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TGF beta 1

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

TGFB1

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
1KLA,1KLC,1KLD,3KFD,4KV5

Identifiers

Aliases

TGFB1, CED, DPD1, LAP, TGFB, TGFbeta, transforming growth factor beta 1, IBDIMDE, TGF-beta1

External IDs

OMIM:190180;MGI:98725;HomoloGene:540;GeneCards:TGFB1;OMA:TGFB1 - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19q13.2	Start	41,301,587bp^[1]
Band	19q13.2	End	41,353,922bp^[1]

Gene location (Mouse)

Chr.	Chromosome 7 (mouse)^[2]

Band	7 A3\|7 13.98 cM	Start	25,386,427bp^[2]
Band	7 A3\|7 13.98 cM	End	25,404,502bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

granulocyte

monocyte

stromal cell of endometrium

ascending aorta

Descending thoracic aorta

right coronary artery

spleen

right lung

canal of the cervix

blood

Top expressed in

molar

tibiofemoral joint

stroma of bone marrow

granulocyte

calvaria

mesenteric lymph nodes

spleen

lower jaw

thymus

body of femur

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	type II transforming growth factor beta receptor binding protein N-terminus binding cytokine activity enzyme binding growth factor activity antigen binding type I transforming growth factor beta receptor binding protein homodimerization activity protein serine/threonine kinase activator activity protein binding protein heterodimerization activity type III transforming growth factor beta receptor binding transforming growth factor beta receptor binding identical protein binding
Cellular component	cytoplasm extracellular region nucleus microvillus cell surface blood microparticle plasma membrane secretory granule axon soma Golgi lumen platelet alpha granule lumen extracellular matrix extracellular space
Biological process	positive regulation of histone deacetylation positive regulation of transcription regulatory region DNA binding ureteric bud development tolerance induction to self antigen positive regulation of protein phosphorylation endoderm development response to cholesterol positive regulation of MAP kinase activity regulation of sodium ion transport response to progesterone negative regulation of cell cycle response to organic substance mammary gland development T cell homeostasis negative regulation of ossification negative regulation of hyaluronan biosynthetic process protein phosphorylation T cell differentiation positive regulation of vascular permeability animal organ regeneration positive regulation of blood vessel endothelial cell migration negative regulation of epithelial cell proliferation regulation of binding inner ear development myelination negative regulation of macrophage cytokine production cell population proliferation transforming growth factor beta receptor signaling pathway face morphogenesis negative regulation of cell population proliferation positive regulation of receptor clustering regulation of apoptotic process positive regulation of collagen biosynthetic process cellular response to transforming growth factor beta stimulus pathway-restricted SMAD protein phosphorylation regulation of DNA binding regulation of actin cytoskeleton reorganization negative regulation of fat cell differentiation positive regulation of protein metabolic process cell-cell junction organization negative regulation of myoblast differentiation positive regulation of protein kinase B signaling common-partner SMAD protein phosphorylation positive regulation of branching involved in ureteric bud morphogenesis SMAD protein signal transduction epidermal growth factor receptor signaling pathway macrophage derived foam cell differentiation negative regulation of blood vessel endothelial cell migration positive regulation of protein dephosphorylation extrinsic apoptotic signaling pathway negative regulation of extracellular matrix disassembly mitotic cell cycle checkpoint signaling positive regulation of fibroblast proliferation negative regulation of cell differentiation regulation of branching involved in mammary gland duct morphogenesis positive regulation of exit from mitosis negative regulation of transforming growth factor beta receptor signaling pathway negative regulation of gene expression morphogenesis of a branching structure regulation of SMAD protein signal transduction positive regulation of peptidyl-serine phosphorylation cell activation negative regulation of neuroblast proliferation positive regulation of transcription, DNA-templated cell growth negative regulation of T cell proliferation response to wounding negative regulation of cell growth positive regulation of chemotaxis protein export from nucleus regulation of protein import into nucleus positive regulation of peptidyl-tyrosine phosphorylation positive regulation of protein import into nucleus positive regulation of cardiac muscle cell differentiation oligodendrocyte development positive regulation of interleukin-17 production inflammatory response negative regulation of interleukin-17 production lymph node development T cell activation Notch signaling pathway negative regulation of protein phosphorylation regulation of blood vessel remodeling SMAD protein complex assembly regulation of striated muscle tissue development response to vitamin D chondrocyte differentiation regulatory T cell differentiation regulation of cartilage development branch elongation involved in mammary gland duct branching positive regulation of bone mineralization positive regulation of epithelial cell proliferation female pregnancy cellular response to organic cyclic compound positive regulation of extracellular matrix assembly cellular calcium ion homeostasis wound healing negative regulation of transcription by RNA polymerase II response to glucose positive regulation of epithelial to mesenchymal transition cellular response to dexamethasone stimulus negative regulation of production of miRNAs involved in gene silencing by miRNA mitigation of host defenses by virus lens fiber cell differentiation positive regulation of NF-kappaB transcription factor activity extracellular matrix assembly ATP biosynthetic process hematopoietic progenitor cell differentiation regulation of interleukin-23 production positive regulation of protein secretion frontal suture morphogenesis epithelial to mesenchymal transition phosphate-containing compound metabolic process regulation of gene expression adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains negative regulation of release of sequestered calcium ion into cytosol response to radiation mononuclear cell proliferation negative regulation of transcription, DNA-templated negative regulation of T cell activation positive regulation of odontogenesis lipopolysaccharide-mediated signaling pathway positive regulation of protein localization to nucleus response to estradiol regulation of cell migration response to hypoxia hyaluronan catabolic process negative regulation of phagocytosis response to organic cyclic compound positive regulation of protein-containing complex assembly protein kinase B signaling negative regulation of cell-cell adhesion negative regulation of gene silencing by miRNA positive regulation of regulatory T cell differentiation cellular response to growth factor stimulus positive regulation of pathway-restricted SMAD protein phosphorylation mammary gland branching involved in thelarche response to laminar fluid shear stress ageing regulation of regulatory T cell differentiation platelet degranulation negative regulation of DNA replication myeloid dendritic cell differentiation salivary gland morphogenesis receptor catabolic process MAPK cascade positive regulation of histone acetylation regulation of transforming growth factor beta receptor signaling pathway positive regulation of phosphatidylinositol 3-kinase activity negative regulation of protein localization to plasma membrane positive regulation of NAD+ ADP-ribosyltransferase activity negative regulation of immune response regulation of cell population proliferation negative regulation of skeletal muscle tissue development positive regulation of peptidyl-threonine phosphorylation positive regulation of smooth muscle cell differentiation positive regulation of isotype switching to IgA isotypes connective tissue replacement involved in inflammatory response wound healing ossification involved in bone remodeling positive regulation of apoptotic process positive regulation of vascular endothelial growth factor production positive regulation of superoxide anion generation digestive tract development cell migration positive regulation of fibroblast migration positive regulation of cell division germ cell migration positive regulation of transcription by RNA polymerase II negative regulation of mitotic cell cycle positive regulation of SMAD protein signal transduction positive regulation of pri-miRNA transcription by RNA polymerase II positive regulation of gene expression positive regulation of cell population proliferation liver regeneration regulation of epithelial to mesenchymal transition involved in endocardial cushion formation positive regulation of mononuclear cell migration cellular response to insulin-like growth factor stimulus positive regulation of cell migration response to immobilization stress cellular response to mechanical stimulus cellular response to ionizing radiation vasculogenesis neural tube closure heart valve morphogenesis development of the heart neural tube development membrane protein intracellular domain proteolysis leukocyte migration ventricular cardiac muscle tissue morphogenesis positive regulation of ERK1 and ERK2 cascade transforming growth factor beta receptor signaling pathway involved in heart development embryonic liver development BMP signaling pathway cell development apoptotic process regulation of pri-miRNA transcription by RNA polymerase II positive regulation of production of miRNAs involved in gene silencing by miRNA regulation of signaling receptor activity
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


7040


21803

Ensembl


ENSG00000105329


ENSMUSG00000002603

UniProt


P01137


P04202

RefSeq (mRNA)


NM_000660


NM_011577

RefSeq (protein)


NP_000651


NP_035707

Location (UCSC)

Chr 19: 41.3 – 41.35 Mb

Chr 7: 25.39 – 25.4 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Transforming growth factor beta 1 orTGF-β1 is a polypeptide member of thetransforming growth factor beta superfamily ofcytokines. It is a secreted protein that performs many cellular functions, including the control ofcell growth,cell proliferation,cell differentiation, andapoptosis. In humans, TGF-β1 is encoded by theTGFB1gene.^[5]^[6]

Function

[edit]

T cells

[edit]

SomeT cells (e.g.regulatory T cells) release TGF-β1 to inhibit the actions of other T cells. Specifically, TGF-β1 prevents theinterleukin(IL)-1- &interleukin-2-dependentproliferation in activated T cells,^[12]^[13] as well as the activation of quiescenthelper T cells andcytotoxic T cells.^[14]^[15] Similarly, TGF-β1 can inhibit the secretion and activity of many othercytokines includinginterferon-γ,tumor necrosis factor-alpha (TNF-α), and variousinterleukins. It can also decrease the expression levels of cytokine receptors, such as theIL-2 receptor to down-regulate the activity of immune cells. However, TGF-β1 can alsoincrease the expression of certain cytokines in T cells and promote their proliferation,^[16] particularly if the cells are immature.^[11]

B cells

[edit]

TGF-β1 has similar effects onB cells that also vary according to thedifferentiation state of the cell. It inhibits proliferation, stimulatesapoptosis of B cells,^[17] and controls the expression ofantibody,transferrin andMHC class II proteins on immature and mature B cells.^[11]^[17]

Myeloid cells

[edit]

The effects of TGF-β1 onmacrophages andmonocytes are predominantly suppressive; this cytokine can inhibit the proliferation of these cells and prevent their production of reactive oxygen (e.g.superoxide (O₂⁻)) and nitrogen (e.g.nitric oxide (NO)) intermediates. However, as with other cell types, TGF-β1 can also have the opposite effect on cells of myeloid origin. For example, TGF-β1 acts as achemoattractant, directing an immune response to certainpathogens. Likewise, macrophages and monocytes respond to low levels of TGF-β1 in a chemotactic manner. Furthermore, the expression of monocytic cytokines (such asinterleukin(IL)-1α, IL-1β, andTNF-α),^[15] and macrophage'sphagocytic can be increased by the action of TGF-β1.^[11]

TGF-β1 reduces the efficacy of theMHC II inastrocytes anddendritic cells, which in turn decreases the activation of appropriatehelper T cell populations.^[18]^[19]

Interactions

[edit]

TGF beta 1 has been shown tointeract with:

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000105329 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000002603 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Ghadami M, Makita Y, Yoshida K, Nishimura G, Fukushima Y, Wakui K, et al. (January 2000)."Genetic mapping of the Camurati-Engelmann disease locus to chromosome 19q13.1-q13.3".American Journal of Human Genetics.66 (1):143–147.doi:10.1086/302728.PMC 1288319.PMID 10631145.
^Vaughn SP, Broussard S, Hall CR, Scott A, Blanton SH, Milunsky JM, et al. (May 2000). "Confirmation of the mapping of the Camurati-Englemann locus to 19q13. 2 and refinement to a 3.2-cM region".Genomics.66 (1):119–121.doi:10.1006/geno.2000.6192.PMID 10843814.
^"Entrez Gene: TGFB1 transforming growth factor, beta 1".
^Assoian RK, Komoriya A, Meyers CA, Miller DM, Sporn MB (Jun 1983)."Transforming growth factor-beta in human platelets. Identification of a major storage site, purification, and characterization".Journal of Biological Chemistry.258 (11):7155–7160.doi:10.1016/S0021-9258(18)32345-7.PMID 6602130.
^Custo S, Baron B, Felice A, Seria E (5 July 2022)."A comparative profile of total protein and six angiogenically-active growth factors in three platelet products".GMS Interdisciplinary Plastic and Reconstructive Surgery DGPW.11 (Doc06): Doc06.doi:10.3205/iprs000167.PMC 9284722.PMID 35909816.
^Derynck R, Jarrett JA, Chen EY, Eaton DH, Bell JR, Assoian RK, et al. (1985)."Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells".Nature.316 (6030):701–705.Bibcode:1985Natur.316..701D.doi:10.1038/316701a0.PMID 3861940.S2CID 4245501.
^^a ^b ^c ^dLetterio JJ, Roberts AB (1998)."Regulation of immune responses by TGF-beta".Annual Review of Immunology.16:137–161.doi:10.1146/annurev.immunol.16.1.137.PMID 9597127.
^Wahl SM, Hunt DA, Wong HL, Dougherty S, McCartney-Francis N, Wahl LM, et al. (May 1988)."Transforming growth factor-beta is a potent immunosuppressive agent that inhibits IL-1-dependent lymphocyte proliferation".Journal of Immunology.140 (9). Baltimore, Md.:3026–3032.doi:10.4049/jimmunol.140.9.3026.PMID 3129508.S2CID 35425214.
^Tiemessen MM, Kunzmann S, Schmidt-Weber CB, Garssen J, Bruijnzeel-Koomen CA, Knol EF, et al. (Dec 2003)."Transforming growth factor-beta inhibits human antigen-specific CD4+ T cell proliferation without modulating the cytokine response".International Immunology.15 (12):1495–1504.doi:10.1093/intimm/dxg147.PMID 14645158.
^Gilbert KM, Thoman M, Bauche K, Pham T, Weigle WO (Jun 1997). "Transforming growth factor-beta 1 induces antigen-specific unresponsiveness in naive T cells".Immunological Investigations.26 (4):459–472.doi:10.3109/08820139709022702.PMID 9246566.
^^a ^bWahl SM, Wen J, Moutsopoulos N (Oct 2006)."TGF-beta: a mobile purveyor of immune privilege".Immunological Reviews.213:213–227.doi:10.1111/j.1600-065X.2006.00437.x.PMID 16972906.S2CID 84309271.
^Zhu H, Wang Z, Yu J, Yang X, He F, Liu Z, et al. (March 2019). "Role and mechanisms of cytokines in the secondary brain injury after intracerebral hemorrhage".Progress in Neurobiology.178 101610.doi:10.1016/j.pneurobio.2019.03.003.PMID 30923023.S2CID 85495400.
^^a ^bLebman DA, Edmiston JS (Dec 1999)."The role of TGF-beta in growth, differentiation, and maturation of B lymphocytes".Microbes and Infection.1 (15):1297–1304.doi:10.1016/S1286-4579(99)00254-3.PMID 10611758.
^Rodríguez LS, Narváez CF, Rojas OL, Franco MA, Ángel J (2012-01-01)."Human myeloid dendritic cells treated with supernatants of rotavirus infected Caco-2 cells induce a poor Th1 response".Cellular Immunology.272 (2):154–161.doi:10.1016/j.cellimm.2011.10.017.PMID 22082567.
^Dong Y, Tang L, Letterio JJ, Benveniste EN (July 2001)."The Smad3 protein is involved in TGF-beta inhibition of class II transactivator and class II MHC expression".Journal of Immunology.167 (1). Baltimore, Md.:311–319.doi:10.4049/jimmunol.167.1.311.PMID 11418665.
^Hildebrand A, Romarís M, Rasmussen LM, Heinegård D, Twardzik DR, Border WA, et al. (September 1994)."Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta".The Biochemical Journal.302 (Pt 2):527–534.doi:10.1042/bj3020527.PMC 1137259.PMID 8093006.
^Schönherr E, Broszat M, Brandan E, Bruckner P, Kresse H (July 1998). "Decorin core protein fragment Leu155-Val260 interacts with TGF-beta but does not compete for decorin binding to type I collagen".Archives of Biochemistry and Biophysics.355 (2):241–248.doi:10.1006/abbi.1998.0720.PMID 9675033.
^Takeuchi Y, Kodama Y, Matsumoto T (Dec 1994)."Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity".Journal of Biological Chemistry.269 (51):32634–32638.doi:10.1016/S0021-9258(18)31681-8.PMID 7798269.
^Choy L, Derynck R (November 1998)."The type II transforming growth factor (TGF)-beta receptor-interacting protein TRIP-1 acts as a modulator of the TGF-beta response".Journal of Biological Chemistry.273 (47):31455–31462.doi:10.1074/jbc.273.47.31455.PMID 9813058.
^Saharinen J, Keski-Oja J (August 2000)."Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta".Molecular Biology of the Cell.11 (8):2691–2704.doi:10.1091/mbc.11.8.2691.PMC 14949.PMID 10930463.
^Ebner R, Chen RH, Lawler S, Zioncheck T, Derynck R (November 1993). "Determination of type I receptor specificity by the type II receptors for TGF-beta or activin".Science.262 (5135). New York, N.Y.:900–902.Bibcode:1993Sci...262..900E.doi:10.1126/science.8235612.PMID 8235612.
^Oh SP, Seki T, Goss KA, Imamura T, Yi Y, Donahoe PK, et al. (March 2000)."Activin receptor-like kinase 1 modulates transforming growth factor-beta 1 signaling in the regulation of angiogenesis".Proceedings of the National Academy of Sciences of the United States of America.97 (6):2626–2631.Bibcode:2000PNAS...97.2626O.doi:10.1073/pnas.97.6.2626.PMC 15979.PMID 10716993.
^McGonigle S, Beall MJ, Feeney EL, Pearce EJ (February 2001). "Conserved role for 14-3-3epsilon downstream of type I TGFbeta receptors".FEBS Letters.490 (1–2):65–69.doi:10.1016/s0014-5793(01)02133-0.PMID 11172812.S2CID 84710903.

External links

[edit]

Overview of all the structural information available in thePDB forUniProt:P01137 (Transforming growth factor beta-1) at thePDBe-KB.

v t e PDB gallery
1kla: SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 1-17 OF 33 STRUCTURES 1klc: SOLUTION STRUCTURE OF TGF-B1, NMR, MINIMIZED AVERAGE STRUCTURE 1kld: SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 18-33 OF 33 STRUCTURES

Cell signaling:TGFβ signaling pathway

TGF beta superfamily of ligands

Ligand ofACVR orTGFBR	TGF beta family TGF-β1 TGF-β2 TGF-β3 Activin and inhibin INHA INHBA INHBB INHBC Nodal
Ligand ofBMPR	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 Anti-müllerian hormone

TGF beta receptors
(Activin,BMP,family)

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

Ligand inhibitors

Coreceptors

Other

SARA

Growth factors

Fibroblast

FGF receptor ligands:	FGF1/FGF2/FGF5 FGF3/FGF4/FGF6
KGF	FGF7/FGF10/FGF22 FGF8/FGF17/FGF18 FGF9/FGF16/FGF20
FGF homologous factors:	FGF11(FHF3) FGF12(FHF1) FGF13(FHF2) FGF14(FHF4)
hormone-like:FGF15/19	FGF15 FGF19 FGF21 FGF23

EGF-like domain

TGFβ pathway

TGFβ

Insulin/IGF/
Relaxin family

Insulin andInsulin-like growth factor	IGF1 IGF2
Relaxin family peptide hormones	INSL3 INSL4 INSL5 INSL6 Relaxin 1 2 3

Platelet-derived

Vascular endothelial

Other

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)