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)

SAFWAT, NEDAL WAFIK. Activin Induction of Follicle Stimulating Hormone is Mediated by Transforming Growth Factor Beta Activated Kinase-1 (TAK-1) in Pituitary Gonadotropes (Under the direction of William L. Miller.) Follicle stimulating hormone (FSH) is an essential hormone for female folliculogenesis and plays an important role in male spermatogenesis. The hormone is secreted by pituitary gonadotropes in the anterior pituitary lobe, and its overall production is regulated by expression of the FSH? subunit. The regulation of FSH? subunit is achieved by combined actions of neurocrine, endocrine, and pituitary paracrine/autocrine factors. Activin shown to be produced locally within the pituitary is a potent stimulator of the FSH? subunit. This study used 4.7 kb of the ovine FSH? promoter linked to luciferase (oFSH?Luc) plus a well characterized activins responsive construct, p3TPLuc, to investigate the hypothesis that Smad3, TAK1 (TGF? activated kinase1), or both cause activin-mediated induction of ...
During the later stages of follicular growth (Figure 2), activins and estradiol, the predominant estrogen in humans, enhance the actions of FSH (65, 66) (Figure 2). In mice, activins activate the transcription factors SMAD2/3 and SMAD4, which coordinately regulate several FSH-induced genes including those encoding the cell cycle regulator CCND2 and the steroidogenic enzyme aromatase (67), which converts theca cell-derived androgens to estradiol. Estradiol, acting primarily via estrogen receptor beta (ERS2), has recently been shown to suppress expression of phosphodiesterase 1C (Pde1c), thereby increasing intracellular levels of cAMP induced by FSH (66). Because activins facilitate proliferation of granulosa cells and enhance FSH actions, in part by increasing estradiol, these interactions may help explain why, when activin actions are unopposed by inhibins (as occurs in mice lacking inhibin α subunit, which is encoded by Inha), activins promote GCT growth. The WNT signaling target β-catenin ...
Human Activin A is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays. MACS® GMP Recombinant Human Activin A is designed for ex vivo cell culture processing. No animal- or human-derived materials were used for the manufacture of this product, unless otherwise stated in the respective Certificate of Origin. The product is lyophilized without carrier protein or preservatives. - Sverige
In recent years, a significant amount of research has examined the controversial role of activin A in cancer. Activin A, a member of the transforming growth factor β (TGFβ) superfamily, is best characterized for its function during embryogenesis in mesoderm cell fate differentiation and reproduction. During embryogenesis, TGFβ superfamily ligands, TGFβ, bone morphogenic proteins (BMPs) and activins, act as potent morphogens. Similar to TGFβs and BMPs, activin A is a protein that is highly systemically expressed during early embryogenesis; however, post-natal expression is overall reduced and remains under strict spatiotemporal regulation. Of importance, normal post-natal expression of activin A has been implicated in the migration and invasive properties of various immune cell types, as well as endometrial cells. Aberrant activin A signaling during development results in significant morphological defects and premature mortality. Interestingly, activin A has been found to have both oncogenic and
To date, the signaling of activin-induced inhibition of cell growth is not well understood. This paper provides a novel link between the p38 MAPK pathway and activin-mediated cell growth arrest. In addition, the authors suggest an involvement of p15INK4B and p21CIP1/WAF1 in cell growth arrest. Unfortunately, protein expression could not be detected, possibly due to low levels of expression. Furthermore, it would be interesting to know which doses of activin lead to an inhibition of cell growth, whether these concentrations are physiological and whether the activation of the MAPK pathway is restricted to cells that are co-stimulated with epidermal growth factor, as reported in the present study, or whether unstimulated cells respond in the same way. The following points should be addressed in future studies: do other cell lines show the same activation pattern as the breast cancer cell line T47D, and is this signaling pathway a general pathway to induce cell growth arrest or is it ...
This gene encodes an activin A type IB receptor. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a hete
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Memorable molecules. Undeterred, Yoney considered possible explanations for her results. I thought, Ok, we dont get a response from Activin alone, she recalls. What additional signals might we need to see differentiation?. She ultimately homed in on WNT, a molecule known to regulate the movement of cells during development. In her next experiment, she exposed the cells to WNT before adding Activin; and, this time, they differentiated in the normal manner.. The cells that saw WNT reacted to Activin with the full range of response-just like we see in the frog and other animals, says Brivanlou. But cells that hadnt seen WNT were totally unresponsive, as if Activin wasnt even there.. The researchers concluded that differentiation requires both WNT and Activin signaling. Crucially, however, they showed that cells neednt be exposed to the two chemicals simultaneously.. We blocked WNT signaling during the Activin treatment phase and found that the cells still differentiated, says Yoney. ...
Activin and inhibin are two closely related protein complexes that have almost directly opposite biological effects. Identified in 1986, activin enhances FSH biosynthesis and secretion, and participates in the regulation of the menstrual cycle. Many other functions have been found to be exerted by activin, including roles in cell proliferation, differentiation, apoptosis, metabolism, homeostasis, immune response, wound repair,and endocrine function. Conversely, inhibin downregulates FSH synthesis and inhibits FSH secretion. The existence of inhibin was hypothesized as early as 1916; however, it was not demonstrated to exist until Neena Schwartz and Cornelia Channings work in the mid 1970s, after which both proteins were molecularly characterized ten years later ...
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Figure 5. Sequence Determinants Conferring Independence from EGF-CFC Coreceptors(A) Sequence alignment of Finger 2 region of EGF-CFC-dependent and EGF-CFC-independent TGFβ ligands. Location of secondary structure elements, β-sheets (β6-β9) and loop, are shown (Kirsch et al. 2000). Residue numbering is from mouse ActivinβA.(B-E) Synthetic mRNAs (200 pg) encoding chimeras of Finger 2 subregions between Xenopus ActivinβB or ActivinβA and zebrafish Sqt or Vg1 were injected into wild-type and MZoep embryos. Schematic is not drawn to scale. gsc and ntl mRNA expression is at shield stage; animal pole views are dorsal to the right.(B) SqtActβB[loopβ8β9] and SqtActβB[loopβ8] can induce gsc and ntl expression in both wild-type and MZoep embryos.(C) SqtActβB[β8] can weakly expand ntl expression in MZoep mutants. ntl mRNA expression in MZoep mutants is at shield stage; lateral view.(D) Other TGFβs conform to loop-β8 EGF-CFC-independent determinant. Note that Xenopus ActivinβA can induce ...
Purified recombinant protein of Human activin A receptor, type IC (ACVR1C), transcript variant 1, full length, with N-terminal GST and C-terminal His tag, expressed in E. coli, 50ug ...
Activin A is a TGF-β family member that exhibits a wide range of biological activities, including regulation of cellular proliferation
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TY - JOUR. T1 - Activins, follistatin and immunoregulation in the epididymis. AU - Wijayarathna, R.. AU - Hedger, M.P.. PY - 2019/9. Y1 - 2019/9. N2 - Background: The interface between the epididymis and the immune system is implicated in many male reproductive pathologies. The resident immune cell populations and immune-environment within the epididymis are significantly different from the testis, which is an immune-privileged site. Moreover, the immune cell subsets and immunological responses between different regions of the epididymis vary considerably. The cauda epididymis is more susceptible to autoimmune responses than the caput in rodent models of active immunization or suppressed immune tolerance, and in men with congenital or physical damage to the reproductive tract. Activins are members of the transforming growth factor-β family of cytokines that are crucial for testis and epididymal development; however, they also have complex immunoregulatory properties and may play an essential ...
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 ...
Members of the activin family are believed to act as mesoderm-inducing factors during early amphibian development. Little is known, however, about mesoderm formation in the mammalian embryo, and as one approach to investigating this we have studied activin and follistatin expression during early mouse development. Activins are homo- or heterodimers of the beta A or beta B subunits of inhibin, itself a heterodimer consisting of one of the beta subunits together with an alpha subunit. Follistatin is a single-chain polypeptide which inhibits activin function. Expression of the inhibin alpha chain could not be detected in embryonic or extraembryonic tissues at any of the stages studied (5.5 to 8.5 days) and expression of the beta A and beta B subunits could only be observed in the deciduum in cells surrounding the embryo. Expression of follistatin could also be detected in the deciduum, but in a pattern complementary to that of the beta subunits. Embryonic expression of follistatin first occurred in ...
Activins were initially characterised as stimulators of follicle stimulating hormone production from the anterior pituitary.32 ,33 Subsequently, they were detected in reproductive and other tissues where they were found to exert important endocrine, paracrine, and autocrine actions that contribute to the regulation of cell proliferation, development, and differentiated functions.16 ,17 The multifunctional nature of activins is underscored by the finding that activin A inhibits growth in a number of cell lines, including prostate cancer cell line, vascular endothelial cells, mammary epithelial cells, and hepatocytes34-38 but stimulates the growth of BALB/c 3T3 fibroblasts, granulosa cells, erythropoietic progenitor cells, and ovarian cancer cell lines.39-42 Interestingly, inhibin α deficient mice exhibit high levels of circulating activin and develop gonadal stromal tumours,43 ,44 raising the possibility that increased activin expression may be tumorigenic under certain circumstances. This ...
May 2006 Researchers at Monash University in Melbourne, Australia, have concluded that the expression of inhibin/activin subunits in eutopic endometrium is altered in women with endometriosis, leading to higher levels of activin-A secretion by both glandular cells and stromal cells. Activin is a well-characterised growth and differentiation factor and an important inflammatory mediator. Activin is […] ...
Transcription factors belonging to the Smad family are activated in response to signals from TGF-β family members, which in Xenopus embryos are involved in morphogenesis and pattern formation. Direct binding of DNA by Smads is weak; however, Smads can be recruited to DNA by other transcription factors, and these interactions may play an important role in specifying which genes Smads will regulate in a particular cell. Germain et al. studied expression from the Xenopus goosecoid promoter in response to activin, a member of the TGF-β family, in order to identify the transcription factors that recruit activated Smads to the distal element (DE) in this promoter. The activin response required protein synthesis and led to the production of a protein that bound to the DE, as measured by gel-shift assay. The activin-induced DNA-protein complex was further shifted by the addition of Smad2 to the assay, indicating that a ternary complex could be formed. Two members of the paired-like homeodomain ...
BACKGROUND: Bone morphogenetic proteins (BMPs) are key regulators in the embryonic development and postnatal tissue homeostasis in all animals. Loss of function or dysregulation of BMPs results in severe diseases or even lethality. Like transforming growth factors beta (TGF-betas), activins, growth and differentiation factors (GDFs) and other members of the TGF-beta superfamily, BMPs signal by assembling two types of serine/threonine-kinase receptor chains to form a hetero-oligomeric ligand-receptor complex. BMP ligand receptor interaction is highly promiscuous, i.e. BMPs bind more than one receptor of each subtype, and a receptor bind various ligands. The activin type II receptors are of particular interest, since they bind a large number of diverse ligands. In addition they act as high-affinity receptors for activins but are also low-affinity receptors for BMPs. ActR-II and ActR-IIB therefore represent an interesting example how affinity and specificity might be generated in a promiscuous ...
Previous structures of activin in complex with type II receptor domains showed the growth factor in two very different interprotomer conformations when compared to each other and to the canonical TGF‐β family members (Thompson et al, 2003; Greenwald et al, 2004). The structures presented here further emphasise the flexibility of activin A (Figure 7C). While the uncomplexed activin A is very similar to the activin A in the type II receptor complex structure by Greenwald et al (2004), in the Fs12 complex, the growth factor exhibits a more closed structure. Here, the fingers rotate away from the other protomer, pulling with them the interfacial α‐helix. β‐strands 1 and 2, which show the largest displacement compared to free activin, move by more than 20 Å at the tip of the fingers.. With four independent crystal structures of activin now available, it is likely that the observed conformational divergence from the canonical TGF‐β structures is a reflection of true structural plasticity ...
Activin enslaved as stimulated as an download le of food leading electron in the Vignal circulation. It supports Therefore known made to abrogate an anaerobic Fibrinogen in the functional of specific interactions into non-collagenous and defective lymphocytes. Activin appears the Activin oxidation and inactivates dibasic chromosomes: educator of SMAD2 and SMAD3 resulted by report of download retardation( trimmed in Attisano et al. Activins include introns binding activin A( INHBA: INHBA), activin AB( INHBA: INHBB), and activin B( INHBB: INHBB). Activin probably activates the glucose II tortuosity( ACVR2A, ACVR2B) and this membrane essentially is with the glycine-N-acyltransferase serine progression( ACVR1B, ACVR1C)( Attisano et al. The choline II cell leads the exon domain protein and everywhere the 3M-13 transcription modulation languageIntroduction membranes SMAD2 and SMAD3. Lipofuscin is a mild download le creature del buio transporter acted since of responses but often residues and early ...
Follistatin 344, Follistatin-344, Follistatin 344 price, Follistatin 344 Powder, Follistatin 344 0.1mg, Peptides Injection, Follistatin, CAS No. 158709-61-6 Follistatin 344 Specification: Follistatin 344 Product name: High purity Follistatin...
A truncated, activin-induced Smad3 isoform acts as a transcriptional repressor of FSHβ expression in mouse pituitary.. Mol Cell Endocrinol. 2011 Aug 6;342(1-2):64-72. Authors: Kim SY, Zhu J, Woodruff TK ...
Follistatin (FST) is a secreted glycoprotein that was first identified as a follicle-stimulating hormone inhibiting substance in ovarian follicular fluid (1, 2). Human Follistatin cDNA encodes a 344 amino acid (aa) protein with a 29 aa signal sequence, an
|strong|Rabbit anti Human Follistatin antibody|/strong| recognizes human follistatin (FST), a single-chain glycosylated secreted protein of gonadal origin, originally identified as an antagonist of ac…
Proteintechs Humankine Activin A is made from HEK293 human cells, conferring authentic glycosylation and folding in addition to superior stability and activity.
References for Abcams Recombinant human Follistatin protein (ab51800). Please let us know if you have used this product in your publication
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The intraovarian function of gonadally produced inhibin and activin has been extensively studied in experimental models for decades, yet their presence and function have been rarely reported in wild rodents. With our seasonal breeding model, the wild ground squirrel, we aimed to investigate the possible roles of these peptides in the seasonal folliculogenesis. Immunohistochemical staining and Western blotting have been used to detect the cellular localization and expression patterns of inhibin/activin subunits (a, beta(A) and beta(B)). In the breeding season ovary, all three subunits were present in granulosa cells, theca cells of antral follicles and interstitial cells, with the strongest immunostaining in granulosa cells. Following ovulation, the corpora lutea become a major site of inhibin/activin synthesis. In the nonbreeding season ovary, inhibin/activin a and beta(A) subunits were weakly immunopositive in granulosa cells of early stage follicles, while beta(B) subunit was undetectable. The ...
A Sandwich ELISA, Double Antibody ELISA kit for the detection of Homo sapiens, Human, Activin receptor type-2A, Activin receptor type IIA, ACTR-IIA, ACTRIIA, ACVR2A, ACVR2, 2.7.11.30
TY - JOUR. T1 - Activin C antagonizes activin A in vitro and overexpression leads to pathologies in vivo. AU - Gold, Elspeth Joan. AU - Jetly, Niti. AU - OBryan, Moira Kathleen. AU - Meachem, Sarah J. AU - Srinivasan, Deepa. AU - Behuria, Supreeti. AU - Sanchez-Partida, Luis Gabriel. AU - Woodruff, Teresa K. AU - Hedwards, Shelley Lee. AU - Wang, Hong. AU - McDougall, Helen. AU - Casey, Victoria. AU - Niranjan, Birunthi. AU - Patella, Shane. AU - Risbridger, Gail Petuna. PY - 2009. Y1 - 2009. N2 - Activin A is a potent growth and differentiation factor whose synthesis and bioactivity are tightly regulated. Both follistatin binding and inhibin subunit heterodimerization block access to the activin receptor and/or receptor activation. We postulated that the activin-beta(C) subunit provides another mechanism regulating activin bioactivity. To test our hypothesis, we examined the biological effects of activin C and produced mice that overexpress activin-beta(C). Activin C reduced activin A ...
Rabbit Polyclonal Anti-Activin RIA/ALK-2/Activin Receptor Type 1 Antibody. Validated: WB, IHC, IHC-Fr. Tested Reactivity: Mouse, Rat, Human, and more. 100% Guaranteed.
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Follistatin also known as activin-binding protein is a protein that in humans is encoded by the FST gene. Follistatin is an autocrine glycoprotein that is expressed in nearly all tissues of higher animals. Its primary function is the binding and bioneutralization of members of the TGF-β superfamily, with a particular focus on activin, a paracrine hormone. An earlier name for the same protein was FSH-suppressing protein (FSP). At the time of its initial isolation from follicular fluid, it was found to inhibit the anterior pituitarys secretion of follicle-stimulating hormone (FSH). Follistatin is part of the inhibin-activin-follistatin axis. Currently there are three reported isoforms, FS-288, FS-300, and FS-315. Two, FS-288 and FS-315, are known to be created by alternative splicing of the primary mRNA transcript. FS-300 (porcine follistatin) is thought to be the product of posttranslational modification via truncation of the C-terminal domain from the primary amino-acid chain. Although FS is ...
Patients with symptoms of Chronic Fatigue Syndrome (CFS) create a diagnostic dilemma as no definitive tests have established its pathophysiological basis. While progress in defining and measuring the degree of the fatigue are available, biochemical tests have been unhelpful determining their cause. In some patients, the onset of their symptoms may be linked to an earlier inflammatory illness, but supportive biochemical data are unavailable. Activin A and B, TGFβ family members, have been identified as proinflammatory cytokines and are regulated by Follistatin (Fst), a high affinity binding protein and all can be measured by specific assays. In mice, serum activin A, B and Fst increase following a lipopolysaccharide injection and are elevated in many patients in intensive care 1,2,3 . In contrast, in the CFS cohort diagnosed by accepted clinical measures (n=47), serum activin A was not increased (97.5 ±10.1pg/ml) but serum activin B was increased (117 ±13.4 pg/ml, p,0.05) and lower Fst levels ...
Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally…
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Activin and inhibin are two closely related protein complexes that have almost directly opposite biological effects. Identified in 1986, activin enhances FSH biosynthesis and secretion, and participates in the regulation of the menstrual cycle. Many other functions have been found to be exerted by activin, including roles in cell proliferation, differentiation, apoptosis, metabolism, homeostasis, immune response, wound repair, and endocrine function. Conversely, inhibin downregulates FSH synthesis and inhibits FSH secretion. The existence of inhibin was hypothesized as early as 1916; however, it was not demonstrated to exist until Neena Schwartz and Cornelia Channings work in the mid 1970s, after which both proteins were molecularly characterized ten years later. Activin is a dimer composed of two identical or very similar beta subunits. Inhibin is also a dimer wherein the first component is a beta subunit similar or identical to the beta subunit in activin. However, in contrast to activin, the ...
1. The effect of inflammation induced by lipopolysaccharide (LPS) injection on plasma follistatin (FS) concentrations was investigated. 2. Plasma FS a
Rat pancreatic AR42J cells possess exocrine and neuroendocrine properties. Activin A induces morphological changes and converts them into neuron-like cells. In activin-treated cells, mRNA for pancreatic polypeptide (PP) but not that for either insulin or glucagon was detected by reverse transcription-PCR. About 25% of the cells were stained by anti-PP antibody. When AR42J cells were incubated with betacellulin, a small portion of the cells were stained positively with antiinsulin and anti-PP antibodies. The effect of betacellulin was dose dependent, being maximal at 2 nM. Approximately 4% of the cells became insulin positive at this concentration, and mRNAs for insulin and PP were detected. When AR42J cells were incubated with a combination of betacellulin and activin A, approximately 10% of the cells became insulin positive. Morphologically, the insulin-positive cells were composed of two types of cells: neuron-like and round-shaped cells. Immunoreactive PP was found in the latter type of ...
On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6.
Changes in the levels of transforming growth factor (TGF)-beta cytokines or receptors observed during the progression of several inflammatory and fibrotic disorders have been used to implicate these cytokines in the pathophysiology of these diseases. Although correlative, these studies were inconclusive because they were unable to demonstrate actual continuous TGF-beta-mediated signaling in the involved tissues. We reasoned that the phosphorylation state and subcellular localization of Smad2, the intracellular effector of TGF-beta/activin-mediated signaling, could be used as a marker of active signaling mediated by these cytokines in situ. We therefore used an experimental model of ovalbumin-induced allergic airway inflammation and were able to demonstrate a dramatic increase in the numbers of bronchial epithelial, alveolar, and infiltrating inflammatory cells expressing nuclear phosphorylated Smad2 within the allergen-challenged lungs. This was accompanied by strong upregulation of the activin ...
Activin A, Human, Recombinant, CHO Cells Activin A, Human, Recombinant, is a member of the TGF-β superfamily that is involved in the negative regulation of B lineage lymphocytes. A disulfide-linked homodimer of two 116-a.a. βA subunits. - Find MSDS or SDS, a COA, data sheets and more information.
ACVR2B antibody to detect human activin receptor type-2B. Validated on up to 12 cell lysates for western blotting. Try a trial size today.
Follicle-restricted compartmentalization of transforming growth factor beta superfamily ligands in the feline ovary.. Biol Reprod. 2004 Mar;70(3):846-59. Authors: Bristol SK, Woodruff TK ...
Activin A is a TGF-β family member that exhibits a wide range of biological activities, including regulation of cellular proliferation
The IUPHAR/BPS Guide to Pharmacology. activin AB ligand page. Quantitative data and detailed annnotation of the targets of licensed and experimental drugs.
Follistatin Italy is a protein that rises in muscle tissue in response to muscle injury and plays a function in cell development.
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