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.
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
A broadly distributed protein that binds directly to ACTIVINS. It functions as an activin antagonist, inhibits FOLLICLE STIMULATING HORMONE secretion, regulates CELL DIFFERENTIATION, and plays an important role in embryogenesis. Follistatin is a single glycosylated polypeptide chain of approximately 37-kDa and is not a member of the inhibin family (INHIBINS). Follistatin also binds and neutralizes many members of the TRANSFORMING GROWTH FACTOR BETA family.
Receptors 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.
They are glycopeptides and subunits in INHIBINS and ACTIVINS. Inhibins and activins belong to the transforming growth factor beta superfamily.
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.
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).
The inner zone of the adrenal cortex. This zone produces the enzymes that convert PREGNENOLONE, a 21-carbon steroid, to 19-carbon steroids (DEHYDROEPIANDROSTERONE; and ANDROSTENEDIONE) via 17-ALPHA-HYDROXYPREGNENOLONE.
The beta subunit of follicle stimulating hormone. It is a 15-kDa glycopolypeptide. Full biological activity of FSH requires the non-covalently bound heterodimers of an alpha and a beta subunit. Mutation of the FSHB gene causes delayed puberty, or infertility.
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.
Anterior pituitary cells that can produce both FOLLICLE STIMULATING HORMONE and LUTEINIZING HORMONE.
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 receptor-regulated smad protein that undergoes PHOSPHORYLATION by ACTIVIN RECEPTORS, TYPE I. It regulates TRANSFORMING GROWTH FACTOR BETA and ACTIVIN signaling.
A factor synthesized in a wide variety of tissues. It acts synergistically with TGF-alpha in inducing phenotypic transformation and can also act as a negative autocrine growth factor. TGF-beta has a potential role in embryonal development, cellular differentiation, hormone secretion, and immune function. TGF-beta is found mostly as homodimer forms of separate gene products TGF-beta1, TGF-beta2 or TGF-beta3. Heterodimers composed of TGF-beta1 and 2 (TGF-beta1.2) or of TGF-beta2 and 3 (TGF-beta2.3) have been isolated. The TGF-beta proteins are synthesized as precursor proteins.
Bone-growth regulatory factors that are members of the transforming growth factor-beta superfamily of proteins. They are synthesized as large precursor molecules which are cleaved by proteolytic enzymes. The active form can consist of a dimer of two identical proteins or a heterodimer of two related bone morphogenetic proteins.
A pair of highly specialized muscular canals extending from the UTERUS to its corresponding OVARY. They provide the means for OVUM collection, and the site for the final maturation of gametes and FERTILIZATION. The fallopian tube consists of an interstitium, an isthmus, an ampulla, an infundibulum, and fimbriae. Its wall consists of three histologic layers: serous, muscular, and an internal mucosal layer lined with both ciliated and secretory cells.
A major gonadotropin secreted by the adenohypophysis (PITUITARY GLAND, ANTERIOR). Follicle-stimulating hormone stimulates GAMETOGENESIS and the supporting cells such as the ovarian GRANULOSA CELLS, the testicular SERTOLI CELLS, and LEYDIG CELLS. FSH consists of two noncovalently linked subunits, alpha and beta. Within a species, the alpha subunit is common in the three pituitary glycoprotein hormones (TSH, LH, and FSH), but the beta subunit is unique and confers its biological specificity.
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.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
Signal molecules that are involved in the control of cell growth and differentiation.
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.
The reproductive organ (GONADS) in female animals. In vertebrates, the ovary contains two functional parts: the OVARIAN FOLLICLE for the production of female germ cells (OOGENESIS); and the endocrine cells (GRANULOSA CELLS; THECA CELLS; and LUTEAL CELLS) for the production of ESTROGENS and PROGESTERONE.
The middle germ layer of an embryo derived from three paired mesenchymal aggregates along the neural tube.
The male gonad containing two functional parts: the SEMINIFEROUS TUBULES for the production and transport of male germ cells (SPERMATOGENESIS) and the interstitial compartment containing LEYDIG CELLS that produce ANDROGENS.
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.
A gland in males that surrounds the neck of the URINARY BLADDER and the URETHRA. It secretes a substance that liquefies coagulated semen. It is situated in the pelvic cavity behind the lower part of the PUBIC SYMPHYSIS, above the deep layer of the triangular ligament, and rests upon the RECTUM.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

The homeobox gene Pitx2: mediator of asymmetric left-right signaling in vertebrate heart and gut looping. (1/1189)

Left-right asymmetry in vertebrates is controlled by activities emanating from the left lateral plate. How these signals get transmitted to the forming organs is not known. A candidate mediator in mouse, frog and zebrafish embryos is the homeobox gene Pitx2. It is asymmetrically expressed in the left lateral plate mesoderm, tubular heart and early gut tube. Localized Pitx2 expression continues when these organs undergo asymmetric looping morphogenesis. Ectopic expression of Xnr1 in the right lateral plate induces Pitx2 transcription in Xenopus. Misexpression of Pitx2 affects situs and morphology of organs. These experiments suggest a role for Pitx2 in promoting looping of the linear heart and gut.  (+info)

Identification of a nuclear localization signal in activin/inhibin betaA subunit; intranuclear betaA in rat spermatogenic cells. (2/1189)

Activin is a dimeric glycoprotein hormone that was initially characterized by its ability to stimulate pituitary FSH secretion and was subsequently recognized as a growth factor with diverse biological functions in a large variety of tissues. In the testis, activin has been implicated in the auto/paracrine regulation of spermatogenesis through its cognate cell membrane receptors on Sertoli and germ cells. In this study we provide evidence for intranuclear activin/inhibin betaA subunit and show its distribution in the rat seminiferous epithelium. We have shown by transient expression in HeLa cells of beta-galactosidase fusion proteins that the betaA subunit precursor contains a functional nuclear localization signal within the lysine-rich sequence corresponding to amino acids 231-244. In all stages of the rat seminiferous epithelial cycle, an intense immunohistochemical staining of nuclear betaA was demonstrated in intermediate or type B spermatogonia or primary spermatocytes in their initial stages of the first meiotic prophase, as well as in pachytene spermatocytes and elongating spermatids primarily in stages IX-XII. In some pachytene spermatocytes, the pattern of betaA immunoreactivity was consistent with the characteristic distribution of pachytene chromosomes. In the nuclei of round spermatids, betaA immunoreactivity was less intense, and in late spermatids it was localized in the residual cytoplasm, suggesting disposal of betaA before spermatozoal maturation. Immunoblot analysis of a protein extract from isolated testicular nuclei revealed a nuclear betaA species with a molecular mass of approximately 24 kDa, which is more than 1.5 times that of the mature activin betaA subunit present in activin dimers. These results suggest that activin/inhibin betaA may elicit its biological functions through two parallel signal transduction pathways, one involving the dimeric molecule and cell surface receptors and the other an alternately processed betaA sequence acting directly within the nucleus. According to our immunohistochemical data, betaA may play a significant role in the regulation of nuclear functions during meiosis and spermiogenesis.  (+info)

Dominant-negative Smad2 mutants inhibit activin/Vg1 signaling and disrupt axis formation in Xenopus. (3/1189)

Smads are central mediators of signal transduction for the TGFbeta superfamily. However, the precise functions of Smad-mediated signaling pathways in early development are unclear. Here we demonstrate a requirement for Smad2 signaling in dorsoanterior axis formation during Xenopus development. Using two point mutations of Smad2 previously identified in colorectal carcinomas, we show that Smad2 ushers Smad4 to the nucleus to form a transcriptional activation complex with the nuclear DNA-binding protein FAST-1 and that the mutant proteins interact normally with FAST-1 but fail to recruit Smad4 into the nucleus. This mechanism of inhibition specifically restricts the dominant-negative activity of these mutants to the activin/Vg1 signaling pathway without inhibiting BMPs. Furthermore, expression of these mutants in Xenopus animal caps inhibits but does not abolish activin and Vg1 induction of mesoderm and in the embryo results in a truncated dorsoanterior axis. These studies define a mechanism through which mutations in Smad2 may block TGFbeta-dependent signaling and suggest a critical role for inductive signaling mediated by the Smad2 pathway in Xenopus organizer function.  (+info)

Activin and TGFbeta limit murine primordial germ cell proliferation. (4/1189)

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

Expression of inhibin/activin subunits and their receptors and binding proteins in human preimplantation embryos. (5/1189)

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

Identification of two amino acids in activin A that are important for biological activity and binding to the activin type II receptors. (6/1189)

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)

Characterization of the Ets-type protein ER81 in Xenopus embryos. (7/1189)

A function for FGF-type peptide growth factors has been implied for early mesodermal patterning events in Xenopus laevis. FGF signalling operates via the MAP kinase cascade that can directly activate the transcription of organizer-expressed genes, such as Xbra and Xegr-1. We have recently provided evidence for a critical role of Ets-type transcription factors in FGF mediated Xegr-1 transcription activation. Here, we report on the identification of the Xenopus Ets-type protein ER81 that is expressed in a pattern overlapping with the ones of Xegr-1 and Xbra during gastrulation. Microinjection in XER81 encoding mRNA into ventral blastomeres of Xenopus embryos results in the induction of ectopic, tail-like protrusions, whereas dorsal overexpression results in disturbed eye development. In the animal cap assay, ectopic expression of XER81 is found to interfere with activin mediated induction of Xegr-1 and gsc, but not with the Xbra response to activin.  (+info)

Establishment of substratum polarity in the blastocoel roof of the Xenopus embryo. (8/1189)

The fibronectin fibril matrix on the blastocoel roof of the Xenopus gastrula contains guidance cues that determine the direction of mesoderm cell migration. The underlying guidance-related polarity of the blastocoel roof is established in the late blastula under the influence of an instructive signal from the vegetal half of the embryo, in particular from the mesoderm. Formation of an oriented substratum depends on functional activin and FGF signaling pathways in the blastocoel roof. Besides being involved in tissue polarization, activin and FGF also affect fibronectin matrix assembly. Activin treatment of the blastocoel roof inhibits fibril formation, whereas FGF modulates the structure of the fibril network. The presence of intact fibronectin fibrils is permissive for directional mesoderm migration on the blastocoel roof extracellular matrix.  (+info)

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.

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.

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.

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.

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.

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, 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.

The zona reticularis is a layer of the adrenal cortex, which is the outer part of the adrenal gland. These glands are located on top of the kidneys and are responsible for producing several important hormones. The adrenal cortex itself has three distinct layers: the zona glomerulosa, the zona fasciculata, and the zona reticularis.

The zona reticularis is the innermost layer of the adrenal cortex. It is responsible for producing and releasing certain steroid hormones, particularly androgens such as dehydroepiandrosterone (DHEA) and its sulfate (DHEAS). These androgens are precursor hormones that can be converted into more potent androgens or estrogens in other parts of the body. The zona reticularis plays a crucial role in sexual development and function, as well as maintaining overall health and well-being.

Disorders related to the zona reticularis may result in abnormal hormone production, leading to conditions such as congenital adrenal hyperplasia, Cushing's syndrome, or Addison's disease. Proper diagnosis and treatment of these disorders typically involve endocrinologists, healthcare professionals specializing in hormonal and metabolic disorders.

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

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

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

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.

Gonadotrophs are a type of hormone-secreting cells located in the anterior pituitary gland, a small endocrine gland at the base of the brain. These cells produce and release two important gonadotropin hormones: follicle-stimulating hormone (FSH) and luteinizing hormone (LH).

Follicle-stimulating hormone (FSH) plays a crucial role in the reproductive system by stimulating the growth and development of ovarian follicles in females and sperm production in males. In females, FSH also promotes the production of estrogen during the menstrual cycle.

Luteinizing hormone (LH) is responsible for triggering ovulation in females, releasing a mature egg from the ovary into the fallopian tube. In addition, LH stimulates the production of progesterone by the remaining cells of the ruptured follicle, which forms the corpus luteum. In males, LH helps regulate testosterone production in the testes.

Gonadotrophs are essential for maintaining reproductive function and hormonal balance in both sexes. Their activity is controlled by the hypothalamus, another part of the brain that releases gonadotropin-releasing hormone (GnRH) to regulate FSH and LH secretion.

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.

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

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

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

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

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

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

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

The Fallopian tubes, also known as uterine tubes or oviducts, are a pair of slender tubular structures in the female reproductive system. They play a crucial role in human reproduction by providing a passageway for the egg (ovum) from the ovary to the uterus (womb).

Each Fallopian tube is typically around 7.6 to 10 centimeters long and consists of four parts: the interstitial part, the isthmus, the ampulla, and the infundibulum. The fimbriated end of the infundibulum, which resembles a fringe or frill, surrounds and captures the released egg from the ovary during ovulation.

Fertilization usually occurs in the ampulla when sperm meets the egg after sexual intercourse. Once fertilized, the zygote (fertilized egg) travels through the Fallopian tube toward the uterus for implantation and further development. The cilia lining the inner surface of the Fallopian tubes help propel the egg and the zygote along their journey.

In some cases, abnormalities or blockages in the Fallopian tubes can lead to infertility or ectopic pregnancies, which are pregnancies that develop outside the uterus, typically within the Fallopian tube itself.

Follicle-Stimulating Hormone (FSH) is a glycoprotein hormone secreted and released by the anterior pituitary gland. In females, it promotes the growth and development of ovarian follicles in the ovary, which ultimately leads to the maturation and release of an egg (ovulation). In males, FSH stimulates the testes to produce sperm. It works in conjunction with luteinizing hormone (LH) to regulate reproductive processes. The secretion of FSH is controlled by the hypothalamic-pituitary-gonadal axis and its release is influenced by the levels of gonadotropin-releasing hormone (GnRH), estrogen, inhibin, and androgens.

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.

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

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

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

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

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

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

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.

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

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

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

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

The mesoderm contributes to the formation of structures such as:

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

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

The testis, also known as the testicle, is a male reproductive organ that is part of the endocrine system. It is located in the scrotum, outside of the abdominal cavity. The main function of the testis is to produce sperm and testosterone, the primary male sex hormone.

The testis is composed of many tiny tubules called seminiferous tubules, where sperm are produced. These tubules are surrounded by a network of blood vessels, nerves, and supportive tissues. The sperm then travel through a series of ducts to the epididymis, where they mature and become capable of fertilization.

Testosterone is produced in the Leydig cells, which are located in the interstitial tissue between the seminiferous tubules. Testosterone plays a crucial role in the development and maintenance of male secondary sexual characteristics, such as facial hair, deep voice, and muscle mass. It also supports sperm production and sexual function.

Abnormalities in testicular function can lead to infertility, hormonal imbalances, and other health problems. Regular self-examinations and medical check-ups are recommended for early detection and treatment of any potential issues.

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.

The prostate is a small gland that is part of the male reproductive system. Its main function is to produce a fluid that, together with sperm cells from the testicles and fluids from other glands, makes up semen. This fluid nourishes and protects the sperm, helping it to survive and facilitating its movement.

The prostate is located below the bladder and in front of the rectum. It surrounds part of the urethra, the tube that carries urine and semen out of the body. This means that prostate problems can affect urination and sexual function. The prostate gland is about the size of a walnut in adult men.

Prostate health is an important aspect of male health, particularly as men age. Common prostate issues include benign prostatic hyperplasia (BPH), which is an enlarged prostate not caused by cancer, and prostate cancer, which is one of the most common types of cancer in men. Regular check-ups with a healthcare provider can help to detect any potential problems early and improve outcomes.

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

... called activin βA, activin βB, activin βC and activin βE. Activin βA and βB are identical to the two beta subunits of inhibin. ... Two activin βA subunits give rise to activin A, one βA, and one βB subunit gives rise to activin AB, and so on. Various, but ... In the male, activin enhances spermatogenesis. Activin is strongly expressed in wounded skin, and overexpression of activin in ... Activin type 1 receptors: ACVR1, ACVR1B, ACVR1C Activin type 2 receptors: ACVR2A, ACVR2B Activin binds to the Type II receptor ...
... inhibin/activin betaA and betaB and the activin type II and inhibin beta-glycan receptors in the developing human testis". ... The activin type 2 receptors belong to a larger TGF-beta receptor family and modulate signals for transforming growth factor ... There are two activin type two receptors: ACVR2A and ACVR2B. Despite the large amount of processes that these ligands regulate ... Activin plays a significant role in reproduction. ACVR2 receptors are present in the testis during testicular development. ...
The Activin type I receptors transduce signals for a variety of members of the Transforming growth factor beta superfamily of ... There are three type I Activin receptors: ACVR1, ACVR1B, and ACVR1C. Each bind to a specific type II receptor-ligand complex. ... This family of cytokines and hormones include activin, Anti-müllerian hormone (AMH), bone morphogenetic proteins (BMPs), and ...
Stenvers, K. L.; Findlay, J. K. (2012). "Inhibins and activins: Towards the future. A tribute to the late Professor Wylie W. ...
Inhibins and activins also regulate bone mass. Beall, C.; Ashford, M. L.; McCrimmon, R. J. (2011). "The physiology and ... In the reproductive system, inhibins and follistatin counterregulate activins, to control follicle-stimulating hormone and so ... activins, and follistatin in the aging female and male". Semin Reprod Med. 22 (3): 209-17. doi:10.1055/s-2004-831896. PMID ... Activin and Inhibin". Mol Cell Endocrinol. 310 (1-2): 11-20. doi:10.1016/j.mce.2009.07.001. PMC 2951729. PMID 19615428. Watts ...
"Entrez Gene: ACVRL1 activin A receptor type II-like 1". Olivieri C, Mira E, Delù G, Pagella F, Zambelli A, Malvezzi L, ... Oh SP, Seki T, Goss KA, Imamura T, Yi Y, Donahoe PK, Li L, Miyazono K, ten Dijke P, Kim S, Li E (March 2000). "Activin receptor ... It is also known as activin receptor-like kinase 1, or ALK1. This gene encodes a type I cell-surface receptor for the TGF-beta ... ten Dijke P, Ichijo H, Franzén P, Schulz P, Saras J, Toyoshima H, Heldin CH, Miyazono K (October 1993). "Activin receptor-like ...
1997). "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells ... 2001). "Localization of activin beta(A)-, beta(B)-, and beta(C)-subunits in humanprostate and evidence for formation of new ... Furthermore, the beta B subunit forms a homodimer, activin B, and also joins with the beta A subunit to form a heterodimer, ... 2002). "Production of activins by the human endosalpinx". J. Clin. Endocrinol. Metab. 87 (11): 5283-9. doi:10.1210/jc.2001- ...
1992). "Effect of activin A on globin gene expression in purified human erythroid progenitors". Blood. 79 (3): 773-81. doi: ... Shav-Tal Y, Zipori D (2003). "The role of activin a in regulation of hemopoiesis". Stem Cells. 20 (6): 493-500. doi:10.1634/ ... Shimonaka M, Inouye S, Shimasaki S, Ling N (1991). "Follistatin binds to both activin and inhibin through the common subunit". ... Xu J, McKeehan K, Matsuzaki K, McKeehan WL (1995). "Inhibin antagonizes inhibition of liver cell growth by activin by a ...
On the contrary, inhibition of Nodal and Activin signaling enabled the differentiation of hESCs. GRCh38: Ensembl release 89: ... August 2001). "The orphan receptor ALK7 and the Activin receptor ALK4 mediate signaling by Nodal proteins during vertebrate ... Vallier L, Alexander M, Pedersen RA (2006). "Activin/Nodal and FGF pathways cooperate to maintain pluripotency of human ... Chng Z, Vallier L, Pedersen R (2011). "Activin/ nodal signaling and pluripotency". Vitamins and Hormones. 85: 38-58. doi: ...
A truncated activin receptor inhibits mesoderm induction and formation of axial structures in Xenopus embryos. Nature 359:609 - ... Members of the TGF-β superfamily, Activin and Nodal, are essential for mesodermal induction, while FGF and Wnt are in charge of ... Activin-mediated mesoderm induction requires FGF. Development 120:453-462. 8. Kimelman D, Griffin KJ. Vertebrate mesendoderm ... In Xenopus, VegT activates transcription of Nodal-related genes (Xnr) genes, Activin and other mesodermal transcripts, which ...
"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. ...
... is an activin type 2 receptor. This gene encodes activin A type II receptor. Activins are dimeric growth and ... "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells". ... "Variations in activin receptor, inhibin/activin subunit and follistatin mRNAs in human prostate tumour tissues". Br. J. Cancer ... "Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. ...
In the blood, activin and follistatin are both known to be involved in the inflammatory response following tissue injury or ... The activin-binding protein follistatin is produced by folliculostellate (FS) cells of the anterior pituitary. FS cells make ... Follistatin also known as activin-binding protein is a protein that in humans is encoded by the FST gene. Follistatin is an ... In the tissues activin has a strong role in cellular proliferation, thereby making follistatin the safeguard against ...
"Activin A Is Essential for Neurogenesis Following Neurodegeneration". Stem Cells. 27 (6): 1330-46. doi:10.1002/stem.80. PMC ...
"Activin signaling regulates Sertoli cell differentiation and function". Endocrinology. 153 (12): 6065-77. doi:10.1210/en.2012- ... secreted during the early stages of fetal life inhibin and activins, secreted after puberty, work together to regulate FSH ...
It binds to and inhibits activin receptor type-2B. On August 20, 2013, it was announced that bimagrumab had received a ... an activin receptor type II inhibitor, on pituitary neurohormonal axes". Clinical Endocrinology. 88 (6): 908-919. doi:10.1111/ ...
Labonne, C.; Whitman, M. (1994-05-01). "Mesoderm induction by activin requires FGF-mediated intracellular signals". Trends in ... During her doctoral study, LaBonne discovered that activin-mediated mesoderm induction required FGF signaling and elucidated ...
Kato MV (2000). "A secreted tumor-suppressor, mac25, with activin-binding activity". Mol. Med. 6 (2): 126-35. doi:10.1007/ ...
The cytokines interleukin-1α (IL-1α), IL-6 and Activin A are found in the testis, often at high levels. In other tissues, these ... Lee W, Mason AJ, Schwall R, Szonyi E, Mather JP (1989). "Secretion of activin by interstitial cells in the testis". Science. ... Boitani C, Stefanini M, Fragale A, Morena AR (1995). "Activin stimulates Sertoli cell proliferation in a defined period of rat ... Mather JP, Attie KM, Woodruff TK, Rice GC, Phillips DM (1990). "Activin stimulates spermatogonial proliferation in germ-Sertoli ...
Ovine uterine serpin also binds to activin, IgM and IgA. Another possible role for uterine serpins is in the inhibition of ... October 1999). "Uterine milk protein, a novel activin-binding protein, is present in ovine allantoic fluid". Endocrinology. 140 ...
Zhou S, Zawel L, Lengauer C, Kinzler KW, Vogelstein B (July 1998). "Characterization of human FAST-1, a TGF beta and activin ... FOXH1 encodes a human homolog of Xenopus forkhead activin signal transducer-1. FOXH1 protein binds SMAD2 and activates an ... "Smad4 and FAST-1 in the assembly of activin-responsive factor". Nature. 389 (6646): 85-89. Bibcode:1997Natur.389...85C. doi: ... "Smad4 and FAST-1 in the assembly of activin-responsive factor". Nature. 389 (6646): 85-89. Bibcode:1997Natur.389...85C. doi: ...
Activin A receptor type 2A (ACVR2A) is a transmembrane receptor that is involved in ligand-binding and mediates the functions ... "ACVR2A activin A receptor type 2A [Homo sapiens (human)] - Gene - NCBI". Gene. Bock, J B; Klumperman, J; Davanger, S; Scheller ... of activins. Syntaxin 6 functions in trans-Golgi network vesicle trafficking, perhaps targeting to endosomes in mammalian cells ...
2003). "Inhibin, activin, follistatin, activin receptors and beta-glycan gene expression in the placental tissue of patients ... 2003). "Activin betaC-subunit heterodimers provide a new mechanism of regulating activin levels in the prostate". Endocrinology ... 2001). "Localization of activin beta(A)-, beta(B)-, and beta(C)-subunits in humanprostate and evidence for formation of new ... Inhibins and activins, also members of the TGF-beta superfamily, are hormones with opposing actions and are involved in ...
BMP and activin membrane-bound inhibitor homolog (Xenopus laevis), also known as BAMBI, is a protein which in humans is encoded ... "Entrez Gene: BMP and activin membrane-bound inhibitor homolog (Xenopus laevis)". Degen WG, Weterman MA, van Groningen JJ, ... 2008). "The pseudoreceptor BMP and activin membrane-bound inhibitor positively modulates Wnt/beta-catenin signaling". J. Biol. ... 2004). "Identification of BMP and activin membrane-bound inhibitor (BAMBI), an inhibitor of transforming growth factor-beta ...
ACE-011 was a chimeric protein, created by fusing the binding portion of the activin type 2 receptors to part of an antibody; ... the resulting protein binds to activin and prevents it from acting. Knopf took over as CEO in 2007. He became known for showing ... a protein therapeutic that was an activin type 2 receptor antagonist intended to treat bone loss. ...
"Activin A and follistatin in patients with nonalcoholic fatty liver disease". Metabolism. 65 (10): 1550-8. doi:10.1016/j. ... skeletal tissue hormones including activins, follistatins and irisin as well as with the quality of the diet and the protective ...
A mutation in the gene ACVR1 (also known as activin-like kinase 2 (ALK2)) is responsible for the disease. ACVR1 encodes activin ... Normally, the ACVR1 gene encodes the activin receptor type-1 transmembrane kinase that bind BMP receptors (Type I BMPR and Type ... Fibro/adipogenic progenitors (FAPs) may be the disease-causing cell type responsible for activin A dependent ectopic bone ... the company initiated a phase 1 study of its activin antibody, REGN 2477, in healthy volunteers; a phase 2 trial in FOP ...
This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. ... Lebrun JJ, Takabe K, Chen Y, Vale W (January 1999). "Roles of pathway-specific and inhibitory Smads in activin receptor ... "Smad4 and FAST-1 in the assembly of activin-responsive factor". Nature. 389 (6646): 85-9. Bibcode:1997Natur.389...85C. doi: ...
It blocks TGFβ1 and activin associating with the receptor, blocking access to SMAD2. It is an inhibitory SMAD (I-SMAD) and is ... By occupying type I receptors for Activin and bone morphogenetic protein (BMP), it also plays a role in negative feedback of ... Lebrun JJ, Takabe K, Chen Y, Vale W (January 1999). "Roles of pathway-specific and inhibitory Smads in activin receptor ... and activin-mediated growth arrest and apoptosis in B cells". J. Biol. Chem. 274 (19): 13637-42. doi:10.1074/jbc.274.19.13637. ...
... and activin are involved in regulating important cellular functions such as proliferation, differentiation, apoptosis, and ... "Repression of bone morphogenetic protein and activin-inducible transcription by Evi-1". The Journal of Biological Chemistry. ... "Repression of bone morphogenetic protein and activin-inducible transcription by Evi-1". The Journal of Biological Chemistry. ...
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 ...
There are three activins: Activin A, Activin B and Activin AB. Activins are involved in embryogenesis and osteogenesis. They ... It can then either form a receptor complex with activin A receptor, type IB (ACVR1B) or with activin A receptor, type IC ( ... TGFβs, Activins, Nodals and some GDFs are mediated by SMAD2 and SMAD3, while BMPs, AMH and a few GDFs are mediated by SMAD1, ... BMP and activin membrane bound inhibitor (BAMBI), has a similar extracellular domain as type I receptors. It lacks an ...
"Entrez Gene: INHBA inhibin, beta A (activin A, activin AB alpha polypeptide)". Lewis, K A; Gray P C; Blount A L; MacConell L A ... "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells" (PDF). ... 2005). "Activin, inhibin and the human breast". Mol. Cell. Endocrinol. 225 (1-2): 77-82. doi:10.1016/j.mce.2004.02.016. PMID ... 1992). "Effect of activin A on globin gene expression in purified human erythroid progenitors". Blood. 79 (3): 773-81. doi: ...
Activin receptor type-2B is a protein that in humans is encoded by the ACVR2B gene. ACVR2B is an activin type 2 receptor. ... This gene encodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A type ... Schneider-Kolsky ME, Manuelpillai U, Waldron K, Dole A, Wallace EM (2002). "The distribution of activin and activin receptors ... "Inhibin interferes with activin signaling at the level of the activin receptor complex in Chinese hamster ovary cells". ...
Activin A receptor, type I (ACVR1) is a protein which in humans is encoded by the ACVR1 gene; also known as ALK-2 (activin ... This gene encodes activin A type I receptor which signals a particular transcriptional response in concert with activin type II ... Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I ( I and IB) and two ... "Entrez Gene: ACVR1 (activin A receptor, type I)". Inman GJ, Nicolás FJ, Callahan JF, Harling JD, Gaster LM, Reith AD, Laping NJ ...

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