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TGFB3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1KTZ, 1TGJ, 1TGK, 2PJY, 3EO1, 4UM9
Identifiers
Aliases	TGFB3, ARVD, ARVD1, RNHF, TGF-beta3, Transforming growth factor, beta 3, LDS5, transforming growth factor beta 3, TGF beta 3
External IDs	OMIM: 190230; MGI: 98727; HomoloGene: 2433; GeneCards: TGFB3; OMA:TGFB3 - orthologs
Gene location (Human)
Chr.	Chromosome 14 (human)
End	75,983,011 bp
Gene location (Mouse)
Chr.	Chromosome 12 (mouse)
End	86,125,815 bp
RNA expression pattern
	Top expressed in
	saphenous vein; ; canal of the cervix; ; gallbladder; ; prostate; ; cartilage tissue; ; smooth muscle tissue; ; body of pancreas; ; periodontal fiber; ; body of uterus; ; C1 segment;
	Top expressed in
	external carotid artery; ; molar; ; aortic valve; ; internal carotid artery; ; lactiferous gland; ; ascending aorta; ; ankle; ; umbilical cord; ; ankle joint; ; calvaria;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	type III transforming growth factor beta receptor binding; cytokine activity; type I transforming growth factor beta receptor binding; protein binding; protein heterodimerization activity; transforming growth factor beta receptor binding; growth factor activity; transforming growth factor beta binding; type II transforming growth factor beta receptor binding; identical protein binding;
Cellular component	cytoplasm; extracellular matrix; T-tubule; plasma membrane; secretory granule; cell surface; soma; platelet alpha granule lumen; nucleus; extracellular region; extracellular space; intracellular membrane-bounded organelle; collagen-containing extracellular matrix;
Biological process	regulation of apoptotic process; negative regulation of neuron apoptotic process; positive regulation of collagen biosynthetic process; cell-cell junction organization; regulation of MAPK cascade; SMAD protein signal transduction; positive regulation of bone mineralization; embryonic neurocranium morphogenesis; response to progesterone; female pregnancy; response to laminar fluid shear stress; ageing; platelet degranulation; in utero embryonic development; negative regulation of transforming growth factor beta receptor signaling pathway; wound healing; salivary gland morphogenesis; mammary gland development; odontogenesis; response to estrogen; positive regulation of protein secretion; ossification involved in bone remodeling; uterine wall breakdown; frontal suture morphogenesis; inner ear development; negative regulation of macrophage cytokine production; lung alveolus development; digestive tract development; transforming growth factor beta receptor signaling pathway; positive regulation of filopodium assembly; positive regulation of cell division; face morphogenesis; detection of hypoxia; positive regulation of transcription by RNA polymerase II; positive regulation of SMAD protein signal transduction; positive regulation of tight junction disassembly; positive regulation of epithelial to mesenchymal transition; positive regulation of stress fiber assembly; regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; positive regulation of apoptotic process; response to hypoxia; positive regulation of pathway-restricted SMAD protein phosphorylation; positive regulation of transcription, DNA-templated; negative regulation of vascular associated smooth muscle cell proliferation; BMP signaling pathway; cell development; regulation of signaling receptor activity; positive regulation of cell population proliferation; negative regulation of cell population proliferation; secondary palate development; regulation of cell population proliferation;
	Sources:Amigo / QuickGO
Orthologs
	7043
	21809
	ENSG00000119699
	ENSMUSG00000021253
	P10600
	P17125
	NM_003239; NM_001329938; NM_001329939
	NM_009368
	NP_001316867; NP_001316868; NP_003230
	n/a
	Wikidata
View/Edit Human	View/Edit Mouse

Transforming growth factor beta-3 is a protein that in humans is encoded by the TGFB3 gene.^[5]^[6]

It is a type of protein, known as a cytokine, which is involved in cell differentiation, embryogenesis and development. It belongs to a large family of cytokines called the Transforming growth factor beta superfamily, which includes the TGF-β family, Bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs), inhibins and activins.^[7]

TGF-β3 is believed to regulate molecules involved in cellular adhesion and extracellular matrix (ECM) formation during the process of palate development. Without TGF-β3, mammals develop a deformity known as a cleft palate.^[8]^[9] This is caused by failure of epithelial cells in both sides of the developing palate to fuse. TGF-β3 also plays an essential role in controlling the development of lungs in mammals, by also regulating cell adhesion and ECM formation in this tissue,^[10] and controls wound healing by regulating the movements of epidermal and dermal cells in injured skin.^[5]

Interactions

Transforming growth factor, beta 3 has been shown to interact with TGF beta receptor 2.^[11]^[12]^[13]^[14]

Clinical research

After successful phase I/II trials,^[15] human recombinant TGF-β3 (avotermin, planned trade name Juvista) failed in Phase III trials.^[16]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000119699 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021253 – 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.
^ ^a ^b Bandyopadhyay B, Fan J, Guan S, Li Y, Chen M, Woodley DT, Li W (Mar 2006). "A "traffic control" role for TGFbeta3: orchestrating dermal and epidermal cell motility during wound healing". The Journal of Cell Biology. 172 (7): 1093–105. doi:10.1083/jcb.200507111. PMC 2063766. PMID 16549496.
^ "Entrez Gene: TGFB3 transforming growth factor, beta 3".
^ Herpin A, Lelong C, Favrel P (May 2004). "Transforming growth factor-beta-related proteins: an ancestral and widespread superfamily of cytokines in metazoans". Developmental and Comparative Immunology. 28 (5): 461–85. doi:10.1016/j.dci.2003.09.007. PMID 15062644.
^ Taya Y, O'Kane S, Ferguson MW (Sep 1999). "Pathogenesis of cleft palate in TGF-beta3 knockout mice". Development. 126 (17): 3869–79. doi:10.1242/dev.126.17.3869. PMID 10433915.
^ Dudas M, Nagy A, Laping NJ, Moustakas A, Kaartinen V (Feb 2004). "Tgf-beta3-induced palatal fusion is mediated by Alk-5/Smad pathway". Developmental Biology. 266 (1): 96–108. doi:10.1016/j.ydbio.2003.10.007. PMID 14729481.
^ Kaartinen V, Voncken JW, Shuler C, Warburton D, Bu D, Heisterkamp N, Groffen J (Dec 1995). "Abnormal lung development and cleft palate in mice lacking TGF-beta 3 indicates defects of epithelial-mesenchymal interaction". Nature Genetics. 11 (4): 415–21. doi:10.1038/ng1295-415. PMID 7493022. S2CID 22365206.
^ De Crescenzo G, Pham PL, Durocher Y, O'Connor-McCourt MD (May 2003). "Transforming growth factor-beta (TGF-beta) binding to the extracellular domain of the type II TGF-beta receptor: receptor capture on a biosensor surface using a new coiled-coil capture system demonstrates that avidity contributes significantly to high affinity binding". Journal of Molecular Biology. 328 (5): 1173–83. doi:10.1016/S0022-2836(03)00360-7. PMID 12729750.
^ Hart PJ, Deep S, Taylor AB, Shu Z, Hinck CS, Hinck AP (Mar 2002). "Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex". Nature Structural Biology. 9 (3): 203–8. doi:10.1038/nsb766. PMID 11850637. S2CID 13322593.
^ Barbara NP, Wrana JL, Letarte M (Jan 1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily". The Journal of Biological Chemistry. 274 (2): 584–94. doi:10.1074/jbc.274.2.584. PMID 9872992.
^ Rotzer D, Roth M, Lutz M, Lindemann D, Sebald W, Knaus P (Feb 2001). "Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor". The EMBO Journal. 20 (3): 480–90. doi:10.1093/emboj/20.3.480. PMC 133482. PMID 11157754.
^ Ferguson MW, Duncan J, Bond J, Bush J, Durani P, So K, Taylor L, Chantrey J, Mason T, James G, Laverty H, Occleston NL, Sattar A, Ludlow A, O'Kane S (Apr 2009). "Prophylactic administration of avotermin for improvement of skin scarring: three double-blind, placebo-controlled, phase I/II studies". Lancet. 373 (9671): 1264–74. doi:10.1016/S0140-6736(09)60322-6. PMID 19362676. S2CID 35671002.
^ Renovo shares plummet 75% as scar revision product Juvista fails to meet study endpoints, 14 February 2011