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.
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.
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).
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.
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.
An interleukin-1 receptor subtype that competes with the INTERLEUKIN-1 RECEPTOR TYPE I for binding to INTERLEUKIN-1ALPHA and INTERLEUKIN-1BETA. The interleukin-1 type II receptor appears to lack signal transduction capability. Therefore it may act as a "decoy" receptor that modulates the activity of its ligands. Both membrane-bound and soluble forms of the receptor have been identified.
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.
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.
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 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.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
A receptor-regulated smad protein that undergoes PHOSPHORYLATION by ACTIVIN RECEPTORS, TYPE I. It regulates TRANSFORMING GROWTH FACTOR BETA and ACTIVIN signaling.
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 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.
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.
Cell surface receptors that are specific for INTERLEUKIN-1. Included under this heading are signaling receptors, non-signaling receptors and accessory proteins required for receptor signaling. Signaling from interleukin-1 receptors occurs via interaction with SIGNAL TRANSDUCING ADAPTOR PROTEINS such as MYELOID DIFFERENTIATION FACTOR 88.
A tumor necrosis factor receptor subtype that is expressed primarily in IMMUNE SYSTEM cells. It has specificity for membrane-bound form of TUMOR NECROSIS FACTORS and mediates intracellular-signaling through TNF RECEPTOR ASSOCIATED FACTORS.
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.

Lack of regulation in the heart forming region of avian embryos. (1/298)

The ability to regenerate a heart after ablation of cardiogenic mesoderm has been demonstrated in early stage fish and amphibian embryos but this type of regulation of the heart field has not been seen in avians or mammals. The regulative potential of the cardiogenic mesoderm was examined in avian embryos and related to the spatial expression of genes implicated in early cardiogenesis. With the identification of early cardiac regulators such as bmp-2 and nkx-2.5, it is now possible to reconcile classical embryological studies with molecular mechanisms of cardiac lineage determination in vivo. The most anterior lateral embryonic cells were identified as the region that becomes the heart and removal of all or any subset of these cells resulted in the loss of corresponding cardiac structures. In addition, removal of the lateral heart forming mesoderm while leaving the lateral endoderm intact also results in loss of cardiac structures. Thus the medial anterior mesoderm cannot be recruited into the heart lineage in vivo even in the presence of potentially cardiac inducing endoderm. In situ analysis demonstrated that genes involved in early events of cardiogenesis such as bone morphogenetic protein 2 (bmp-2) and nkx-2.5 are expressed coincidentally with the mapped far lateral heart forming region. The activin type IIa receptor (actR-IIa) is a potential mediator of BMP signaling since it is expressed throughout the anterior mesoderm with the highest level of expression occurring in the lateral prospective heart cells. The posterior boundary of actR-IIa is consistent with the posterior boundary of nkx-2.5 expression, supporting a model whereby ActR-IIa is involved in restricting the heart forming region to an anterior subset of lateral cells exposed to BMP-2. Analysis of the cardiogenic potential of the lateral plate mesoderm posterior to nkx-2.5 and actR-IIa expression demonstrated that these cells are not cardiogenic in vitro and that removal of these cells from the embryo does not result in loss of heart tissue in vivo. Thus, the region of the avian embryo that will become the heart is defined medially, laterally, and posteriorly by nkx-2.5 gene expression. Removal of all or part of the nkx-2.5 expressing region results in the loss of corresponding heart structures, demonstrating the inability of the chick embryo to regenerate cardiac tissue in vivo at stages after nkx-2.5 expression is initiated.  (+info)

Identification of two amino acids in activin A that are important for biological activity and binding to the activin type II receptors. (2/298)

Activins are members of the transforming growth factor-beta family of growth and differentiation factors. In this paper, we report the results of a structure-function analysis of activin A. The primary targets for directed mutagenesis were charged, individual amino acids located in accessible domains of the protein, concentrating on those that differ from transforming growth factor-beta2, the x-ray crystal structure of which is known. Based on the activities of the recombinant activin mutants in two bioassays, 4 out of 39 mutant proteins (D27K, K102A, K102E, and K102R) produced in a vaccinia virus system were selected for further investigation. After production in insect cells and purification of these four mutants to homogeneity, they were studied in bioassays and in cross-linking experiments involving transfected receptor combinations. Mutant D27K has a 2-fold higher specific bio-activity and binding affinity to an ActRIIA/ALK-4 activin receptor complex than wild type activin, whereas mutant K102E had no detectable biological activity and did not bind to any of the activin receptors. Mutant K102R and wild type activin bound to all the activin receptor combinations tested and were equipotent in bioassays. Our results with the Lys-102 mutants indicate that the positive charge of amino acid 102 is important for biological activity and type II receptor binding of activins.  (+info)

Control of digit formation by activin signalling. (3/298)

Major advances in the genetics of vertebrate limb development have been obtained in recent years. However, the nature of the signals which trigger differentiation of the mesoderm to form the limb skeleton remains elusive. Previously, we have obtained evidence for a role of TGFbeta2 in digit formation. Here, we show that activins A and B and/or AB are also signals involved in digit skeletogenesis. activin betaA gene expression correlates with the initiation of digit chondrogenesis while activin betaB is expressed coincidently with the formation of the last phalanx of each digit. Exogenous administration of activins A, B or AB into the interdigital regions induces the formation of extra digits. follistatin, a natural antagonist of activins, is expressed, under the control of activin, peripherally to the digit chondrogenic aggregates marking the prospective tendinous blastemas. Exogenous application of follistatin blocks physiological and activin-induced digit formation. Evidence for a close interaction between activins and other signalling molecules, such as BMPs and FGFs, operating at the distal tip of the limb at these stages is also provided. Chondrogenesis by activins is mediated by BMPs through the regulation of the BMP receptor bmpR-1b and in turn activin expression is upregulated by BMP signalling. In addition, AER hyperactivity secondary to Wnt3A misexpression or local administration of FGFs, inhibits activin expression. In correlation with the restricted expression of activins in the course of digit formation, neither activin nor follistatin treatment affects the development of the skeletal components of the stylopod or zeugopod indicating that the formation of the limb skeleton is regulated by segment-specific chondrogenic signals.  (+info)

Impaired differentiation of endocrine and exocrine cells of the pancreas in transgenic mouse expressing the truncated type II activin receptor. (4/298)

Activin A is expressed in endocrine precursor cells of the fetal pancreatic anlage. To determine the physiological significance of activins in the pancreas, a transgenic mouse line expressing the truncated type II activin receptor under the control of beta-actin promoter was developed. Histological analyses of the pancreas revealed that the pancreatic islets of the transgenic mouse were small in size and were located mainly along the pancreatic ducts. Immunoreactive insulin was detected in islets, some acinar cells, and in some epithelial cells in the duct. In addition, there were abnormal endocrine cells outside the islets. The shape and the size of the endocrine cells varied and some of them were larger than islets. These cells expressed immunoreactive insulin and glucagon. In the exocrine portion, there were morphologically abnormal exocrine cells, which did not form a typical acinar structure. The cells lacked spatial polarity characteristics of acinar cells but expressed immunoreactive amylase, which was distributed diffusely in the cytoplasm. Plasma glucose concentration was normal in the transgenic mouse before and after the administration of glucose. The insulin content of the pancreas in transgenic and normal mice was nearly identical. These results suggest that activins or related ligands regulate the differentiation of the pancreatic endocrine and exocrine cells.  (+info)

The type II activin receptors are essential for egg cylinder growth, gastrulation, and rostral head development in mice. (5/298)

The type II activin receptors, ActRIIA and ActRIIB, have been shown to play critical roles in axial patterning and organ development in mice. To investigate whether their function is required for mesoderm formation and gastrulation as implicated in Xenopus studies, we generated mice carrying both receptor mutations by interbreeding the ActRIIA and ActRIIB knockout mutants. We found that embryos homozygous for both receptor mutations were growth arrested at the egg cylinder stage and did not form mesoderm. Further analyses revealed that ActRIIA(-/-)ActRIIB(+/-) and about 15% of the ActRIIA(-/-) embryos failed to form an elongated primitive streak, resulting in severe disruption of mesoderm formation in the embryo proper. Interestingly, we observed similar gastrulation defects in ActRIIA(-/-)nodal(+/-) double mutants, which, if they developed beyond the gastrulation stage, displayed rostral head defects and cyclopia. These results provide genetic evidence that type II activin receptors are required for egg cylinder growth, primitive streak formation, and rostral head development in mice.  (+info)

Activin stimulation of zebrafish oocyte maturation in vitro and its potential role in mediating gonadotropin-induced oocyte maturation. (6/298)

Activin plays important roles in the regulation of vertebrate reproduction. Using zebrafish, Danio rerio, as a model, the present study aimed at investigating the role of activin in the regulation of final oocyte maturation. Administration of recombinant goldfish activin B significantly increased the rate of oocyte maturation in vitro in a dose- and time-dependent manner. The effect of activin seemed to be additive to the effects of gonadotropin (hCG) and 17alpha,20beta-dihydroxyprogesterone, a potent maturation-inducing hormone in teleosts. The specificity of the activin action was confirmed by coincubation with recombinant human follistatin, which completely abolished the stimulatory effect of activin B. Interestingly, follistatin also significantly inhibited hCG-induced oocyte maturation, suggesting that endogenous activin may be a downstream mediator of gonadotropin actions. No effect of activin B was observed in the presence of actinomycin D, indicating that the action of activin may involve changes in transcriptional activity. These results, together with the demonstration that activin and its type II receptor are expressed in the zebrafish ovary, strongly suggest a paracrine/autocrine role for activin in the controlling of final oocyte maturation.  (+info)

Characterization of bone morphogenetic protein-6 signaling pathways in osteoblast differentiation. (7/298)

Bone morphogenetic protein (BMP)-6 is a member of the transforming growth factor (TGF)-(&bgr;) superfamily, and is most similar to BMP-5, osteogenic protein (OP)-1/BMP-7, and OP-2/BMP-8. In the present study, we characterized the endogenous BMP-6 signaling pathway during osteoblast differentiation. BMP-6 strongly induced alkaline phosphatase (ALP) activity in cells of osteoblast lineage, including C2C12 cells, MC3T3-E1 cells, and ROB-C26 cells. The profile of binding of BMP-6 to type I and type II receptors was similar to that of OP-1/BMP-7 in C2C12 cells and MC3T3-E1 cells; BMP-6 strongly bound to activin receptor-like kinase (ALK)-2 (also termed ActR-I), together with type II receptors, i.e. BMP type II receptor (BMPR-II) and activin type II receptor (ActR-II). In addition, BMP-6 weakly bound to BMPR-IA (ALK-3), to which BMP-2 also bound. In contrast, binding of BMP-6 to BMPR-IB (ALK-6), and less efficiently to ALK-2 and BMPR-IA, together with BMPR-II was detected in ROB-C26 cells. Intracellular signalling was further studied using C2C12 and MC3T3-E1 cells. Among the receptor-regulated Smads activated by BMP receptors, BMP-6 strongly induced phosphorylation and nuclear accumulation of Smad5, and less efficiently those of Smad1. However, Smad8 was constitutively phosphorylated, and no further phosphorylation or nuclear accumulation of Smad8 by BMP-6 was observed. These findings indicate that in the process of differentiation to osteoblasts, BMP-6 binds to ALK-2 as well as other type I receptors, and transduces signals mainly through Smad5 and possibly through Smad1.  (+info)

Mouse Lefty2 and zebrafish antivin are feedback inhibitors of nodal signaling during vertebrate gastrulation. (8/298)

Mammalian lefty and zebrafish antivin form a subgroup of the TGF beta superfamily. We report that mouse mutants for lefty2 have an expanded primitive streak and form excess mesoderm, a phenotype opposite to that of mutants for the TGF beta gene nodal. Analogously, overexpression of Antivin or Lefty2 in zebrafish embryos blocks head and trunk mesoderm formation, a phenotype identical to that of mutants caused by loss of Nodal signaling. The lefty2 mutant phenotype is partially suppressed by heterozygosity for nodal. Similarly, the effects of Antivin and Lefty2 can be suppressed by overexpression of the nodal-related genes cyclops and squint or the extracellular domain of ActRIIB. Expression of antivin is dependent on Nodal signaling, revealing a feedback loop wherein Nodal signals induce their antagonists Lefty2 and Antivin to restrict Nodal signaling during gastrulation.  (+info)

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.

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.

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.

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.

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.

Interleukin-1 type II receptors (IL-1RII), also known as IL-1 receptor type 2 or CD121b, are membrane-bound receptors that belong to the interleukin-1 receptor family. They are encoded by the IL1R2 gene in humans. These receptors have a similar structure to the Interleukin-1 type I receptors (IL-1RI) but do not transmit signals upon IL-1 binding. Instead, IL-1RII acts as a decoy receptor, preventing IL-1 from interacting with its signaling receptor, IL-1RI. This interaction helps regulate the inflammatory response and limits the potential for excessive or inappropriate immune activation.

IL-1RII can be found on various cell types, including B cells, monocytes, and fibroblasts. In addition to its membrane-bound form, a soluble form of IL-1RII (sIL-1RII) is generated through alternative splicing or proteolytic cleavage. The soluble receptor can also bind to IL-1 and inhibit its activity, contributing to the regulation of the immune response.

In summary, Interleukin-1 type II receptors (IL-1RII) are decoy receptors that downregulate the inflammatory response by preventing the interaction between interleukin-1 and its signaling receptor, IL-1RI. They exist in both membrane-bound and soluble forms and can be found on various cell types.

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.

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.

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.

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.

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.

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.

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.

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.

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.

Interleukin-1 (IL-1) receptors are a type of cell surface receptor that bind to and mediate the effects of interleukin-1 cytokines, which are involved in the regulation of inflammatory and immune responses. There are two main types of IL-1 receptors:

1. Type I IL-1 receptor (IL-1R1): This is a transmembrane protein that consists of three domains - an extracellular domain, a transmembrane domain, and an intracellular domain. The extracellular domain contains the binding site for IL-1 cytokines, while the intracellular domain is involved in signal transduction and activation of downstream signaling pathways.
2. Type II IL-1 receptor (IL-1R2): This is a decoy receptor that lacks an intracellular signaling domain and functions to regulate IL-1 activity by preventing its interaction with IL-1R1.

IL-1 receptors are widely expressed in various tissues and cell types, including immune cells, endothelial cells, and nervous system cells. Activation of IL-1 receptors leads to the induction of a variety of biological responses, such as fever, production of acute phase proteins, activation of immune cells, and modulation of pain sensitivity. Dysregulation of IL-1 signaling has been implicated in various pathological conditions, including autoimmune diseases, chronic inflammation, and neurodegenerative disorders.

Tumor Necrosis Factor (TNF) Receptor II, also known as TNFRSF1B or CD120b, is a type of receptor that binds to the TNF-alpha cytokine and plays a crucial role in the immune system. It is a transmembrane protein mainly expressed on the surface of various cells including immune cells, fibroblasts, and endothelial cells.

The activation of TNFRII by TNF-alpha leads to the initiation of intracellular signaling pathways that regulate inflammatory responses, cell survival, differentiation, and apoptosis (programmed cell death). Dysregulation of this receptor's function has been implicated in several pathological conditions such as autoimmune diseases, cancer, and neurodegenerative disorders.

TNFRII is a member of the TNF receptor superfamily (TNFRSF) and consists of an extracellular domain containing multiple cysteine-rich motifs that facilitate ligand binding, a transmembrane domain, and an intracellular domain responsible for signal transduction. Upon ligand binding, TNFRII forms complexes with various adaptor proteins to activate downstream signaling cascades, ultimately leading to the activation of nuclear factor-kappa B (NF-κB), mitogen-activated protein kinases (MAPKs), and other signaling molecules.

In summary, Tumor Necrosis Factor Receptor II is a key regulator of immune responses and cell fate decisions, with its dysregulation contributing to various pathological conditions.

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.

There are two activin type two receptors: ACVR2A and ACVR2B. Despite the large amount of processes that these ligands regulate ... inhibin/activin betaA and betaB and the activin type II and inhibin beta-glycan receptors in the developing human testis". ... which recruits and trans-phosphorylates a type I receptor. The type I receptor recruits a receptor regulated SMAD (R-SMAD) ... "Regulation of muscle growth by multiple ligands signaling through activin type II receptors". Proc. Natl. Acad. Sci. U.S.A. 102 ...
A ligand binds to a Type two receptor, which recruits and trans-phosphorylate a type I receptor. The type I receptor recruits a ... There are three type I Activin receptors: ACVR1, ACVR1B, and ACVR1C. Each bind to a specific type II receptor-ligand complex. ... 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 ( ...
Type II receptors are considered to be constitutively active kinases. This gene encodes activin A type IIB receptor, which ... and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a ... "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. ... "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. ...
"Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. ... and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a ... resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively ... "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. ...
"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, ... It is also known as activin receptor-like kinase 1, or ALK1. This gene encodes a type I cell-surface receptor for the TGF-beta ... "Mutations in the activin receptor-like kinase 1 gene in hereditary haemorrhagic telangiectasia type 2". Nature Genetics. 13 (2 ...
... an activin receptor type II inhibitor, on pituitary neurohormonal axes". Clinical Endocrinology. 88 (6): 908-919. doi:10.1111/ ... It binds to and inhibits activin receptor type-2B. On August 20, 2013, it was announced that bimagrumab had received a ... In 2014, Bimagrumab entered Phase II development, with some research indicating clinical effects. Novartis planned to apply in ... is safe and effective for treating excess adiposity and metabolic disturbances of adult patients with obesity and type 2 ...
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 ... December 2005). "Regulation of muscle growth by multiple ligands signaling through activin type II receptors". Proceedings of ... Treating progeric mice with soluble activin receptor type IIB before the onset of premature ageing signs appear to protects ...
January 2008). "MicroRNA miR-24 inhibits erythropoiesis by targeting activin type I receptor ALK4". Blood. 111 (2): 588-95. doi ... Recently, miR-24 has been shown to suppress expression of two crucial cell cycle control genes, E2F2 and Myc in hematopoietic ... 199 (2): 347-63. doi:10.1083/jcb.201203134. PMC 3471232. PMID 23071155. Wang Q, Huang Z, Xue H, et al. ( ...
"Identification and characterization of a PDZ protein that interacts with activin type II receptors". J Biol Chem. 275 (8): 5485 ... This encoded protein is characterized by two WW domains, a guanylate kinase-like domain, and multiple PDZ domains. It has ... 1998). "Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins". Mol. Cell. Neurosci ... Nakayama M, Kikuno R, Ohara O (2003). "Protein-protein interactions between large proteins: two-hybrid screening using a ...
... and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. ... 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 ... but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II ... "Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs". Mol. Cell ...
"Determination of type I receptor specificity by the type II receptors for TGF-beta or activin". Science. 262 (5135): 900-2. ... Choy L, Derynck R (November 1998). "The type II transforming growth factor (TGF)-beta receptor-interacting protein TRIP-1 acts ... 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 ... 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 ... "Determination of type I receptor specificity by the type II receptors for TGF-beta or activin". Science. 262 (5135): 900-2. ... "Entrez Gene: TGFBR1 transforming growth factor, beta receptor I (activin A receptor type II-like kinase, 53kDa)". Razani B, ... "Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs". Molecular ...
"Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase". Nature ... Ploug M, Ellis V (August 1994). "Structure-function relationships in the receptor for urokinase-type plasminogen activator. ... such as the activin type 2 receptor; and bone morphogenetic protein receptor, type IA. Other LU domain proteins are small ... Other receptors with LU domains include members of the transforming growth factor beta receptor (TGF-beta) superfamily, ...
"Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase". Nature ... Besides uPAR, other receptors with LU domains include members of the transforming growth factor beta receptor (TGF-beta) ... such as the activin type 2 receptor; and bone morphogenetic protein receptor, type IA. Other LU domain proteins are small ... "Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen ...
... activin complex reveals antagonism of both type I and type II receptor binding". Developmental Cell. 9 (4): 535-543. doi: ... Walsh S, Metter EJ, Ferrucci L, Roth SM (June 2007). "Activin-type II receptor B (ACVR2B) and follistatin haplotype ... Lambert-Messerlian G, Eklund E, Pinar H, Tantravahi U, Schneyer AL (2007). "Activin subunit and receptor expression in normal ... Two, FS-288 and FS-315, are known to be created by alternative splicing of the primary mRNA transcript. FS-300 (porcine ...
"Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent ... II. Doxorubicin transport in lung cancer by RLIP76". Int. J. Oncol. 22 (4): 713-20. doi:10.3892/ijo.22.4.713. PMID 12632060. ... involvement of the Ral pathway in receptor endocytosis" (PDF). J. Cell Sci. 113 (16): 2837-44. doi:10.1242/jcs.113.16.2837. ... 48 (2): 551-62. doi:10.18388/abp.2001_3938. PMID 11732624. Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, ...
"Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent ... "Novel factors in regulation of activin signaling". Molecular and Cellular Endocrinology. 225 (1-2): 1-8. doi:10.1016/j.mce. ... "Novel factors in regulation of activin signaling". Molecular and Cellular Endocrinology. 225 (1-2): 1-8. doi:10.1016/j.mce. ... "Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse ...
"Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent ... The product of this gene is part of a protein complex that regulates the endocytosis of growth factor receptors. The encoded ... Its expression can negatively affect receptor internalization and inhibit growth factor signaling. Multiple transcript variants ... "Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis". Oncogene. 18 (43): 5915-22. doi:10.1038/sj. ...
... the ACVR1 gene encodes the activin receptor type-1 transmembrane kinase that bind BMP receptors (Type I BMPR and Type II BMPR) ... ACVR1 encodes activin receptor type-1, a BMP type-1 receptor. The mutation causes substitution of codon 206 from arginine to ... Lin, Shuxian; Svoboda, Kathy K. H.; Feng, Jian Q.; Jiang, Xinquan (5 April 2016). "The biological function of type I receptors ... Fibro/adipogenic progenitors (FAPs) may be the disease-causing cell type responsible for activin A dependent ectopic bone ...
ACE-011 was a chimeric protein, created by fusing the binding portion of the activin type 2 receptors to part of an antibody; ... a protein therapeutic that was an activin type 2 receptor antagonist intended to treat bone loss. ... the resulting protein binds to activin and prevents it from acting. Knopf took over as CEO in 2007. He became known for showing ... At that time, the company had three protein therapeutic candidates being studied in 12 Phase 2 clinical trials, including ...
... also known has Activin A receptor, type I (ACVR1), and the other type II receptors BMPRII and ActRIIA. GDF2 and BMP10 are the ... and activin type II receptors balance BMP9 signals mediated by activin receptor-like kinase-1 in human pulmonary artery ... start with a ligand binding with a high affinity type I receptor (ALK1-7) followed by the recruitment of a type II receptor( ... The physiological receptor of GDF2 is activin receptor-like kinase 1, ALK1 (also called ACVRL1), an endothelial-specific type I ...
... resulting in phosphorylation of type I receptors by type II receptors. This gene encodes activin A type I receptor which ... and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a ... and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding ... Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I ( I and IB) ...
8 September - Scientists report that suppressing activin type 2 receptors-signalling proteins myostatin and activin A via ... 17 July - Scientists report that yeast cells of the same genetic material and within the same environment age in two distinct ... 1997 - British scientists, led by Ian Wilmut from the Roslin Institute, report cloning Dolly the sheep using DNA from two adult ... The paper's senior author cautions that the two neutralizing systems they demonstrated in cage trials "should not be used with ...
After visualizing droplet dispersal for face shields and masks with exhalation valves scientists report that these two types of ... Scientists report that suppressing activin type 2 receptors-signalling proteins myostatin and activin A via activin A/myostatin ... In two studies researchers of the Global Carbon Project summarise and analyse new estimates of the global methane budget and ... 31 July Two ice caps in Nunavut, Canada have disappeared completely, confirming predictions of a study published in 2017 that ...
... error Type II lattice Type II string theory Type-II superconductor Type II supernova Type 2 sequence Activin type 2 receptors ... a Japanese tank Type II keratin Type II error used in statistics for a "false negative" ... Type II, a Japanese submachine gun Type 2 12 cm Mortar, a Japanese weapon Type 2 20 mm AA machine cannon, a Japanese weapon ... Motorola Type II Multiple endocrine neoplasia type 2 Neurofibromatosis type II R-Type II Type I and type II errors Type II ...
... activin A receptor type II-like 1f ANKRD33: encoding protein Ankyrin repeat domain 33 APOF: encoding protein Apolipoprotein F ... type II, gamma PIWIL1: encoding protein Piwi-like protein 1 PLBD1: encoding protein Phospholipase B domain containing 1 1 POP5 ... encoding protein Gaba type a receptor associated protein like 1 GPD1: encoding protein Glycerol-3-phosphate dehydrogenase 1 ... non-receptor type 11 (Noonan syndrome 1) PUS1: encoding enzyme tRNA pseudouridine synthase A PUS7L: encoding enzyme ...
... type I, type II, and type III. There are seven type I receptors, termed the activin-like receptors (ALK1-7), five type II ... In the transduction pathway, ligand-bound type II receptors activate type I receptors by phosphorylation, which then ... The Type I receptors have a glycine-serine (GS, or TTSGSGSG) repeat motif of around 30 AA, a target of type II activity. At ... Unlike the Type I and II receptors which are kinases, TGFBR3 has a Zona pellucida-like domain. Its core domain binds TGF-beta ...
... resulting in phosphorylation of type I receptors by type II receptors. This gene encodes activin A type IB receptor, composed ... and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a ... "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. ... "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. ...
... signaling pathway by repressing the expression of TGF-beta receptor type II". Molecular and Cellular Biology. 27 (23): 8228- ... where the TGF-β receptor is located. The receptors for TGF-β, (including nodal, activin, myostatin and other family members) ... The complex of two SMAD3 (or of two SMAD2) and one SMAD4 binds directly to DNA though interactions of the MH1 domain. These ... October 2007). "Profibrogenic transforming growth factor-beta/activin receptor-like kinase 5 signaling via connective tissue ...
There are two activin type two receptors: ACVR2A and ACVR2B. Despite the large amount of processes that these ligands regulate ... inhibin/activin betaA and betaB and the activin type II and inhibin beta-glycan receptors in the developing human testis". ... which recruits and trans-phosphorylates a type I receptor. The type I receptor recruits a receptor regulated SMAD (R-SMAD) ... "Regulation of muscle growth by multiple ligands signaling through activin type II receptors". Proc. Natl. Acad. Sci. U.S.A. 102 ...
Activin is growth suppressive and enhances migration similar to transforming growth factor beta in colon cancer, indic … ... ACVR2-complemented MSI-H colon cancers restore activin-SMAD signaling, decrease growth, and slow their cell cycle following ... Activin Receptors, Type II / drug effects * Activin Receptors, Type II / genetics * Activin Receptors, Type II / metabolism* ... Activin Receptors, Type I * Activin Receptors, Type II * activin receptor type II-A ...
Activin_recp; Activin types I and II receptor domain. pfam07714. Location:115 → 398. Pkinase_Tyr; Protein tyrosine kinase. ... activin receptor type-1C. Names. ACTR-IC. ALK-7. activin A receptor, type IC. activin receptor type IC. activin receptor-like ... ACVR1C activin A receptor type 1C [Homo sapiens] ACVR1C activin A receptor type 1C [Homo sapiens]. Gene ID:130399 ... Activin_recp; Activin types I and II receptor domain. pfam07714. Location:195 → 478. Pkinase_Tyr; Protein tyrosine kinase. ...
... and activin-receptor inhibitors the next upcoming drug class, highly effective treatments for obesity are in sight. ... Bimagrumab. This drug is a monoclonal antibody activin receptor inhibitor that binds to activin type II receptors. In a phase 2 ... 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 ...
Type II Activin Receptor (ActRII/ACVR2) phosphorylates Type I Activin Receptor (ActRIB/ACVR1B) in response to NODAL Stable ... Type II Activin Receptor (ActRII/ACVR2) phosphorylates Type I Activin Receptor (ActRIB/ACVR1B) in response to NODAL (Homo ... As inferred from the response of the activin receptor to activin, the type II component of the NODAL receptor phosphorylates ... ACVR2A,B (ActRIIA,B) phosphorylates ACVR1B (ActRIB, ALK4) in response to Activin (Homo sapiens) ...
Human ACVR2A(Activin A Receptor Type II A) ELISA Kit To Order : [email protected]. Human Activin A Receptor Type II A (ACVR2A) ... Description: A sandwich ELISA kit for detection of Activin A Receptor Type II A from Human in samples from blood, serum, plasma ... Human ACVR2A(Activin A Receptor Type II A) ELISA Kit. ... Activin A Receptor Type II A (ACVR2A) Antibody. 20-abx241944 ... Description: Recombinant Bovine Activin A Receptor Type II A expressed in: E.coli ...
The BMPR2 gene provides instructions for making a protein called bone morphogenetic protein receptor type 2. Learn about this ... type II activin receptor-like kinase. Additional Information & Resources. Tests Listed in the Genetic Testing Registry. *Tests ... Bone morphogenetic protein receptor type 2 spans the cell membrane, so that one end of the protein is on the outer surface of ... The BMPR2 gene provides instructions for making a protein called bone morphogenetic protein receptor type 2. The BMPR2 gene ...
A comparative analysis of single-cell RNA sequencing data collected from three HUCMSCs and two human umbilical vein endothelial ... activin A receptor-like type 1, ACVRL1; and endoglin, ENG) and their ligands play a critical role in the etiology of PAH1,7,8,9 ... Two types of scRNA-seq analysis were performed. (1) The HUCMSCs that generated the CM used for treating the reported case ( ... Transforming growth factor beta (TGFβ) receptor superfamily members (bone morphogenetic protein receptor 2, BMPR2; ...
Endoglin gene mutations lead to the clinical subtype of HHT-1, and mutations in the activin A receptor type II-like 1 gene ( ... Mutations in the activin receptor-like kinase 1 gene in hereditary haemorrhagic telangiectasia type 2. Nat Genet. 1996 Jun. 13( ... All types of chronic liver disease may give rise to this syndrome. Approximately 80% of affected patients have signs and ... Approximately 80% of pulmonary arteriovenous malformations are of the simple type; [9] most of the associated aneurysms are ...
... suppression of prostate cancer invasion is regulated by activin and bone morphogenetic protein type II receptors. PLoS ONE 8, ... Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor. J. Biol. Chem. 276, ... SAAM II: Simulation, Analysis, and Modeling Software for tracer and pharmacokinetic studies. Metab. Clin. Exp. 47, 484-492 ( ... The N = 17 kinases that gave significant findings (Students t-test ,0.05) in the same direction in each of two separate ...
There are two predominant types of HHT caused by mutations in endoglin (ENG) and ACVRL1/activin receptor-like kinase 1 (ALK1) ... activin receptor-like kinase 1. FKBP12. FK binding protein 12. Id1. inhibitor differentiation 1. PAI-1. plasminogen activator ... Immunosuppressor FK506 Increases Endoglin and Activin Receptor-Like Kinase 1 Expression and Modulates Transforming Growth ... Immunosuppressor FK506 Increases Endoglin and Activin Receptor-Like Kinase 1 Expression and Modulates Transforming Growth ...
Effect of Activin A receptor type II-like kinase 5 (ALK5) inhibitor A83-01 on intracellular CLDN3 localization. hBEpC epithelia ... Two receptor subunits are known, receptor type I and type II subunits. TGF-β1 binding to either subunit initiates their ... assembly into a heteromeric protein complex that consists of two type I and two type II subunits. Within this complex, type II ... TGF-β1-induced redistribution of claudin 3 from tight junctions into cell nuclei is prevented by activin A receptor type II- ...
Receptors for Activin, Dpp, Screw and Gbb *baboon - an activin type I receptor *punt - Type II TGF beta receptor functioning in ... occurs through a hetero-tetrameric receptor complex comprising of two distinct type one BMP receptors and two type II receptors ... BMP and activin pathways *saxophone - type I receptor for Gbb *thick veins - type I receptor of Dpp *wishful thinking - type II ... type I), put (type II), and the co-Smad medea (med). Analyzing the expression of the Dpp receptor Tkv and the activation ...
The Bone Morphogenetic Protein Receptor (BMPR) family is a group of transmembrane proteins that play crucial roles in cell ... while type II receptors comprise BMPR2 and ActRII (Activin receptor type II) subtypes. Such receptors exhibit unique ligand- ... The BMPR family includes both type I and type II receptors.. Type I receptors consist of BMPR1B (ALK6) and BMPR1A (also called ... The Bone Morphogenetic Protein Receptor (BMPR) family includes transmembrane receptors that play vital roles in tissue ...
Activin proteins have a wide range of biological activities, including mesoderm induction, neural cell differentiation, bone ... Two New FBS Publications to Share. *Fresh Antibodies for Fall Research. *New Research Using Our Human Brain Astrocytes ... Corticotropin Releasing Hormone Receptor 1. P41006. 100 ug Blocking Peptide. Delta Opioid Receptor 3-17. P10100. 100 ug ... Neurotensin Receptor 1 (NTS1). P14020. 100 ug Blocking Peptide. Nicotinic acetylcholine receptor alpha7. P41009. 100 ug ...
type: go. obsolete: False. Description: Combining with activin, one of two gonadal glycoproteins related to transforming growth ... activin-activated receptor activity. id: GO:0017002. name: activin-activated receptor activity. namespace: molecular_function. ... activin receptor activity, type I. GO:0016362. activin receptor activity, type II. ...
Four children with pulmonary AVMs carried an endoglin gene mutation (HHT type 1), and 1 carried an activin receptor-like kinase ... Two were referred because of skin telangiectases and 2, because of multiple episodes of epistaxis. Screening results revealed a ... HHT type 2). The 2 children with spinal AVMs belong to the same HHT type 2 family. No mutation was found in 1 child with ...
... activin A receptor, type I (ACVR1)/activin receptor-like kinase-2 (ALK2), Janus kinase (JAK) 1, and JAK2. This activity may ... 2] Chifotides, H.T., Bose, P. & Verstovsek, S. Momelotinib: an emerging treatment for myelofibrosis patients with anemia. J ... 2] Patients treated with the most commonly used JAK inhibitor will often require transfusions, and more than 30% will ...
keywords = "physiology: Activin Receptors, Type II, Cell Line, Cells, Cultured, Comparative Study, Endothelial Cells, cytology ... In endothelial cells TGF-beta utilizes a second type I receptor, ALK1, activating the Smad1/Smad5 pathway. Consequently, a ... In endothelial cells TGF-beta utilizes a second type I receptor, ALK1, activating the Smad1/Smad5 pathway. Consequently, a ... In endothelial cells TGF-beta utilizes a second type I receptor, ALK1, activating the Smad1/Smad5 pathway. Consequently, a ...
DMH-1 is a selective inhibitor of bone morphogenic protein (BMP) type-I receptor activin receptor-like kinase 2 (ALK2) receptor ... Receptor Serine/Threonine Kinases (RSTKs) / BMP and Other Activin Receptors / BMP and Other Activin Receptor Inhibitors / DMH-1 ... Keywords: DMH-1, DMH-1 supplier, selective, activin, receptors, alk2, acvr1, bmp, type, I, bone, morphogenic, morphogenetic, ... Mohedas et al (2013) Development of an ALK2-biased BMP type I receptor kinase inhibitor. ACS Chem.Biol. 8 1291 PMID: 23547776 ...
Atr-II, Atr: Activin-A-receptor-88CD, dorsal holes C, pun, TGF-beta-type-receptor-like, activin receptor, activin receptor type ... Tgf-r: TGF-beta-type-receptor-like, Activin-A-receptor-88CD, dlhC: dorsal holes C, Act-r, TGF-B, SFO046, ... II, Atr88CD, l(3)10460, Punt, TGF-beta, put, CG7904, STK-C, Tgf-r: TGF-beta-type-receptor-li, AtrII, l(3)j5A5, punt. ... TAAD2, TGFbR2, HNPCC6, MFS2, TbetaR-II, TGFBR2, TGFR-2, TGFbeta-RII, TbetaRII, RIIC, AAT3, TGF_beta_RII, FAA3. ...
A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva. Nat ... was identified as a recurrent missense mutation in the GS activation domain of activin receptor Ia/activinlike kinase 2 (ACVR1/ ... type I receptor, in all individuals with classic fibrodysplasia ossificans progressiva. [4, 5] Recently, additional mutations ... type I receptor ACVR1. Hum Mutat. 2009 Mar. 30(3):379-90. [QxMD MEDLINE Link]. ...
... activin receptor type-2B; TG, triglyceride; RBC, red blood cell; Hgb, hemoglobin; S6K1, ribosomal protein S6 kinase beta-1; ... The ACSM National Conference included a symposium and roundtable meeting on AAS in sports-two polarized groups evolved: those ... Specificity of ligand-dependent androgen receptor stabilization: receptor domain interactions influence ligand dissociation and ... well-being type (interested in looking and feeling good with low risk-taking); and 4) YOLO "You Only Live Once" type (is ...
Receptor Type 1 Activin Receptor Type I ACTR-I Serine Threonine-protein Kinase Receptor R1 SKR1 Activin Receptor-like Kinase 2 ... Activin Receptor 1, Activin Receptor I, ACTR-I, Serine/Threonine-protein Kinase Receptor R1, SKR1, Activin Receptor-like Kinase ... TGF-B Superfamily Receptor I, TSR-I, ACVRLK2) ... ALK-2 TGF-B Superfamily Receptor Type I TSR-I ACVRLK2 Antibody ... TGF-B superfamily receptor type I; activin A receptor, type II-like kinase 2; serine/threonine-protein kinase receptor R1; ...
In addition to BMPR2, mutations in activin A receptor type II-like 1 (ACVRL1) [51], endoglin (ENG) [52], SMAD family member 9 ( ... a high degree of heterogeneity is often observed in the amount and type of instability within and between cancer types. However ... The two tumour-suppressor genes, ataxia-telangiectasia mutated (ATM) and p53, play a crucial role in responses to damaged DNA. ... NR4A nuclear receptors in atherosclerosis and vein-graft disease. Trends Cardiovasc Med 2007; 17: 105-111. ...
activin receptor type II-B 70% * Skeletal Muscle 63% * Myostatin 56% 7 Scopus citations ... Engaging students with team-based learning in courses taught at two campuses synchronously: Two case studies in health sciences ... Genetic regulation of rejection and survival following human lung transplantation by the innate immune receptor CD14. Palmer, S ... Ex ante economic evaluation of genetic testing for the ARG389 beta1-adrenergic receptor polymorphism to support bucindolol ...
CRYSTAL STRUCTURE OF THE ACTIVIN RECEPTOR TYPE-2A LIGAND BINDING DOMAIN IN COMPLEX WITH BIMAGRUMAB FV - 5NH3 , canSARS ... CRYSTAL STRUCTURE OF THE ACTIVIN RECEPTOR TYPE-2A LIGAND BINDING DOMAIN IN COMPLEX WITH BIMAGRUMAB FV ... CRYSTAL STRUCTURE OF THE ACTIVIN RECEPTOR TYPE-2A LIGAND BINDING DOMAIN IN COMPLEX WITH BIMAGRUMAB FV ...
The experimental data is in the form of mass spectrometry, yeast two-hybrid, protein structure prediction, light microscopy and ... activin. *transforming growth factor beta. *TGF-beta receptor binding. *transforming growth factor beta ligand binding to type ... Interacting selectively and non-covalently with the transforming growth factor beta receptor.. ...
  • Activin receptor-like kinase 7 silencing alleviates cardiomyocyte apoptosis, cardiac fibrosis, and dysfunction in diabetic rats. (nih.gov)
  • There are two predominant types of HHT caused by mutations in endoglin ( ENG ) and ACVRL1 / activin receptor-like kinase 1 ( ALK1 ) genes, named HHT1 and HHT2, respectively. (aspetjournals.org)
  • TGF-β1 acts predominantly through phosphorylation of the C-terminal MH2 domains of SMAD2 and SMAD3 via activin receptor-like kinase 5 (ALK5), of which activity is located at the C-terminal part of TGFBR1. (springer.com)
  • Dorsoventral (DV) patterning of the Drosophila embryo is initiated by a broad Dorsal (Dl) nuclear gradient, which is regulated by a conserved signaling pathway that includes the Toll receptor and Pelle kinase. (sdbonline.org)
  • Four children with pulmonary AVMs carried an endoglin gene mutation (HHT type 1), and 1 carried an activin receptor-like kinase 1 gene mutation (HHT type 2). (nih.gov)
  • Momelotinib has a differentiated mode of action with inhibitory ability along three key signalling pathways: activin A receptor, type I (ACVR1)/activin receptor-like kinase-2 (ALK2), Janus kinase (JAK) 1, and JAK2. (gsk.com)
  • DMH-1 is a selective inhibitor of bone morphogenic protein (BMP) type-I receptor activin receptor-like kinase 2 (ALK2) receptor (IC 50 = 108 nM or 12.6 nM in in vitro kinase assays). (tocris.com)
  • The genetic cause of fibrodysplasia ossificans progressiva was identified as a recurrent missense mutation in the GS activation domain of activin receptor Ia/activinlike kinase 2 ( ACVR1/ALK2 ), a bone morphogenetic protein (BMP) type I receptor, in all individuals with classic fibrodysplasia ossificans progressiva. (medscape.com)
  • Myostatin binding to type IIB activin receptor (ActRIIB) on muscle surface induces the recruitment and activation of activin receptor-like kinase 5 (ALK5), and eventually leads to forkhead box O3 (FoxO3a)-dependent transcription to promote muscle protein breakdown via the ubiquitin-proteasome system ( 23 ). (spandidos-publications.com)
  • Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. (tgf-a.com)
  • Within the last several years, many therapeutic strategies have already been created to inhibit TGF-receptor kinase inhibitors, buy BV-6 TGF-neutralizing antibodies, soluble receptor decoys (Fc fusions) and TGF-antisense oligonucleotides [12]. (molecularcircuit.com)
  • Expression cloning of an activin receptor, a predicted transmembrane serine kinase. (chemeurope.com)
  • 1993). "Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors. (chemeurope.com)
  • 1996). "Identification of type I and type II serine/threonine kinase receptors for growth/differentiation factor-5. (chemeurope.com)
  • ATL significantly reduced the expression of COX-2 by inhibiting the kinase activity of IKKβ by targeting the ATP-binding site and then attenuating the binding of NF-κB to the COX-2 promoter region. (biomedcentral.com)
  • ATL exerts its anti-tumor effects in human GBM cells at least in part via NF-κB/COX-2-mediated signaling cascades by inhibiting IKKβ kinase activity. (biomedcentral.com)
  • Momelotinib (OJJAARA) is an oral Janus kinase 1 and 2 (JAK1/JAK2) and activin A receptor, type I (ACVR1) inhibitor that ha. (cn1699.cn)
  • Active TGFβ induces the heteromeric complex formation of two single transmembrane serine/threonine kinase family receptors, i.e. (encyclopedia.pub)
  • 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)
  • 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)
  • Complemented ACVR2 protein complexed with ACVR1 with activin treatment, generating nuclear phosphoSMAD2 and activin-specific gene transcription. (nih.gov)
  • 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)
  • In human beings, three isoforms of TGF-have been explained, TGF-ligands is definitely transduced through cell surface area recaptor complexes of two unique types of transmembrane serine-threonine kinases, the sort I and type II receptors. (molecularcircuit.com)
  • Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. (chemeurope.com)
  • These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. (chemeurope.com)
  • 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)
  • Seven type I receptors (Activin-recaptor like kinases, ALKs, 1C7) and five type II receptors are known in vertebrates. (molecularcircuit.com)
  • Type II receptors are considered to be constitutively active kinases. (chemeurope.com)
  • Activins signal through heterodimeric receptor complexes composed of type I (Activin RIA or RIB) and type II (Activin RIIA or RIIB) transmembrane Ser/Thr kinases. (bio-techne.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)
  • In a lab, it has been shown that truncated mutations in the ACVR2 gene causes a significant reduction in activin mediated cell signaling. (wikipedia.org)
  • ACVR2 transmits the growth effects of activin via phosphorylation of SMAD proteins to affect gene transcription. (nih.gov)
  • The BMPR2 gene provides instructions for making a protein called bone morphogenetic protein receptor type 2. (medlineplus.gov)
  • Recently, researchers have found that this gene family plays a broader role in regulating the growth and differentiation of numerous types of cells. (medlineplus.gov)
  • The type I target gene folded gastrulation is activated only in response to peak levels of the Dl gradient, so that expression is restricted to a subdomain of the presumptive mesoderm. (sdbonline.org)
  • The type II target gene snail contains a series of low-affinity Dl-binding sites, as well as binding sites for the bHLH activator, Twist. (sdbonline.org)
  • The type IV target gene rhomboid is expressed in lateral stripes that encompass the ventral half of the presumptive neuroectoderm. (sdbonline.org)
  • ALK1 signalling analysis identifies angiogenesis related genes and reveals disparity between TGF-beta and constitutively active receptor induced gene expression. (manchester.ac.uk)
  • Analysing ALK1 regulated gene expression after 4 hours revealed 13 genes to be up- and 2 to be down-regulated. (manchester.ac.uk)
  • Evaluation of ALK1 regulated gene expression in different human endothelial cell types was not in complete agreement. (manchester.ac.uk)
  • Dive into the research topics of 'ALK1 signalling analysis identifies angiogenesis related genes and reveals disparity between TGF-beta and constitutively active receptor induced gene expression. (manchester.ac.uk)
  • Variations in this gene are a cause of susceptibility to colorectal cancer type 3 (CRCS3). (cancerindex.org)
  • While Smad1/5/8 are phosphorylated by ALK1/2/3/6 upon BMP or GDF activation, Smad2/3 are phosphorylated by ALK4/5/7 pursuing TGF-binds TGF-receptor type II (Ttarget gene promoters, the Smad complicated associates with additional transcription elements [22,23]. (molecularcircuit.com)
  • Activin A receptor, type IIA , also known as ACVR2A , is a human gene. (chemeurope.com)
  • This gene encodes activin A type II receptor. (chemeurope.com)
  • a b Entrez Gene: ACVR2A activin A receptor, type IIA. (chemeurope.com)
  • 1994). "Expression of the type II activin receptor gene in the human placenta. (chemeurope.com)
  • The thorough expression of every Inhibitors,Modulators,Libraries up regulated gene in pediatric AML was presented in Figure two along with the expression of down regulated genes was presented in Figure three. (microrna21.com)
  • BMPR family of proteins is a valuable tool for studying ligand-receptor interactions, downstream signaling events, and determining therapeutic targets. (news-medical.net)
  • Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. (neuromics.com)
  • Activins and Inhibins are TGF‑ beta superfamily proteins that regulate a wide range of processes including mesoderm induction, reproductive system development and function, liver growth and regeneration, wound healing, and inflammation. (bio-techne.com)
  • There are two activin type two receptors: ACVR2A and ACVR2B. (wikipedia.org)
  • Signals through activin receptors type-2, ACVR2A and ACVR2B, and activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3. (cusabio.com)
  • Type I receptors consist of BMPR1B (ALK6) and BMPR1A (also called ALK3), while type II receptors comprise BMPR2 and ActRII (Activin receptor type II) subtypes. (news-medical.net)
  • analyzed the impact of RN1 (a natural product extracted from Panax notoginseng ) on bone morphogenetic protein receptors (BMPR1A and BMPR2). (news-medical.net)
  • Mutations in bone morphogenetic protein receptor 2 ( BMPR2 ) are the cause of most heritable cases but the vast majority of other cases are genetically undefined. (biomedcentral.com)
  • For example, bone morphogenetic protein receptor type 2 ( BMPR2 ) mutations are observed in 60-80% of familial (FPAH) cases, but data from population registries indicate that penetrance of the disease phenotype ranges from 14 to 42% [ 6 ]. (biomedcentral.com)
  • We demonstrate that TGF-β1 activates TGF-β1 receptors TGFBR1 and TGFBR2 resulting in ALK5-mediated phosphorylation of SMAD2. (springer.com)
  • TGF-beta signalling is mediated by the TbetaRII/ALK5 receptor complex activating the Smad2/Smad3 pathway. (manchester.ac.uk)
  • DMH-1 exhibits 6- and 19-fold selectivity for ALK-2 over ALK-1 and ALK-3, respectively, and no significant inhibition of AMPK, ALK5, KDR (VEGFR-2) or PDGFR β receptors. (tocris.com)
  • The type I receptor recruits a receptor regulated SMAD (R-SMAD) which it phosphorylates. (wikipedia.org)
  • ACVR2-complemented MSI-H colon cancers restore activin-SMAD signaling, decrease growth, and slow their cell cycle following ligand stimulation but show increased cellular migration. (nih.gov)
  • Upon ligand binding, type I receptors phosphorylate cytoplasmic SMAD transcription factors, which then translocate to the nucleus and interact directly with DNA or in complex with other transcription factors (Bondestam et al. (nih.gov)
  • Thus, activated, type I subunits recruit and phosphorylate receptor SMADs (R-smad), which are the first intracellular mediators of TGF-β signalling. (springer.com)
  • The ligand binds a sort II receptor, which phosphorylates somebody type I receptor, which propagates the sign in the cell via phosphorylation of downstream Smad-dependent and -self-employed procedures [20]. (molecularcircuit.com)
  • Morphogen receptor genes and metamorphogenes: skeleton keys to metamorphosis. (medscape.com)
  • The new genes were identified based solely on rare deleterious missense variants, a variant type that could not be adequately assessed in either cohort alone. (biomedcentral.com)
  • Rare variant analysis of a large international consortium identified two new candidate genes- FBLN2 and PDGFD . (biomedcentral.com)
  • Lately research connected to mechanisms of leukemia cell resistance to Fas FasL mediated apoptosis selleck chemical such as Fas and FasL mutation and expression abnormality, Fas signaling transduction pathway abnormality, and regulatory have an impact on of apoptotic regulatory genes on Fas FasL process, as well as tactics replying to antiapoptosis of leukemia cells including NF kappa B, XIAP, membrane receptor CD28 and matrix metalloproteinase 7 obtained some pro gresses. (microrna21.com)
  • ACVR2 receptors are present in the testis during testicular development. (wikipedia.org)
  • hMLH1 and ACVR2 mutant HCT116 cells were previously stably transferred with chromosome 2 (HCT116+chr2), restoring a single regulated copy of wild-type ACVR2 but not hMLH1. (nih.gov)
  • HCT116+chr2 cells and HEC59+chr2 cells, but not ACVR2-mutant HCT116 or HEC59 cells, acquired wild-type ACVR2 as well as expression of ACVR2 wild-type messenger RNA. (nih.gov)
  • ACVR2-restored cells showed decreased growth and reduced S phase but increased cellular migration following activin treatment. (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. (medlineplus.gov)
  • 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. (medlineplus.gov)
  • The physiology and pathophysiology of inhibin, activin and follistatin in female reproduction. (chemeurope.com)
  • Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism. (chemeurope.com)
  • Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. (tgf-a.com)
  • The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. (tgf-a.com)
  • Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. (chemeurope.com)
  • The activin type 2 receptors belong to a larger TGF-beta receptor family and modulate signals for transforming growth factor beta ligands. (wikipedia.org)
  • Despite the large amount of processes that these ligands regulate, they all operate through essentially the same pathway: A ligand binds to a type 2 receptor, which recruits and trans-phosphorylates a type I receptor. (wikipedia.org)
  • Several ligands that signal through the activin type 2 receptors regulate muscle growth. (wikipedia.org)
  • Such receptors exhibit unique ligand-binding specificities and mediate distinct signaling cascades, even though they could cross-interact with other TGF-β family ligands. (news-medical.net)
  • and type II receptors are required for binding ligands and for expression of type I receptors. (chemeurope.com)
  • In endothelial cells TGF-beta utilizes a second type I receptor, ALK1, activating the Smad1/Smad5 pathway. (manchester.ac.uk)
  • In addition, the results suggest endothelial cell type specific ALK1 and TGF-beta signalling. (manchester.ac.uk)
  • TGF-superfamily also contains other elements involved in bone tissue Rabbit Polyclonal to EFNA3 homeostasis including: activins, inhibins, and bone tissue morphogeneticproteins (BMPs). (molecularcircuit.com)
  • Activins are disulfide‑linked homodimers or heterodimers of beta subunits, while Inhibins contain the alpha subunit and beta A or beta B . Human beta C consists of an 18 aa signal sequence, a 218 aa propeptide, and a 116 aa mature segment (4). (bio-techne.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Activin A Receptor Type II A (ACVR2A) in tissue homogenates, cell lysates and other biological fluids. (lotuskringpoeldijk.nl)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Activin A Receptor Type II A (ACVR2A) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (lotuskringpoeldijk.nl)
  • This is a highly specific antibody against TGF beta Receptor I. (tgf-a.com)
  • Activin is growth suppressive and enhances migration similar to transforming growth factor beta in colon cancer, indicating that abrogation of the effects of activin contribute to the pathogenesis of MSI-H colon cancers. (nih.gov)
  • 1996). "Inhibitory effects of activin on the growth and morpholgenesis of primary and transformed mammary epithelial cells. (chemeurope.com)
  • As inferred from the response of the activin receptor to activin, the type II component of the NODAL receptor phosphorylates the type I component in response to NODAL binding. (reactome.org)
  • We believe that decisive treatment benefit can only be achieved by targeting distinct cell types and pathways that collectively sustain tumor growth. (lu.se)
  • Smads 1, buy BV-6 2, 3, 5 and 8 will be the receptor-associated Smads or R-Smads. (molecularcircuit.com)
  • 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. (medlineplus.gov)
  • Upon binding, this complex translocates to the cytoplasm, where it interacts with TGF-beta receptor type-1 (TGFBR1), leading to the degradation of both the encoded protein and TGFBR1. (cancerindex.org)
  • The aim of this study was to determine the effect of eight weeks of high-intensity interval training on activin receptor type II in heart and plasma levels of myostatin in male rats.Methods: After the familiarization period, twenty male rats with the limitation of three months of age were randomly divided to control (n = 10) and high-intensity interval training (n=10) groups. (ac.ir)
  • Activin receptor type II in the myocardial left ventricle was measured using immunohistochemistry method, and myostatin was measured by the enzyme-linked immunosorbent assay (ELISA) method. (ac.ir)
  • 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)
  • In addition, COX-2 is a target of non-steroidal anti-inflammatory drugs (NSAIDs), and its selective inhibitors could effectively prevent inflammation, proliferation and angiogenesis and induce apoptosis in human cancer cells. (biomedcentral.com)
  • Combining with activin, one of two gonadal glycoproteins related to transforming growth factor beta, to initiate a change in cell activity. (systemsbiology.net)
  • Interacting selectively and non-covalently with the transforming growth factor beta receptor. (yeastrc.org)
  • Transforming growth factor-beta (TGFβ) was discovered more than thirty years ago as a secreted polypeptide from sarcoma virus-infected cells that promoted the soft agar independent growth of normal rat kidney (NRK) cells [ 1 ] [ 2 ] . (encyclopedia.pub)
  • 1996). "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors. (chemeurope.com)
  • The receptors are ligand binding factors of type 1, 2 or 3 and protein-molecules that receive chemical-signals from outside a cell. (tgf-a.com)
  • When such chemical-signals couple or bind to a receptor, they cause some form of cellular/tissue-response, e.g. a change in the electrical-activity of a cell. (tgf-a.com)
  • In this sense, am olfactory receptor is a protein-molecule that recognizes and responds to endogenous-chemical signals, chemokinesor cytokines e.g. an acetylcholine-receptor recognizes and responds to its endogenous-ligand, acetylcholine. (tgf-a.com)
  • Decreased expression of activin A receptor 1C may result in Ca(2+) -induced aberrant skin hypersensitivity. (nih.gov)
  • The expression of beta C is restricted compared to the widespread distribution of beta A and beta B . Activin C is expressed as an approximately 20 kDa dimer predominantly by hepatocytes but also by multiple cell types in the male and female reproductive tracts, posterior pituitary and adrenal glands, and nociceptive afferent dorsal root ganglia neurons (5‑7). (bio-techne.com)
  • [1] , [2] Patients treated with the most commonly used JAK inhibitor will often require transfusions, and more than 30% will discontinue treatment due to anaemia. (gsk.com)
  • Motixafortide (APHEXDATM) is a selective C-X-C motif chemokine receptor 4 (CXCR4) inhibitor being developed by BioLineRx u. (cn1699.cn)
  • Determination of type I receptor specificity by the type II receptors for TGF-beta or activin. (sinica.edu.tw)
  • The fucose-binding lectin, LecB, displays a unique carbohydrate-binding site that incorporates two closely located calcium ions bridging between the ligand and protein, providing specificity and unusually high affinity. (bvsalud.org)
  • Here we comprehensively analyzed the antiviral activity of all IFNα subtypes against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) to identify the underlying immune signatures and explore their therapeutic potential. (bvsalud.org)
  • Prophylaxis of primary human airway epithelial cells (hAEC) with different IFNα subtypes during SARS-CoV-2 infection uncovered distinct functional classes with high, intermediate, and low antiviral IFNs. (bvsalud.org)
  • 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)
  • The localization of nuclear factor kappa B (NF-κB) p50/p65 and its binding to the cyclooxygenase 2 (COX-2) promoter were determined using confocal immunofluorescence, a streptavidin-agarose pulldown assay and a chromatin immunoprecipitation (ChIP) assay. (biomedcentral.com)
  • J Bone Joint Surg Am . 1993 Feb. 75(2):215-9. (medscape.com)
  • Activins are also involved in growth and differentiation of several tissues from different species. (neuromics.com)
  • What are the consequences of expressing a constitutively activated form of the Toll receptor, Toll(10b), in anterior regions of the early embryo? (sdbonline.org)
  • Within this complex, type II subunits phosphorylate type I subunits at their N-terminal domain. (springer.com)
  • Cloning of the human activin receptor cDNA reveals high evolutionary conservation. (chemeurope.com)
  • 2. Find values for the kinetic parameters from experimental b pathway have been detected in several human diseases, estimates or by fitting the model to experimental kinetic most notably in many forms of cancer, and in fibrotic diseases data. (lu.se)
  • Step 2 often presents the main limitation for a pathway or a simple ON/OFF language as means to draw conclusions modeling approach. (lu.se)
  • Description: A sandwich ELISA kit for detection of Activin A Receptor Type II A from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (lotuskringpoeldijk.nl)
  • میوستاتین به روش Enzyme-linked immunosorbent assay (ELISA) و گیرنده‌ی کینازی نوع II بطن چپ قلب به روش Immunohistochemistry (IHC) اندازه‌گیری شد. (ac.ir)
  • ACVR1C is a type I receptor for the TGFB (see MIM 190180) family of signaling molecules. (nih.gov)
  • DAPK activates MARK1/2 to regulate microtubule assembly, neuronal differentiation, and tau toxicity. (sinica.edu.tw)
  • TβRI acts downstream of TβRII, and is the main component of the receptor complex that triggers various downstream signaling activities [ 17 ] . (encyclopedia.pub)
  • Results We identified a homozygous 2 bp deletion in MMP21, encoding matrix metalloproteinase-21, as the sole coding mutation that segregated with the phenotype. (bmj.com)
  • A comparative analysis of single-cell RNA sequencing data collected from three HUCMSCs and two human umbilical vein endothelial cell (HUVEC) controls identified eight common cell clusters, all of which indicated regenerative potential specific for HUCMSCs. (nature.com)