Contents 1 Structure 2 Function 2.1 Activin 2.2 Inhibin 2.2.1 In females 2.2.2 In males 3 Mechanism of action 3.1 Activin 3.2 Inhibin 4 Clinical significance 4.1 Activin 4.2 Inhibin 5 References 6 External links

Structure[edit] The activin and inhibin protein complexes are both dimeric in structure, and, in each complex, the two monomers are linked to one another by a single disulfide bond.[10] In addition, both complexes are derived from the same family of related genes and proteins but differ in their subunit composition.[7] Below is a list of the most common inhibin and activin complexes and their subunit composition: Class Activity Complex Dimer subunits 1 2 Inhibin inhibits FSH secretion Inhibin A α βA Inhibin B α βB Activin stimulates FSH secretion Activin A βA βA Activin AB βA βB Activin B βB βB Schematic diagram of the 1D structures of inhibin and activin. The black line between the monomers represents a disulfide bond. The alpha and beta subunits share approximately 25% sequence similarity, whereas the similarity between beta subunits is approximately 65%.[9] In mammals, four beta subunits have been described, called activin βA, activin βB, activin βC and activin βE. Activin βA and βB are identical to the two beta subunits of inhibin. A fifth subunit, activin βD, has been described in Xenopus laevis. 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 not all theoretically possible, heterodimers have been described.[11][12] The subunits are linked by a single covalent disulfide bond. The βC subunit is able to form activin heterodimers with βA or βB subunits but is unable to dimerize with inhibin α.[13]

Function[edit] Activin[edit] Activin is produced in the gonads, pituitary gland, placenta, and other organs: In the ovarian follicle, activin increases FSH binding and FSH-induced aromatization. It participates in androgen synthesis enhancing LH action in the ovary and testis. In the male, activin enhances spermatogenesis. Activin is strongly expressed in wounded skin, and overexpression of activin in epidermis of transgenic mice improves wound healing and enhances scar formation. Its action in wound repair and skin morphogenesis is through stimulation of keratinocytes and stromal cells in a dose-dependent manner.[14] Activin also regulates the morphogenesis of branching organs such as the prostate, lung, and especially kidney. Activin A increased the expression level of type-I collagen suggesting that activin A acts as a potent activator of fibroblasts. Lack of activin during development results in neural developmental defects. Upregulation of Activin A drives pluripotent stem cells into a mesoendodermal fate, and thus provides a useful tool for stem cell differentiation and organoid formation.[15] Inhibin[edit] In both females and males, inhibin inhibits FSH production. Inhibin does not inhibit the secretion of GnRH from the hypothalamus.[16][17] However, the overall mechanism differs between the sexes: In females[edit] Inhibin is produced in the gonads, pituitary gland, placenta, corpus luteum and other organs. FSH stimulates the secretion of inhibin from the granulosa cells of the ovarian follicles in the ovaries. In turn, inhibin suppresses FSH. Inhibin B reaches a peak in the early- to mid-follicular phase, and a second peak at ovulation. Inhibin A reaches its peak in the mid-luteal phase. Inhibin secretion is diminished by GnRH, and enhanced by insulin-like growth factor-1 (IGF-1). In males[edit] It is secreted from the Sertoli cells,[18] located in the seminiferous tubules inside the testes. Androgens stimulate inhibin production; this protein may also help to locally regulate spermatogenesis.[19]

Mechanism of action[edit] Activin[edit] As with other members of the superfamily, activins interact with two types of cell surface transmembrane receptors (Types I and II) which have intrinsic serine/threonine kinase activities in their cytoplasmic domains: Activin type 1 receptors: ACVR1, ACVR1B, ACVR1C Activin type 2 receptors: ACVR2A, ACVR2B Activin binds to the Type II receptor and initiates a cascade reaction that leads to the recruitment, phosphorylation, and activation of Type I activin receptor. This then interacts with and then phosphorylates SMAD2 and SMAD3, two of the cytoplasmic SMAD proteins. Smad3 then translocates to the nucleus and interacts with SMAD4 through multimerization, resulting in their modulation as transcription factor complexes responsible for the expression of a large variety of genes. Inhibin[edit] In contrast to activin, much less is known about the mechanism of action of inhibin, but may involve competing with activin for binding to activin receptors and/or binding to inhibin-specific receptors.[8]

Clinical significance[edit] Activin[edit] Activin A is more plentiful in the adipose tissue of obese, compared to lean persons.[20] Activin A promotes the proliferation of adipocyte progenitor cells, while inhibiting their differentiation into adipocytes.[20] Activin A also increases inflammatory cytokines in macrophages.[20] A mutation in the gene for the activin receptor ACVR1 results in fibrodysplasia ossificans progressiva, a fatal disease that causes muscle and soft tissue to gradually be replaced by bone tissue.[21] This condition is characterized by the formation of an extra skeleton that produces immobilization and eventually death by suffocation.[21] The mutation in ACVR1 causes activin A, which normally acts as an antagonist of the receptor and blocks osteogenesis (bone growth), to behave as an agonist of the receptor and to induce hyperactive bone growth.[21] On 2 September 2015, Regeneron announced that they had developed an antibody for activin A that effectively cures the disease in an animal model of the condition.[22] Mutations in the ACVR1 gene have also been linked to cancer, especially diffuse intrinsic pontine glioma (DIPG).[23][24][25] In January 2017, the Journal of Translational Medicine reported that elevated Activin B levels with normal Activin A levels provided a biomarker for myalgic encephalomyelitis/chronic fatigue syndrome.[26] Inhibin[edit] Quantification of inhibin A is part of the prenatal quad screen that can be administered during pregnancy at a gestational age of 16–18 weeks. An elevated inhibin A (along with an increased beta-hCG, decreased AFP, and a decreased estriol) is suggestive of the presence of a fetus with Down syndrome.[27] As a screening test, abnormal quad screen test results need to be followed up with more definitive tests. It also has been used as a marker for ovarian cancer.[28][29] Inhibin B may be used as a marker of spermatogenesis function and male infertility. The mean serum inhibin B level is significantly higher among fertile men (approximately 140 pg/mL) than in infertile men (approximately 80 pg/mL).[30] In men with azoospermia, a positive test for inhibin B slightly raises the chances for successfully achieving pregnancy through testicular sperm extraction (TESE), although the association is not very substantial, having a sensitivity of 0.65 (95% confidence interval [CI]: 0.56–0.74) and a specificity of 0.83 (CI: 0.64–0.93) for prediction the presence of sperm in the testes in non-obstructive azoospermia.[31]

References[edit] ^ Vale W, Rivier J, Vaughan J, McClintock R, Corrigan A, Woo W, Karr D, Spiess J (1986). "Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid". Nature. 321 (6072): 776–9. doi:10.1038/321776a0. PMID 3012369.  ^ Ling N, Ying SY, Ueno N, Shimasaki S, Esch F, Hotta M, Guillemin R (1986). "Pituitary FSH is released by a heterodimer of the beta-subunits from the two forms of inhibin". Nature. 321 (6072): 779–82. doi:10.1038/321779a0. PMID 3086749.  ^ Chen YG, Wang Q, Lin SL, Chang CD, Chuang J, Chung J, Ying SY (May 2006). "Activin signaling and its role in regulation of cell proliferation, apoptosis, and carcinogenesis". Experimental Biology and Medicine. 231 (5): 534–44. PMID 16636301.  ^ Sulyok S, Wankell M, Alzheimer C, Werner S (October 2004). "Activin: an important regulator of wound repair, fibrosis, and neuroprotection". Molecular and Cellular Endocrinology. 225 (1–2): 127–32. doi:10.1016/j.mce.2004.07.011. PMID 15451577.  ^ van Zonneveld P, Scheffer GJ, Broekmans FJ, Blankenstein MA, de Jong FH, Looman CW, Habbema JD, te Velde ER (March 2003). "Do cycle disturbances explain the age-related decline of female fertility? Cycle characteristics of women aged over 40 years compared with a reference population of young women". Human Reproduction. 18 (3): 495–501. doi:10.1093/humrep/deg138. PMID 12615813.  ^ Makanji Y, Zhu J, Mishra R, Holmquist C, Wong WP, Schwartz NB, Mayo KE, Woodruff TK (October 2014). "Inhibin at 90: from discovery to clinical application, a historical review". Endocrine Reviews. 35 (5): 747–94. doi:10.1210/er.2014-1003. PMC 4167436 . PMID 25051334.  ^ a b Burger HG, Igarashi M (April 1988). "Inhibin: definition and nomenclature, including related substances". The Journal of Clinical Endocrinology and Metabolism. 66 (4): 885–6. PMID 3346366.  ^ a b Robertson DM, Burger HG, Fuller PJ (March 2004). "Inhibin/activin and ovarian cancer". Endocrine-Related Cancer. Bioscientifica. 11 (1): 35–49. doi:10.1677/erc.0.0110035. PMID 15027884.  ^ a b Kingsley DM (Jan 1994). "The TGF-beta superfamily: new members, new receptors, and new genetic tests of function in different organisms". Genes & Development. 8 (2): 133–46. doi:10.1101/gad.8.2.133. PMID 8299934.  ^ Ying SY (December 1987). "Inhibins and activins: chemical properties and biological activity". Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine. 186 (3): 253–64. doi:10.3181/00379727-186-42611a. PMID 3122219.  ^ Xu P, Hall AK (November 2006). "The role of activin in neuropeptide induction and pain sensation". Developmental Biology. 299 (2): 303–9. doi:10.1016/j.ydbio.2006.08.026. PMID 16973148.  ^ Deli A, Kreidl E, Santifaller S, Trotter B, Seir K, Berger W, Schulte-Hermann R, Rodgarkia-Dara C, Grusch M (March 2008). "Activins and activin antagonists in hepatocellular carcinoma". World Journal of Gastroenterology. 14 (11): 1699–709. doi:10.3748/wjg.14.1699. PMC 2695910 . PMID 18350601. Archived from the original on 22 April 2009.  ^ Mellor SL, Cranfield M, Ries R, Pedersen J, Cancilla B, de Kretser D, Groome NP, Mason AJ, Risbridger GP (December 2000). "Localization of activin beta(A)-, beta(B)-, and beta(C)-subunits in humanprostate and evidence for formation of new activin heterodimers of beta(C)-subunit". The Journal of Clinical Endocrinology and Metabolism. 85 (12): 4851–8. doi:10.1210/jc.85.12.4851. PMID 11134153.  ^ Bamberger C, Schärer A, Antsiferova M, Tychsen B, Pankow S, Müller M, Rülicke T, Paus R, Werner S (September 2005). "Activin controls skin morphogenesis and wound repair predominantly via stromal cells and in a concentration-dependent manner via keratinocytes". The American Journal of Pathology. 167 (3): 733–47. doi:10.1016/S0002-9440(10)62047-0. PMC 1698729 . PMID 16127153. [permanent dead link] ^ Pauklin S, Vallier L (2015). "Activin/Nodal signalling in stem cells". Development. 142 (4): 607–19. doi:10.1242/dev.091769. PMID 25670788.  ^ Luisi S, Florio P, Reis FM, Petraglia F (2005). "Inhibins in female and male reproductive physiology: role in gametogenesis, conception, implantation and early pregnancy". Human Reproduction Update. 11 (2): 123–35. doi:10.1093/humupd/dmh057. PMID 15618291.  ^ Le T, Bhushan V, Hofmann J (2012). First Aid for the USMLE Step 1. McGraw Hill. p. 534. ISBN 978-0-07-177636-3.  ^ Skinner MK, McLachlan RI, Bremner WJ (October 1989). "Stimulation of Sertoli cell inhibin secretion by the testicular paracrine factor PModS". Molecular and Cellular Endocrinology. 66 (2): 239–49. doi:10.1016/0303-7207(89)90036-1. PMID 2515083.  ^ Meachem SJ, Nieschlag E, Simoni M (November 2001). "Inhibin B in male reproduction: pathophysiology and clinical relevance". European Journal of Endocrinology / European Federation of Endocrine Societies. 145 (5): 561–71. doi:10.1530/eje.0.1450561. PMID 11720872.  ^ a b c Zaragosi LE, Wdziekonski B, Villageois P, Keophiphath M, Maumus M, Tchkonia T, Bourlier V, Mohsen-Kanson T, Ladoux A, Elabd C, Scheideler M, Trajanoski Z, Takashima Y, Amri EZ, Lacasa D, Sengenes C, Ailhaud G, Clément K, Bouloumie A, Kirkland JL, Dani C (2010). "Activin a plays a critical role in proliferation and differentiation of human adipose progenitors". Diabetes. 59 (10): 2513–2521. doi:10.2337/db10-0013. PMC 3279533 . PMID 20530742.  ^ a b c Shore EM, Xu M, Feldman GJ, Fenstermacher DA, Cho TJ, Choi IH, Connor JM, Delai P, Glaser DL, LeMerrer M, Morhart R, Rogers JG, Smith R, Triffitt JT, Urtizberea JA, Zasloff M, Brown MA, Kaplan FS (May 2006). "A recurrent mutation in the BMP type I receptor ACVR1 causes inherited and sporadic fibrodysplasia ossificans progressiva". Nature Genetics. 38 (5): 525–527. doi:10.1038/ng1783. PMID 16642017.  ^ Julie Steenhuysen (2 September 2015). "Regeneron scientists discover key to excess bone growth in rare disease". Reuters.  ^ Taylor KR, Mackay A, Truffaux N, Butterfield YS, Morozova O, Philippe C, Castel D, Grasso CS, Vinci M, Carvalho D, Carcaboso AM, de Torres C, Cruz O, Mora J, Entz-Werle N, Ingram WJ, Monje M, Hargrave D, Bullock AN, Puget S, Yip S, Jones C, Grill J (May 2014). "Recurrent activating ACVR1 mutations in diffuse intrinsic pontine glioma". Nature Genetics. 46 (5): 457–61. doi:10.1038/ng.2925. PMC 4018681 . PMID 24705252.  ^ "Cure Brain Cancer - News - Multiple Breakthroughs in Childhood Brain Cancer DIPG". Cure Brain Cancer Foundation.  ^ Buczkowicz P, Hoeman C, Rakopoulos P, Pajovic S, Letourneau L, Dzamba M, et al. (May 2014). "Genomic analysis of diffuse intrinsic pontine gliomas identifies three molecular subgroups and recurrent activating ACVR1 mutations". Nature Genetics. 46 (5): 451–6. doi:10.1038/ng.2936. PMC 3997489 . PMID 24705254.  ^ Lidbury, Brett A.; Kita, Badia; Lewis, Donald P.; Hayward, Susan; Ludlow, Helen; Hedger, Mark P.; de Kretser, David M. (2017-01-01). "Activin B is a novel biomarker for chronic fatigue syndrome/myalgic encephalomyelitis (CFS/ME) diagnosis: a cross sectional study". Journal of Translational Medicine. 15: 60. doi:10.1186/s12967-017-1161-4. ISSN 1479-5876. PMC 5353946 . PMID 28302133.  ^ Aitken DA, Wallace EM, Crossley JA, Swanston IA, van Pareren Y, van Maarle M, Groome NP, Macri JN, Connor JM (May 1996). "Dimeric inhibin A as a marker for Down's syndrome in early pregnancy". The New England Journal of Medicine. 334 (19): 1231–6. doi:10.1056/NEJM199605093341904. PMID 8606718.  ^ Robertson DM, Pruysers E, Jobling T (April 2007). "Inhibin as a diagnostic marker for ovarian cancer". Cancer Letters. 249 (1): 14–7. doi:10.1016/j.canlet.2006.12.017. PMID 17320281.  ^ Robertson DM, Pruysers E, Burger HG, Jobling T, McNeilage J, Healy D (October 2004). "Inhibins and ovarian cancer". Molecular and Cellular Endocrinology. 225 (1–2): 65–71. doi:10.1016/j.mce.2004.02.014. PMID 15451569.  ^ Myers GM, Lambert-Messerlian GM, Sigman M (December 2009). "Inhibin B reference data for fertile and infertile men in Northeast America". Fertility and Sterility. 92 (6): 1920–3. doi:10.1016/j.fertnstert.2008.09.033. PMID 19006797.  ^ Toulis KA, Iliadou PK, Venetis CA, Tsametis C, Tarlatzis BC, Papadimas I, Goulis DG (2010). "Inhibin B and anti-Mullerian hormone as markers of persistent spermatogenesis in men with non-obstructive azoospermia: a meta-analysis of diagnostic accuracy studies". Human Reproduction Update. 16 (6): 713–24. doi:10.1093/humupd/dmq024. PMID 20601364. 

External links[edit] Activin at the US National Library of Medicine Medical Subject Headings (MeSH) Inhibin at the US National Library of Medicine Medical Subject Headings (MeSH) Grusch M, Kreidl E (2008-08-01). "Activin and follistatin in liver biology and hepatocellular carcinoma". SciTopics. Elsevier. Archived from the original on 9 December 2008. Retrieved 2008-12-24.  v t e Cell signaling: TGFβ signaling pathway TGF beta superfamily of ligands TGF beta family TGF-β1 TGF-β2 TGF-β3 Bone morphogenetic proteins BMP2 BMP3 BMP4 BMP5 BMP6 BMP7 BMP8a BMP8b BMP10 BMP15 Growth differentiation factors GDF1 GDF2 GDF3 GDF5 GDF6 GDF7 Myostatin/GDF8 GDF9 GDF10 GDF11 GDF15 Other Activin and inhibin Anti-müllerian hormone Nodal TGF beta receptors (Activin, BMP) TGFBR1: Activin type 1 receptors ACVR1 ACVR1B ACVR1C ACVRL1 BMPR1 BMPR1A BMPR1B TGFBR2: Activin type 2 receptors ACVR2A ACVR2B AMHR2 BMPR2 TGFBR3: betaglycan Transducers/SMAD R-SMAD (SMAD1 SMAD2 SMAD3 SMAD5 SMAD9) I-SMAD (SMAD6 SMAD7) SMAD4 Ligand inhibitors Cerberus Chordin Decorin Follistatin Gremlin Lefty LTBP1 Noggin PARN THBS1 Coreceptors BAMBI Cripto Other SARA v t e Protein, glycoconjugate: glycoproteins and glycopeptides Mucoproteins Mucin CD43 CD164 MUC1 MUC2 MUC3A MUC3B MUC4 MUC5AC MUC5B MUC6 MUC7 MUC8 MUC12 MUC13 MUC15 MUC16 MUC17 MUC19 MUC20 Other Haptoglobin Intrinsic factor Orosomucoid Peptidoglycan Phytohaemagglutinin Ovomucin Proteoglycans CS/DS Decorin Biglycan Versican HS/CS Testican Perlecan CS Chondroitin sulfate proteoglycans: Aggrecan Neurocan Brevican CD44 CSPG4 CSPG5 Platelet factor 4 Structural maintenance of chromosomes 3 KS Fibromodulin Lumican Keratocan HS Syndecan 1 Other Activin and inhibin ADAM Alpha 1-antichymotrypsin Apolipoprotein H CD70 Asialoglycoprotein Avidin B-cell activating factor 4-1BB ligand Cholesterylester transfer protein Clusterin Colony-stimulating factor Hemopexin Lactoferrin Membrane glycoproteins Myelin protein zero Osteonectin Protein C Protein S Serum amyloid P component Sialoglycoprotein CD43 Glycophorin Glycophorin C Thrombopoietin Thyroglobulin Thyroxine-binding proteins Transcortin Tumor necrosis factor alpha Uteroglobin Vitronectin v t e Hormones Endocrine glands Hypothalamic- pituitary Hypothalamus GnRH TRH Dopamine CRH GHRH Somatostatin (GHIH) MCH Posterior pituitary Oxytocin Vasopressin Anterior pituitary FSH LH TSH Prolactin POMC CLIP ACTH MSH Endorphins Lipotropin GH Adrenal axis Adrenal cortex aldosterone cortisol cortisone DHEA DHEA-S androstenedione Adrenal medulla epinephrine norepinephrine Thyroid Thyroid hormone T3 T4 Calcitonin Thyroid axis Parathyroid PTH Gonadal axis Testis testosterone AMH inhibin Ovary estradiol progesterone activin and inhibin relaxin Placenta hCG HPL estrogen progesterone Pancreas glucagon insulin amylin somatostatin pancreatic polypeptide Pineal gland melatonin N,N-dimethyltryptamine 5-methoxy-N,N-dimethyltryptamine Other Thymus Thymosins Thymosin α1 Beta thymosins Thymopoietin Thymulin Digestive system Stomach gastrin ghrelin Duodenum CCK Incretins GIP GLP-1 secretin motilin VIP Ileum enteroglucagon peptide YY Liver/other Insulin-like growth factor IGF-1 IGF-2 Adipose tissue leptin adiponectin resistin Skeleton Osteocalcin Kidney renin EPO calcitriol prostaglandin Heart Natriuretic peptide ANP BNP v t e TGFβ receptor superfamily modulators Type I ALK1 (ACVRL1) Agonists: Activin (A, B, AB) Avotermin BMP (10) Cetermin GDF (2 (BMP9)) TGFβ (1, 2, 3) Antibodies: Ascrinvacumab Kinase inhibitors: K-02288 ML-347 (LDN-193719, VU0469381) Decoy receptors: Dalantercept Other inhibitors: Disitertide ALK2 (ACVR1A) Agonists: Activin (A, B, AB) AMH (MIS) Avotermin BMP (5, 6, 7, 8A, 8B) Eptotermin alfa TGFβ (1, 2, 3) Kinase inhibitors: DMH-1 DMH-2 Dorsomorphin (BML-275) K-02288 ML-347 (LDN-193719, VU0469381) ALK3 (BMPR1A) Agonists: AMH (MIS) BMP (2, 4, 5, 6, 7, 8A, 8B) Dibotermin alfa Eptotermin alfa Kinase inhibitors: DMH-2 Dorsomorphin (BML-275) K-02288 ALK4 (ACVR1B) Agonists: Activin (A, B, AB) GDF (1, 3, 11 (BMP11)) Myostatin (GDF8) Nodal Antagonists: Inhibin (A, B) Lefty (1, 2) Kinase inhibitors: A 83-01 SB-431542 SB-505124 ALK5 (TGFβR1) Agonists: Avotermin GDF (10 (BMP3B), 11 (BMP11)) TGFβ (1, 2, 3) Antibodies: Fresolimumab Lerdelimumab Metelimumab Kinase inhibitors: A 83-01 D-4476 GW-788388 LY-364947 LY-2109761 Galunisertib (LY-2157299) R-268712 RepSox (E-616452, SJN-2511) SB-431542 SB-505124 SB-525334 SD-208 ALK6 (BMPR1B) Agonists: BMP (2, 4, 5, 6, 7, 8A, 8B, 15 (GDF9B)) Dibotermin alfa Eptotermin alfa GDF (5 (BMP14), 6 (BMP13), 7 (BMP12), 9, 15) Radotermin Kinase inhibitors: DMH-2 Dorsomorphin (BML-275) K-02288 ALK7 (ACVR1C) Agonists: GDF (1, 3, 11 (BMP11)) Nodal Antagonists: Lefty (1, 2) Kinase inhibitors: A 83-01 SB-431542 SB-505124 Type II TGFβR2 Agonists: Avotermin GDF (10 (BMP3B)) TGFβ (1, 2, 3) Antibodies: Fresolimumab Lerdelimumab Metelimumab Kinase inhibitors: DMH-2 LY-364947 BMPR2 Agonists: BMP (2, 4, 6, 7, 10) Dibotermin alfa Eptotermin alfa GDF (2 (BMP9), 5 (BMP14), 6 (BMP13), 7 (BMP12)) Radotermin Antagonists: Inhibin (A, B) ACVR2A (ACVR2) Agonists: Activin (A, B, AB) BMP (2, 4, 5, 6, 7, 8A, 8B, 15 (GDF9B)) Dibotermin alfa Eptotermin alfa GDF (1, 3, 5 (BMP14), 6 (BMP13), 7 (BMP12), 9, 11 (BMP11), 15) Myostatin (GDF8) Nodal Radotermin Antagonists: Inhibin (A, B) Lefty (1, 2) Decoy receptors: Sotatercept ACVR2B Agonists: Activin (A, B, AB) BMP (2, 4, 6, 7) Dibotermin alfa Eptotermin alfa GDF (1, 3, 5 (BMP14), 6 (BMP13), 7 (BMP12)) Myostatin (GDF8) Nodal Osteogenin (BMP3, BMP3A) Radotermin Antagonists: Inhibin (A, B) Lefty (1, 2) Decoy receptors: Ramatercept AMHR2 (AMHR) Agonists: AMH (MIS) Type III TGFβR3 (β-glycan) Ligands: Avotermin Inhibin (A, B) TGFβ (1, 2, 3) Unsorted Endogenous antagonists/inhibitors: BAMBI Cerberus (CER1) Chordin DAN (PARN) Decorin Follistatin Gremlin (Drm) LTBP1 Noggin TGIF Thrombospondin 1 (THBS1) Tomoregulin 1 Antibodies: Stamulumab (against myostatin) TRC105 (against endoglin) Others: Endoglin See also Receptor/signaling modulators Signaling peptide/protein receptor modulators Growth factor receptor modulators Cytokine receptor modulators Retrieved from "" Categories: Genes on human chromosome 2Genes on human chromosome 7Genes on human chromosome 12SWL/mutations associated toMammal reproductive systemHormones of the ovaryPeptide hormonesTGFβ domainHuman female endocrine systemHidden categories: All articles with dead external linksArticles with dead external links from June 2017Articles with permanently dead external linksProtein pages needing a pictureSWLUse dmy dates from April 2017

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Hydrogen PeroxideINHAINHAEntrezHuman Genome OrganisationOMIMNational Center For Biotechnology InformationSwiss-ProtLocus (genetics)Chromosome 2 (human)INHBAINHBAEntrezHuman Genome OrganisationOMIMNational Center For Biotechnology InformationSwiss-ProtLocus (genetics)Chromosome 7 (human)INHBBINHBBEntrezHuman Genome OrganisationOMIMNational Center For Biotechnology InformationSwiss-ProtLocus (genetics)Chromosome 2 (human)INHBCINHBCEntrezHuman Genome OrganisationOMIMNational Center For Biotechnology InformationSwiss-ProtLocus (genetics)Chromosome 12 (human)EntrezHuman Genome OrganisationOMIMNational Center For Biotechnology InformationSwiss-ProtLocus (genetics)Chromosome 12 (human)ProteinMultiprotein ComplexFollicle-stimulating HormoneBiosynthesisSecretionMenstrual CycleCellular DifferentiationApoptosisMetabolismHomeostasisImmune SystemWound HealingEndocrine SystemNeena SchwartzCornelia ChanningProtein DimerAnti-Müllerian HormoneBone Morphogenetic ProteinGrowth Differentiation FactorTGF BetaTransforming Growth Factor Beta SuperfamilyDisulfide BondINHAINHBAINHBBEnlargeHomology (biology)African Clawed FrogINHBCGonadPituitary GlandPlacentaOvarian FollicleAromaticityAndrogenLuteinizing HormoneOvaryTesticleSpermatogenesisSkinEpidermis (skin)Genetically Modified OrganismMouseScarMorphogenesisKeratinocyteStromal CellMorphogenesisProstateLungKidneyType-I CollagenFibroblastStem CellCellular DifferentiationOrganoidFollicle-stimulating HormoneGonadsPituitary GlandPlacentaCorpus LuteumGranulosa CellOvaryMenstrual CycleOvulationMenstrual CycleGonadotropin-releasing HormoneInsulin-like Growth FactorSertoli CellSeminiferous TubulesTestesAndrogensProteinSpermatogenesisTransmembrane ReceptorSerine/threonine-specific Protein KinaseActivin Type 1 ReceptorsACVR1ACVR1BACVR1CActivin Type 2 ReceptorsACVR2AACVR2BMothers Against Decapentaplegic Homolog 2Mothers Against Decapentaplegic Homolog 3R-SMADMothers Against Decapentaplegic Homolog 4Transcription FactorAdipose TissueAdipocyteProgenitor CellCellular DifferentiationCytokineMacrophageMutationACVR1Fibrodysplasia Ossificans ProgressivaOsteogenesisRegeneronAntibodyActivin AAnimal ModelGliomaJournal Of Translational MedicineBiomarkerChronic Fatigue SyndromeQuad ScreenBeta-hCGAlpha-fetoproteinEstriolDown SyndromeOvarian CancerSpermatogenesisMale InfertilityAzoospermiaTesticular Sperm ExtractionDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierPubMed IdentifierBioscientificaDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierWikipedia:Link RotDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierInternational Standard Book NumberSpecial:BookSources/978-0-07-177636-3Digital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDiabetes (journal)Digital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed CentralPubMed IdentifierDigital Object IdentifierInternational Standard Serial NumberPubMed CentralPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierDigital Object IdentifierPubMed IdentifierMedical Subject HeadingsMedical Subject HeadingsTemplate:TGF Beta SignalingTemplate Talk:TGF Beta SignalingCell SignalingTGFβ Signaling PathwayTransforming Growth Factor Beta SuperfamilyTransforming Growth Factor BetaTGF Beta 1TGF Beta 2TGF Beta 3Bone Morphogenetic ProteinBone Morphogenetic Protein 2Bone Morphogenetic Protein 3Bone Morphogenetic Protein 4Bone Morphogenetic Protein 5Bone Morphogenetic Protein 6Bone Morphogenetic Protein 7Bone Morphogenetic Protein 8ABone Morphogenetic Protein 8bBone Morphogenetic Protein 10Bone Morphogenetic Protein 15Growth Differentiation FactorGDF1GDF2GDF3GDF5GDF6GDF7MyostatinGrowth Differentiation Factor-9GDF10GDF11GDF15Anti-Müllerian HormoneNODALTGF Beta ReceptorsActivin ReceptorBone Morphogenetic Protein ReceptorsActivin Type 1 ReceptorsACVR1ACVR1BACVR1CACVRL1Bone Morphogenetic Protein Receptor, Type 1BMPR1ABMPR1BActivin Type 2 ReceptorsACVR2AACVR2BAnti-Müllerian Hormone ReceptorBMPR2BetaglycanSignal TransductionSMAD (protein)R-SMADMothers Against Decapentaplegic Homolog 1Mothers Against Decapentaplegic Homolog 2Mothers Against Decapentaplegic Homolog 3Mothers Against Decapentaplegic Homolog 5Mothers Against Decapentaplegic Homolog 9I-SMADMothers Against Decapentaplegic Homolog 6Mothers Against Decapentaplegic Homolog 7Mothers Against Decapentaplegic Homolog 4TGF Beta Signaling PathwayCerberus (protein)ChordinDecorinFollistatinGremlin (protein)Lefty (protein)Latent TGF-beta Binding ProteinNoggin (protein)Poly(A)-specific RibonucleaseThrombospondin 1Co-receptorBAMBICriptoZinc Finger FYVE Domain-containing Protein 9Template:GlycoproteinsTemplate Talk:GlycoproteinsProteinGlycoconjugateGlycoproteinGlycopeptideMucoproteinMucinCD43CD164MUC1MUC2MUC3AMUC3BMUC4MUC5ACMUC5BMUC6MUC7MUC8MucinMUC13MUC15CA-125MUC17MUC19MUC20HaptoglobinIntrinsic FactorOrosomucoidPeptidoglycanPhytohaemagglutininOvomucinProteoglycanChondroitin SulfateDermatan SulfateDecorinBiglycanVersicanHeparan SulfateChondroitin SulfateTesticanPerlecanChondroitin SulfateChondroitin Sulfate ProteoglycanAggrecanNeurocanBrevicanCD44CSPG4CSPG5Platelet Factor 4SMC3 (gene)Keratan SulfateFibromodulinLumicanKeratocanHeparan SulfateSyndecan 1A Disintegrin And MetalloproteinaseAlpha 1-antichymotrypsinApolipoprotein HCD70AsialoglycoproteinAvidinB-cell Activating Factor4-1BB LigandCholesterylester Transfer ProteinClusterinColony-stimulating FactorHemopexinLactoferrinMembrane GlycoproteinsMyelin Protein ZeroOsteonectinProtein CProtein SSerum Amyloid P ComponentSialoglycoproteinCD43GlycophorinGlycophorin CThrombopoietinThyroglobulinThyroxine-binding ProteinsTranscortinTumor Necrosis Factor AlphaUteroglobinVitronectinTemplate:HormonesTemplate Talk:HormonesHormoneEndocrine GlandHypothalamic-pituitary HormoneHypothalamusGonadotropin-releasing HormoneThyrotropin-releasing HormoneDopamineCorticotropin-releasing HormoneGrowth Hormone Releasing HormoneSomatostatinMelanin Concentrating HormonePosterior PituitaryOxytocinVasopressinAnterior PituitaryFollicle-stimulating HormoneLuteinizing HormoneThyroid-stimulating HormoneProlactinProopiomelanocortinCorticotropin-like Intermediate PeptideAdrenocorticotropic HormoneMelanocyte-stimulating HormoneEndorphinsLipotropinGrowth HormoneHypothalamic–pituitary–adrenal AxisAdrenal GlandAldosteroneCortisolCortisoneDehydroepiandrosteroneDehydroepiandrosterone SulfateAndrostenedioneAdrenal GlandEpinephrineNorepinephrineThyroidThyroid HormoneTriiodothyronineThyroxineCalcitoninHypothalamic–pituitary–thyroid AxisParathyroid GlandParathyroid HormoneHypothalamic–pituitary–gonadal AxisTesticleTestosteroneAnti-Müllerian HormoneOvaryEstradiolProgesteroneRelaxinPlacentaHuman Chorionic GonadotropinHuman Placental LactogenEstrogenProgesteronePancreasGlucagonInsulinAmylinSomatostatinPancreatic PolypeptidePineal GlandMelatoninN,N-dimethyltryptamine5-methoxy-N,N-dimethyltryptamineThymusThymosinsThymosin α1Beta ThymosinsThymopoietinThymulinDigestionStomachGastrinGhrelinDuodenumCholecystokininIncretinsGastric Inhibitory PolypeptideGlucagon-like Peptide-1SecretinMotilinVasoactive Intestinal PeptideIleumEnteroglucagonPeptide YYLiverInsulin-like Growth FactorInsulin-like Growth Factor 1Insulin-like Growth Factor 2Adipose TissueLeptinAdiponectinResistinHuman SkeletonOsteocalcinKidneyReninErythropoietinCalcitriolProstaglandinHeartNatriuretic PeptideAtrial Natriuretic PeptideBrain Natriuretic PeptideTemplate:TGFβ Receptor Superfamily ModulatorsTemplate Talk:TGFβ Receptor Superfamily ModulatorsTGFβ Receptor SuperfamilyReceptor ModulatorTGFβ Superfamily ReceptorALK1ActivinActivin AActivin BActivin ABAvoterminBone Morphogenetic ProteinBMP10Growth Differentiation FactorGDF2Transforming Growth Factor BetaTGF Beta 1TGF Beta 2TGF Beta 3AscrinvacumabDalanterceptALK2ActivinActivin AActivin BActivin ABAnti-Müllerian HormoneAvoterminBone Morphogenetic ProteinBMP5BMP6BMP7BMP8ABMP8BEptotermin AlfaTransforming Growth Factor BetaTGF Beta 1TGF Beta 2TGF Beta 3ALK3Anti-Müllerian HormoneBone Morphogenetic ProteinBone Morphogenetic Protein 2BMP4BMP5BMP6BMP7BMP8ABMP8BDibotermin AlfaEptotermin AlfaALK4ActivinActivin AActivin BActivin ABGrowth Differentiation FactorGDF1GDF3GDF11MyostatinNODALInhibinInhibin AInhibin BLefty (protein)LEFTY2SB-431542ALK5AvoterminGrowth Differentiation FactorGDF10GDF11Transforming Growth Factor BetaTGF Beta 1TGF Beta 2TGF Beta 3FresolimumabLerdelimumabMetelimumabGalunisertibSB-431542ALK6Bone Morphogenetic ProteinBone Morphogenetic Protein 2BMP4BMP5BMP6BMP7BMP8ABMP8BBMP15Dibotermin AlfaEptotermin AlfaGrowth Differentiation FactorGDF5GDF6GDF7GDF9GDF15ALK7Growth Differentiation FactorGDF1GDF3GDF11NODALLefty (protein)LEFTY2SB-431542TGFβ Superfamily ReceptorTGFβR2AvoterminGrowth Differentiation FactorGDF10Transforming Growth Factor BetaTGF Beta 1TGF Beta 2TGF Beta 3FresolimumabLerdelimumabMetelimumabBMPR2Bone Morphogenetic ProteinBone Morphogenetic Protein 2BMP4BMP6BMP7BMP10Dibotermin AlfaEptotermin AlfaGrowth Differentiation FactorGDF2GDF5GDF6GDF7InhibinInhibin AInhibin BACVR2AActivinActivin AActivin BActivin ABBone Morphogenetic ProteinBone Morphogenetic Protein 2BMP4BMP5BMP6BMP7BMP8ABMP8BBMP15Dibotermin AlfaEptotermin AlfaGrowth Differentiation FactorGDF1GDF3GDF5GDF6GDF7GDF9GDF11GDF15MyostatinNODALInhibinInhibin AInhibin BLefty (protein)LEFTY2ACVR2AActivinActivin AActivin BActivin ABBone Morphogenetic ProteinBone Morphogenetic Protein 2BMP4BMP6BMP7Dibotermin AlfaEptotermin AlfaGrowth Differentiation FactorGDF1GDF3GDF5GDF6GDF7MyostatinNODALBone Morphogenetic Protein 3InhibinInhibin AInhibin BLefty (protein)LEFTY2AMHR2Anti-Müllerian HormoneTGFβ Superfamily ReceptorTGFβR3AvoterminInhibinInhibin AInhibin BTransforming Growth Factor BetaTGF Beta 1TGF Beta 2TGF Beta 3BAMBICerberus (protein)ChordinDAN (protein)DecorinFollistatinGremlin (protein)LTBP1 (gene)Noggin (protein)Transforming Growth Interacting FactorThrombospondin 1StamulumabTRC105EndoglinTemplate:Receptor ModulatorsTemplate:Signaling Peptide/protein Receptor ModulatorsTemplate:Growth Factor Receptor ModulatorsTemplate:Cytokine Receptor ModulatorsHelp:CategoryCategory:Genes On Human Chromosome 2Category:Genes On Human Chromosome 7Category:Genes On Human Chromosome 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