-9 inhibits lymphatic vessel formation via activin receptor-like kinase 1 during development and ... Gpr116 Receptor Regulates Distinctive Functions in Pneumocytes and Vascular Endothelium. Colin Niaudet, Jennifer J Hofmann, ...
  • Inadequate efficacy similarly halted the development of agents impinging on the activity of the activin receptor-like kinase (ALK)1, a member of the transforming growth factor-β superfamily. (lu.se)
  • CAMBRIDGE, Mass., January 19, 2021 - Sumitomo Dainippon Pharma Oncology, Inc., a developer of novel cancer therapeutics, today announced that the first patient has been dosed in a Phase 1/2 study evaluating the investigational agent TP-0184, an activin receptor-like kinase 2 (ALK2) and ALK5 inhibitor, for the treatment of anemia in adult patients with low or intermediate risk myelodysplastic syndromes (MDS). (massbio.org)
  • TP-0184 is an activin receptor-like kinase 2 (ALK2) and ALK5 inhibitor. (massbio.org)
  • Therefore, a mouse model was developed with a genetics-based approach that conditionally deleted the causative activin receptor-like kinase 1 ( Acvrl1 or Alk1 ) gene. (thejns.org)
  • i.e., activin receptor-like kinase 5 (ALK5) receptor] and TGF-Beta/Smad signaling pathway in CNT-induced collagen production in human lung fibroblasts. (cdc.gov)
  • With a differentiated mechanism of action, momelotinib has inhibitory ability along three important signalling pathways, Janus kinase (JAK) 1, and JAK2 and activin A receptor type I (ACVR1). (pharmaceutical-business-review.com)
  • Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. (idrblab.net)
  • 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. (bvsalud.org)
  • [ 24 ] Effective therapies for fibrodysplasia ossificans progressiva may be based on blocking activinlike kinase-2 or blocking of activin receptor IA/activin-like kinase 2 signaling. (medscape.com)
  • The genetic cause of fibrodysplasia ossificans progressiva lies within the ACVR1 gene, which encodes a type I BMP transmembrane receptor. (medscape.com)
  • A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva. (medscape.com)
  • Classic and atypical fibrodysplasia ossificans progressiva (FOP) phenotypes are caused by mutations in the bone morphogenetic protein (BMP) type I receptor ACVR1. (medscape.com)
  • These proteins are receptor-type kinases of Ser/Thr type, which have a single transmembrane domain and a specific hydrophilic Cys-rich ligand-binding domain. (wikipedia.org)
  • 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). (bvsalud.org)
  • 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. (bvsalud.org)
  • An Activin receptor is a receptor which binds activin. (wikipedia.org)
  • GnRH binds to GnRH- receptors on pituitary gonadotropes ( 4 , 9 ). (frontiersin.org)
  • In rodents, after activin binds to gonadotrope membrane activin receptors, transcription factors, such as Smad4 are recruited and directly interact with the FSHβ gene promoter to upregulate its expression ( 15 , 18 ). (frontiersin.org)
  • Response to "Mutations of the NOGGIN and of the activin A type I receptor genes in fibrodysplasia ossificans progressiva (FOP)" by Lucotte et al. (ox.ac.uk)
  • FSH synthesis and release are also regulated by several other proteins, such as follistatin, inhibin, and activin ( 12 - 17 ). (frontiersin.org)
  • A novel mutation in the activin A type 1 receptor gene was described in one patient. (medscape.com)
  • Proprotein convertase subtilisin/kexin type-9 (PCSK9) is a posttranslational regulator of the LDL receptor (LDLR). (jci.org)
  • Both pathways involve sex-specific molecular signals from the somatic cells of the developing gonads and a suite of intrinsic receptors, signal transducers, transcription factors, RNA stability factors, and epigenetic modulators that act in complex, interconnected positive and negative regulatory networks. (annualreviews.org)
  • Identification of TGF-beta receptor-1 as a key regulator of carbon nanotube -induced fibrogenesis. (cdc.gov)
  • To elucidate the cause of motor symptoms in Parkinson's disease, we analyzed the mechanism of motor control using genetically engineered mice, focusing on the roles of D1 and D2 dopamine receptors (D1R and D2R) and NMDA receptor-mediated signal transduction, and especially found the importance of D1R-mediated signal transduction. (nii.ac.jp)
  • The requirement for tumor angiogenesis has been therapeutically exploited in the clinical setting mainly by means of inhibition of the vascular endothelial growth factor family of ligands and receptors. (lu.se)
  • 2) RT-PCR analysis of progesterone receptor, activin βA, activin βB, and activin receptor II mRNA was completed with L19 ribosomal protein mRNA as control. (topsan.org)
  • Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3. (idrblab.net)
  • Our group and others have generated a number of FSH ligand and receptor GOF mouse models. (frontiersin.org)
  • Form 10-K and Form 10-Q filings with the deep understanding of activin biology at Lilly with the. (koelnagenda-archiv.de)
  • Form 10-K and Form 10-Q filings with the United States Securities and Exchange Commission (the "SEC"). II A and B receptors to block activin and myostatin signaling. (koelnagenda-archiv.de)
  • 2011 . Activin/Nodal signaling controls divergent transcriptional networks in human embryonic stem cells and in endoderm progenitors. (annualreviews.org)
  • Among those, transforming growth factor-beta (TGF-beta) ligands and receptors demonstrate a critical role during EMT. (nih.gov)
  • In the chick, TGF-beta ligands and some receptors have specific functions during EMT. (nih.gov)
  • Functionally, endoglin modulates TGF- β superfamily signaling pathways through interaction with ligand-binding receptors or direct binding of ligands [ 9 , 11 , 12 ]. (hindawi.com)
  • Bimagrumab is a first-in-class, fully human IgG1/λ monoclonal antibody to activin type II receptors that blocks binding of ligands including myostatin, activins and GDF11. (pipelinereview.com)
  • However, expression of receptors and ligands in cell lines does not necessarily indicate parallel alterations in PDAC in vivo . (biomedcentral.com)
  • Specifically, it binds to and inhibits activin A and other TGF- β superfamily ligands. (edrugz.net)
  • In immunosuppressed animals with combined filaggrin and STAT3 defects in the skin, vaccinia scarification yielded pronounced local and distant viral spread accompanied by elevated levels of the TGF-b family ligand activin A. Small molecule inhibition of activin receptor (ALK5) signaling promoted viral clearance from the skin but not disseminated infection sites. (nih.gov)
  • Receptors involved in the EMT process include TGF-beta receptor type II (TBRII), TBRIII, endoglin and the TBRI receptors, ALK2 and ALK5. (nih.gov)
  • Further studies will reveal the identification of ligand and receptor-specific activities. (nih.gov)
  • The transforming growth factor beta (TGF- β ) superfamily, which includes TGF- β isoforms, activins, and bone morphogenetic proteins (BMPs), is known to regulate many processes, including wound healing, angiogenesis, and immune responses [ 5 - 8 ]. (hindawi.com)
  • 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. (bvsalud.org)
  • TNFRSF 1 1 A is a member of the TNF-receptor superfamily. (targetmol.com)
  • GITR, also known as TNFRSF 1 8(CD 3 57), belongs to the tumor necrosis factor receptor (TNF-R) superfamily. (targetmol.com)
  • Activin type II receptor restoration in ACVR2-deficient colon cancer cells induces transforming growth factor-beta response pathway genes. (nih.gov)
  • Previous studies have associated the activin type II receptor (ActRII) pathway with muscle wasting and other aging-related conditions. (nih.gov)
  • ACVR2A promoter polymorphism rs1424954 in the Activin-A signaling pathway in trophoblasts. (cdc.gov)
  • Interleukin 1 5 Receptor alpha (IL- 1 5Rα) is a transmembrane glycoprotein that plays a pleiotropic role in immune development and function, including the positive maintenance of lymphocyte homeostasis. (targetmol.com)
  • Linzess (Linaclotide) is the first-in-class medicine that acts on the intestinal epithelial cells and stimulates the transmembrane Guanylate Cyclase 2C receptors (GC-2C). (edrugz.net)
  • We are currently evaluating the role of activin A in shaping innate and adaptive immune responses to skin infection in mice, and testing TGF-b family signaling inhibitors, and other potential co-therapies, to identify VIG-sparing combinations. (nih.gov)
  • With nutrient-stimulated hormone therapies for obesity in phase 3 trials, and activin-receptor inhibitors the next upcoming drug class, highly effective treatments for obesity are on the horizon. (medscape.com)
  • She then briefly touched on activin receptor inhibitors -"the next [medication] class that I think will be up and coming," she speculated. (medscape.com)
  • Multiple transforming growth factor-beta isoforms and receptors function during epithelial-mesenchymal cell transformation in the embryonic heart. (nih.gov)
  • The activin type II receptor (ACVR2) gene is a putative tumor suppressor gene that is frequently mutated in microsatellite-unstable colon cancers (MSI-H colon cancers). (nih.gov)
  • ACVR2 is a member of the transforming growth factor (TGF)-beta type II receptor (TGFBR2) family and controls cell growth and differentiation. (nih.gov)
  • This observed similarity between the activin and TGF-beta signaling systems suggests that activin may serve as an alternative activator of TGF-beta effectors, including SMADs, and that frameshift mutation of ACVR2 may contribute to MSI-H colon tumorigenesis via disruption of alternate TGF-beta effector pathways. (nih.gov)
  • CDD866 can bind to the receptor and prevent activin A from activating it. (nih.gov)
  • Activin receptors also bind TRANSFORMING GROWTH FACTOR BETA . (bvsalud.org)
  • Genetic association of the activin A receptor gene (ACVR2A) and pre-eclampsia. (cdc.gov)
  • The BMPR2 gene provides instructions for making a protein called bone morphogenetic protein receptor type 2. (encyclopedia.pub)
  • Zavegepant Nasal Spray (Zavzpret) is a small-molecule, competitive antagonist of the calcitonin gene-related peptide (CGRP) receptor, which is a target for the treatment of migraine. (edrugz.net)
  • A plasma membrane-associated form of the androgen receptor enhances nuclear androgen signaling in osteoblasts and prostate cancer cells. (chip-atlas.org)
  • Myelofibrosis is the principal pathologic finding in a hematologic disease called "primary myelofibrosis with myeloid metaplasia" that is included among the myeloproliferative disorders, all of which are neoplastic, clonal blood diseases in which a dysregulated excessive or dysplastic production of blood cells is driven by acquired cytokine receptor, gain-of-function mutations, most notably in the signal transducer, JAK2. (nih.gov)
  • About half of the mutations involved in this condition disrupt the assembly of bone morphogenetic protein receptor type 2, reducing the amount of this protein in cells. (encyclopedia.pub)
  • Other mutations prevent bone morphogenetic protein receptor type 2 from reaching the cell surface or alter its structure so it cannot receive or transmit signals. (encyclopedia.pub)
  • Bone morphogenetic protein receptor type 2 spans the cell membrane, so that one end of the protein is on the outer surface of the cell and the other end remains inside the cell. (encyclopedia.pub)
  • FST plays a role in tumourigenesis, metastasis and angiogenesis of solid tumours through its interaction with activin and BMPs, thus resulting in pathophysiological function. (cusabio.com)
  • When the scientists injected young, healthy mice with activin A, ActRII was activated, and heart function declined. (nih.gov)
  • 17. Rapid Activation of Bone Morphogenic Protein 9 by Receptor-mediated Displacement of Pro-domains. (nih.gov)
  • Jastreboff, from Yale University and the Yale Center for Weight Management, New Haven, Connecticut, provided an overview of the many nutrient-stimulated hormone-based antiobesity therapies in late phases of development - including dual and triple therapies with glucagon-like peptide 1 receptor agonists (GLP-1 RAs), glucose-dependent insulinotropic polypeptide (GIP) agonists, glucagon , and amylin. (medscape.com)
  • Sotatercept is a dimeric fusion protein containing the extracellular domain of the activin receptor 2A (ACVR2A) fused to the Fc domain of human IgG1. (pharmaceutical-technology.com)
  • WINREVAIR (Sotatercept-csrk) is a recombinant activin receptor type IIA-Fc (ActRIIA-Fc) fusion protein. (edrugz.net)
  • CR-1 is reported to have a paracrine activity as a Nodal co-receptor, although CR-1 is primarily produced as a glycosylphosphatidylinositol (GPI)-anchored membrane protein. (fujita-hu.ac.jp)
  • These observations suggest that GPI attachment of CR-1 is required for the paracrine activity as a Nodal co-receptor. (fujita-hu.ac.jp)
  • Cripto-1 (CR-1) has an indispensable role as a Nodal co-receptor for patterning of body axis in embryonic development. (fujita-hu.ac.jp)
  • Hence, local concentrations of FS288 and Activin A may influence the response of some cell types to AMH. (cusabio.com)
  • CD47 contains 1 Ig-like V-type (immunoglobulin-like) domain and is a receptor for the C-terminal cell binding domain of thrombospondin. (targetmol.com)
  • Bimagrumab is a first-in-class activin type II receptor monoclonal antibody previously evaluated in various muscle wasting indications based on its effects on muscle anabolism. (pipelinereview.com)
  • Activin A, a direct target of FS288, did not itself induce reporter activity in P19 cells, but did prevent the FS288-induced increase in AMH signaling. (cusabio.com)
  • Althoughthe specific mechanisms that dictate its biological aggressiveness are notclearly established, it is characterized by a variety of molecularalterations as well as by the overexpression of mitogenic and angiogenicgrowth factors and their receptors. (biomedcentral.com)
  • Identification of TGF-beta receptor-1 as a key regulator of carbon nanotube -induced fibrogenesis. (cdc.gov)

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