Transforming growth factor, beta 3: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Transforming growth factor beta-3''' is a [[protein]] that in humans is encoded by the ''TGFB3'' [[gene]].<ref name="pmid16549496">{{cite journal | vauthors = Bandyopadhyay B, Fan J, Guan S, Li Y, Chen M, Woodley DT, Li W | title = A "traffic control" role for TGFbeta3: orchestrating dermal and epidermal cell motility during wound healing | journal = The Journal of Cell Biology | volume = 172 | issue = 7 | pages = 1093–105 | date = Mar 2006 | pmid = 16549496 | pmc = 2063766 | doi = 10.1083/jcb.200507111 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TGFB3 transforming growth factor, beta 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7043| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
It is a type of protein, known as a [[cytokine]], which is involved in [[cell differentiation]], [[embryogenesis]] and [[developmental biology|development]]. It belongs to a large family of cytokines called the [[Transforming growth factor beta superfamily]], which includes the [[TGF beta|TGF-β family]], [[Bone morphogenetic protein]]s (BMPs), [[growth and differentiation factor]]s (GDFs), [[inhibins]] and [[activin]]s.<ref name = herpin>{{cite journal | vauthors = Herpin A, Lelong C, Favrel P | title = Transforming growth factor-beta-related proteins: an ancestral and widespread superfamily of cytokines in metazoans | journal = Developmental and Comparative Immunology | volume = 28 | issue = 5 | pages = 461–85 | date = May 2004 | pmid = 15062644 | doi = 10.1016/j.dci.2003.09.007 }}</ref>
{{GNF_Protein_box
| image = PBB_Protein_TGFB3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ktz.
| PDB = {{PDB2|1ktz}}, {{PDB2|1tgj}}, {{PDB2|1tgk}}
| Name = Transforming growth factor, beta 3
| HGNCid = 11769
| Symbol = TGFB3
| AltSymbols =; ARVD; FLJ16571; TGF-beta3
| OMIM = 190230
| ECnumber = 
| Homologene = 2433
| MGIid = 98727
| GeneAtlas_image1 = PBB_GE_TGFB3_209747_at_tn.png
| Function = {{GNF_GO|id=GO:0005160 |text = transforming growth factor beta receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component =
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009790 |text = embryonic development}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0016049 |text = cell growth}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7043
    | Hs_Ensembl = ENSG00000119699
    | Hs_RefseqProtein = NP_003230
    | Hs_RefseqmRNA = NM_003239
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 75494195
    | Hs_GenLoc_end = 75517242
    | Hs_Uniprot = P10600
    | Mm_EntrezGene = 21809
    | Mm_Ensembl = ENSMUSG00000021253
    | Mm_RefseqmRNA = XM_994378
    | Mm_RefseqProtein = XP_999472
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 86945904
    | Mm_GenLoc_end = 86968101
    | Mm_Uniprot = Q3TRQ9
  }}
}}
'''Transforming growth factor, beta 3''', also known as '''TGFB3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TGFB3 transforming growth factor, beta 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7043| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
TGF-β3 is believed to regulate molecules involved in [[cell adhesion|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]].<ref>{{cite journal | vauthors = Taya Y, O'Kane S, Ferguson MW | title = Pathogenesis of cleft palate in TGF-beta3 knockout mice | journal = Development | volume = 126 | issue = 17 | pages = 3869–79 | date = Sep 1999 | pmid = 10433915 }}</ref><ref>{{cite journal | vauthors = Dudas M, Nagy A, Laping NJ, Moustakas A, Kaartinen V | title = Tgf-beta3-induced palatal fusion is mediated by Alk-5/Smad pathway | journal = Developmental Biology | volume = 266 | issue = 1 | pages = 96–108 | date = Feb 2004 | pmid = 14729481 | doi = 10.1016/j.ydbio.2003.10.007 }}</ref> This is caused by failure of [[epithelial cell]]s in both sides of the developing palate to fuse. TGF-β3 also plays an essential role in controlling the development of [[lung]]s in mammals, by also regulating cell adhesion and ECM formation in this tissue,<ref>{{cite journal | vauthors = Kaartinen V, Voncken JW, Shuler C, Warburton D, Bu D, Heisterkamp N, Groffen J | title = Abnormal lung development and cleft palate in mice lacking TGF-beta 3 indicates defects of epithelial-mesenchymal interaction | journal = Nature Genetics | volume = 11 | issue = 4 | pages = 415–21 | date = Dec 1995 | pmid = 7493022 | doi = 10.1038/ng1295-415 }}</ref> and controls wound healing by regulating the movements of [[Epidermis (skin)|epidermal]] and [[dermis|dermal]] cells in injured skin.<ref name="pmid16549496"/>
{{PBB_Summary
| section_title =  
| summary_text =  
}}


==References==
== Interactions ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Kalluri R, Neilson EG |title=Epithelial-mesenchymal transition and its implications for fibrosis. |journal=J. Clin. Invest. |volume=112 |issue= 12 |pages= 1776-84 |year= 2004 |pmid= 14679171 |doi= 10.1172/JCI200320530 }}
*{{cite journal  | author=Arrick BA, Lee AL, Grendell RL, Derynck R |title=Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5' untranslated region. |journal=Mol. Cell. Biol. |volume=11 |issue= 9 |pages= 4306-13 |year= 1991 |pmid= 1875922 |doi=  }}
*{{cite journal  | author=ten Dijke P, Hansen P, Iwata KK, ''et al.'' |title=Identification of another member of the transforming growth factor type beta gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 13 |pages= 4715-9 |year= 1988 |pmid= 3164476 |doi=  }}
*{{cite journal  | author=Derynck R, Lindquist PB, Lee A, ''et al.'' |title=A new type of transforming growth factor-beta, TGF-beta 3. |journal=EMBO J. |volume=7 |issue= 12 |pages= 3737-43 |year= 1989 |pmid= 3208746 |doi=  }}
*{{cite journal  | author=Barton DE, Foellmer BE, Du J, ''et al.'' |title=Chromosomal mapping of genes for transforming growth factors beta 2 and beta 3 in man and mouse: dispersion of TGF-beta gene family. |journal=Oncogene Res. |volume=3 |issue= 4 |pages= 323-31 |year= 1989 |pmid= 3226728 |doi=  }}
*{{cite journal  | author=Kaartinen V, Voncken JW, Shuler C, ''et al.'' |title=Abnormal lung development and cleft palate in mice lacking TGF-beta 3 indicates defects of epithelial-mesenchymal interaction. |journal=Nat. Genet. |volume=11 |issue= 4 |pages= 415-21 |year= 1996 |pmid= 7493022 |doi= 10.1038/ng1295-415 }}
*{{cite journal  | author=Nishida K, Sotozono C, Adachi W, ''et al.'' |title=Transforming growth factor-beta 1, -beta 2 and -beta 3 mRNA expression in human cornea. |journal=Curr. Eye Res. |volume=14 |issue= 3 |pages= 235-41 |year= 1995 |pmid= 7796607 |doi=  }}
*{{cite journal  | author=Lin HY, Moustakas A, Knaus P, ''et al.'' |title=The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands. |journal=J. Biol. Chem. |volume=270 |issue= 6 |pages= 2747-54 |year= 1995 |pmid= 7852346 |doi=  }}
*{{cite journal  | author=Rampazzo A, Nava A, Danieli GA, ''et al.'' |title=The gene for arrhythmogenic right ventricular cardiomyopathy maps to chromosome 14q23-q24. |journal=Hum. Mol. Genet. |volume=3 |issue= 6 |pages= 959-62 |year= 1994 |pmid= 7951245 |doi=  }}
*{{cite journal  | author=Zhao Y, Chegini N, Flanders KC |title=Human fallopian tube expresses transforming growth factor (TGF beta) isoforms, TGF beta type I-III receptor messenger ribonucleic acid and protein, and contains [125I]TGF beta-binding sites. |journal=J. Clin. Endocrinol. Metab. |volume=79 |issue= 4 |pages= 1177-84 |year= 1994 |pmid= 7962292 |doi=  }}
*{{cite journal  | author=Hildebrand A, Romarís M, Rasmussen LM, ''et al.'' |title=Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. |journal=Biochem. J. |volume=302 ( Pt 2) |issue=  |pages= 527-34 |year= 1994 |pmid= 8093006 |doi=  }}
*{{cite journal  | author=López-Casillas F, Payne HM, Andres JL, Massagué J |title=Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites. |journal=J. Cell Biol. |volume=124 |issue= 4 |pages= 557-68 |year= 1994 |pmid= 8106553 |doi=  }}
*{{cite journal  | author=Mittl PR, Priestle JP, Cox DA, ''et al.'' |title=The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding. |journal=Protein Sci. |volume=5 |issue= 7 |pages= 1261-71 |year= 1997 |pmid= 8819159 |doi=  }}
*{{cite journal  | author=Ambros RA, Kallakury BV, Malfetano JH, Mihm MC |title=Cytokine, cell adhesion receptor, and tumor suppressor gene expression in vulvar squamous carcinoma: correlation with prominent fibromyxoid stromal response. |journal=Int. J. Gynecol. Pathol. |volume=15 |issue= 4 |pages= 320-5 |year= 1997 |pmid= 8886879 |doi=  }}
*{{cite journal  | author=Djonov V, Ball RK, Graf S, ''et al.'' |title=Transforming growth factor-beta 3 is expressed in nondividing basal epithelial cells in normal human prostate and benign prostatic hyperplasia, and is no longer detectable in prostate carcinoma. |journal=Prostate |volume=31 |issue= 2 |pages= 103-9 |year= 1997 |pmid= 9140123 |doi=  }}
*{{cite journal  | author=Jin L, Qian X, Kulig E, ''et al.'' |title=Transforming growth factor-beta, transforming growth factor-beta receptor II, and p27Kip1 expression in nontumorous and neoplastic human pituitaries. |journal=Am. J. Pathol. |volume=151 |issue= 2 |pages= 509-19 |year= 1997 |pmid= 9250163 |doi=  }}
*{{cite journal  | author=Lidral AC, Romitti PA, Basart AM, ''et al.'' |title=Association of MSX1 and TGFB3 with nonsyndromic clefting in humans. |journal=Am. J. Hum. Genet. |volume=63 |issue= 2 |pages= 557-68 |year= 1998 |pmid= 9683588 |doi=  }}
*{{cite journal  | author=Barbara NP, Wrana JL, Letarte M |title=Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 584-94 |year= 1999 |pmid= 9872992 |doi=  }}
*{{cite journal  | author=Lux A, Attisano L, Marchuk DA |title=Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 9984-92 |year= 1999 |pmid= 10187774 |doi=  }}
*{{cite journal  | author=Mori T, Kawara S, Shinozaki M, ''et al.'' |title=Role and interaction of connective tissue growth factor with transforming growth factor-beta in persistent fibrosis: A mouse fibrosis model. |journal=J. Cell. Physiol. |volume=181 |issue= 1 |pages= 153-9 |year= 1999 |pmid= 10457363 |doi= 10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K }}
}}
{{refend}}


{{protein-stub}}
Transforming growth factor, beta 3 has been shown to [[Protein-protein interaction|interact]] with [[TGF beta receptor 2]].<ref name=pmid12729750>{{cite journal | vauthors = De Crescenzo G, Pham PL, Durocher Y, O'Connor-McCourt MD | title = 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 = Journal of Molecular Biology | volume = 328 | issue = 5 | pages = 1173–83 | date = May 2003 | pmid = 12729750 | doi = 10.1016/S0022-2836(03)00360-7 }}</ref><ref name=pmid11850637>{{cite journal | vauthors = Hart PJ, Deep S, Taylor AB, Shu Z, Hinck CS, Hinck AP | title = Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex | journal = Nature Structural Biology | volume = 9 | issue = 3 | pages = 203–8 | date = Mar 2002 | pmid = 11850637 | doi = 10.1038/nsb766 }}</ref><ref name=pmid9872992>{{cite journal | vauthors = Barbara NP, Wrana JL, Letarte M | title = Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily | journal = The Journal of Biological Chemistry | volume = 274 | issue = 2 | pages = 584–94 | date = Jan 1999 | pmid = 9872992 | doi = 10.1074/jbc.274.2.584 }}</ref><ref name=pmid11157754>{{cite journal | vauthors = Rotzer D, Roth M, Lutz M, Lindemann D, Sebald W, Knaus P | title = Type III TGF-beta receptor-independent signalling of TGF-beta2 via TbetaRII-B, an alternatively spliced TGF-beta type II receptor | journal = The EMBO Journal | volume = 20 | issue = 3 | pages = 480–90 | date = Feb 2001 | pmid = 11157754 | pmc = 133482 | doi = 10.1093/emboj/20.3.480 }}</ref>
 
==Clinical research==
 
After successful phase I/II [[clinical trial|trials]],<ref>{{cite journal | vauthors = 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 | title = Prophylactic administration of avotermin for improvement of skin scarring: three double-blind, placebo-controlled, phase I/II studies | journal = Lancet | volume = 373 | issue = 9671 | pages = 1264–74 | date = Apr 2009 | pmid = 19362676 | doi = 10.1016/S0140-6736(09)60322-6 | url = http://www.thelancet.com/journals/lancet/article/PIIS0140-6736(09)60322-6/abstract}}</ref> human recombinant TGF-β3 ('''Avotermin''', planned trade name '''Juvista''') failed in Phase III trials.<ref>[http://www.thepharmaletter.com/file/102058/renovo-shares-plummet-75-as-scar-revision-product-juvista-fails-to-meet-study-endpoints.html Renovo shares plummet 75% as scar revision product Juvista fails to meet study endpoints], 14 February 2011</ref>
 
== References ==
{{Reflist}}
 
== Further reading ==
{{refbegin|35em}}
* {{cite journal | vauthors = Kalluri R, Neilson EG | title = Epithelial-mesenchymal transition and its implications for fibrosis | journal = The Journal of Clinical Investigation | volume = 112 | issue = 12 | pages = 1776–84 | date = Dec 2003 | pmid = 14679171 | pmc = 297008 | doi = 10.1172/JCI20530 }}
* {{cite journal | vauthors = Arrick BA, Lee AL, Grendell RL, Derynck R | title = Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5' untranslated region | journal = Molecular and Cellular Biology | volume = 11 | issue = 9 | pages = 4306–13 | date = Sep 1991 | pmid = 1875922 | pmc = 361291 | doi =  10.1128/mcb.11.9.4306}}
* {{cite journal | vauthors = ten Dijke P, Hansen P, Iwata KK, Pieler C, Foulkes JG | title = Identification of another member of the transforming growth factor type beta gene family | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 85 | issue = 13 | pages = 4715–9 | date = Jul 1988 | pmid = 3164476 | pmc = 280506 | doi = 10.1073/pnas.85.13.4715 }}
* {{cite journal | vauthors = Derynck R, Lindquist PB, Lee A, Wen D, Tamm J, Graycar JL, Rhee L, Mason AJ, Miller DA, Coffey RJ | title = A new type of transforming growth factor-beta, TGF-beta 3 | journal = The EMBO Journal | volume = 7 | issue = 12 | pages = 3737–43 | date = Dec 1988 | pmid = 3208746 | pmc = 454948 | doi =  }}
* {{cite journal | vauthors = Barton DE, Foellmer BE, Du J, Tamm J, Derynck R, Francke U | title = Chromosomal mapping of genes for transforming growth factors beta 2 and beta 3 in man and mouse: dispersion of TGF-beta gene family | journal = Oncogene Research | volume = 3 | issue = 4 | pages = 323–31 | year = 1989 | pmid = 3226728 | doi =  }}
* {{cite journal | vauthors = Kaartinen V, Voncken JW, Shuler C, Warburton D, Bu D, Heisterkamp N, Groffen J | title = Abnormal lung development and cleft palate in mice lacking TGF-beta 3 indicates defects of epithelial-mesenchymal interaction | journal = Nature Genetics | volume = 11 | issue = 4 | pages = 415–21 | date = Dec 1995 | pmid = 7493022 | doi = 10.1038/ng1295-415 }}
* {{cite journal | vauthors = Nishida K, Sotozono C, Adachi W, Yamamoto S, Yokoi N, Kinoshita S | title = Transforming growth factor-beta 1, -beta 2 and -beta 3 mRNA expression in human cornea | journal = Current Eye Research | volume = 14 | issue = 3 | pages = 235–41 | date = Mar 1995 | pmid = 7796607 | doi = 10.3109/02713689509033520 }}
* {{cite journal | vauthors = Lin HY, Moustakas A, Knaus P, Wells RG, Henis YI, Lodish HF | title = The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands | journal = The Journal of Biological Chemistry | volume = 270 | issue = 6 | pages = 2747–54 | date = Feb 1995 | pmid = 7852346 | doi = 10.1074/jbc.270.6.2747 }}
* {{cite journal | vauthors = Rampazzo A, Nava A, Danieli GA, Buja G, Daliento L, Fasoli G, Scognamiglio R, Corrado D, Thiene G | title = The gene for arrhythmogenic right ventricular cardiomyopathy maps to chromosome 14q23-q24 | journal = Human Molecular Genetics | volume = 3 | issue = 6 | pages = 959–62 | date = Jun 1994 | pmid = 7951245 | doi = 10.1093/hmg/3.6.959 }}
* {{cite journal | vauthors = Zhao Y, Chegini N, Flanders KC | title = Human fallopian tube expresses transforming growth factor (TGF beta) isoforms, TGF beta type I-III receptor messenger ribonucleic acid and protein, and contains [125I]TGF beta-binding sites | journal = The Journal of Clinical Endocrinology and Metabolism | volume = 79 | issue = 4 | pages = 1177–84 | date = Oct 1994 | pmid = 7962292 | doi = 10.1210/jc.79.4.1177 }}
* {{cite journal | vauthors = Hildebrand A, Romarís M, Rasmussen LM, Heinegård D, Twardzik DR, Border WA, Ruoslahti E | title = Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta | journal = The Biochemical Journal | volume = 302 | issue = 2 | pages = 527–34 | date = Sep 1994 | pmid = 8093006 | pmc = 1137259 | doi =  10.1042/bj3020527}}
* {{cite journal | vauthors = López-Casillas F, Payne HM, Andres JL, Massagué J | title = Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites | journal = The Journal of Cell Biology | volume = 124 | issue = 4 | pages = 557–68 | date = Feb 1994 | pmid = 8106553 | pmc = 2119924 | doi = 10.1083/jcb.124.4.557 }}
* {{cite journal | vauthors = Mittl PR, Priestle JP, Cox DA, McMaster G, Cerletti N, Grütter MG | title = The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding | journal = Protein Science | volume = 5 | issue = 7 | pages = 1261–71 | date = Jul 1996 | pmid = 8819159 | pmc = 2143453 | doi = 10.1002/pro.5560050705 }}
* {{cite journal | vauthors = Ambros RA, Kallakury BV, Malfetano JH, Mihm MC | title = Cytokine, cell adhesion receptor, and tumor suppressor gene expression in vulvar squamous carcinoma: correlation with prominent fibromyxoid stromal response | journal = International Journal of Gynecological Pathology | volume = 15 | issue = 4 | pages = 320–5 | date = Oct 1996 | pmid = 8886879 | doi = 10.1097/00004347-199610000-00004 }}
* {{cite journal | vauthors = Djonov V, Ball RK, Graf S, Mottaz AE, Arnold AM, Flanders K, Studer UE, Merz VW | title = Transforming growth factor-beta 3 is expressed in nondividing basal epithelial cells in normal human prostate and benign prostatic hyperplasia, and is no longer detectable in prostate carcinoma | journal = The Prostate | volume = 31 | issue = 2 | pages = 103–9 | date = May 1997 | pmid = 9140123 | doi = 10.1002/(SICI)1097-0045(19970501)31:2<103::AID-PROS5>3.0.CO;2-O }}
* {{cite journal | vauthors = Jin L, Qian X, Kulig E, Sanno N, Scheithauer BW, Kovacs K, Young WF, Lloyd RV | title = Transforming growth factor-beta, transforming growth factor-beta receptor II, and p27Kip1 expression in nontumorous and neoplastic human pituitaries | journal = The American Journal of Pathology | volume = 151 | issue = 2 | pages = 509–19 | date = Aug 1997 | pmid = 9250163 | pmc = 1858020 | doi =  }}
* {{cite journal | vauthors = Lidral AC, Romitti PA, Basart AM, Doetschman T, Leysens NJ, Daack-Hirsch S, Semina EV, Johnson LR, Machida J, Burds A, Parnell TJ, Rubenstein JL, Murray JC | title = Association of MSX1 and TGFB3 with nonsyndromic clefting in humans | journal = American Journal of Human Genetics | volume = 63 | issue = 2 | pages = 557–68 | date = Aug 1998 | pmid = 9683588 | pmc = 1377298 | doi = 10.1086/301956 }}
* {{cite journal | vauthors = Barbara NP, Wrana JL, Letarte M | title = Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily | journal = The Journal of Biological Chemistry | volume = 274 | issue = 2 | pages = 584–94 | date = Jan 1999 | pmid = 9872992 | doi = 10.1074/jbc.274.2.584 }}
* {{cite journal | vauthors = Lux A, Attisano L, Marchuk DA | title = Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1 | journal = The Journal of Biological Chemistry | volume = 274 | issue = 15 | pages = 9984–92 | date = Apr 1999 | pmid = 10187774 | doi = 10.1074/jbc.274.15.9984 }}
* {{cite journal | vauthors = Mori T, Kawara S, Shinozaki M, Hayashi N, Kakinuma T, Igarashi A, Takigawa M, Nakanishi T, Takehara K | title = Role and interaction of connective tissue growth factor with transforming growth factor-beta in persistent fibrosis: A mouse fibrosis model | journal = Journal of Cellular Physiology | volume = 181 | issue = 1 | pages = 153–9 | date = Oct 1999 | pmid = 10457363 | doi = 10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K }}
{{Refend}}
 
== External links ==
* [https://www.ncbi.nlm.nih.gov/books/NBK1131/  GeneReviews/NCBI/NIH/UW entry on Arrhythmogenic Right Ventricular Dysplasia/Cardiomyopathy, Autosomal Dominant]
* [https://www.ncbi.nlm.nih.gov/omim/604772,605676,601214,107970,125645,125647,125671,173325,180902,190230,600996,602086,602087,602861,604400,604401,607450,609040,609160,610193,610476,611528,612048,107970,125645,125647,125671,173325,180902,190230,600996,602086,602087,602861,604400,604401,607450,609040,609160,610193,610476,611528,612048  OMIM entries on Arrhythmogenic Right Ventricular Dysplasia/Cardiomyopathy, Autosomal Dominant]
 
{{PDB Gallery|geneid=7043}}
 
{{TGF beta signaling}}
{{Growth factors}}
{{TGFβ receptor superfamily modulators}}
 
[[Category:Proteins]]
[[Category:TGFβ domain]]

Latest revision as of 04:40, 17 September 2017

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External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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View/Edit Human

Transforming growth factor beta-3 is a protein that in humans is encoded by the TGFB3 gene.[1][2]

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.[3]

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.[4][5] 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,[6] and controls wound healing by regulating the movements of epidermal and dermal cells in injured skin.[1]

Interactions

Transforming growth factor, beta 3 has been shown to interact with TGF beta receptor 2.[7][8][9][10]

Clinical research

After successful phase I/II trials,[11] human recombinant TGF-β3 (Avotermin, planned trade name Juvista) failed in Phase III trials.[12]

References

  1. ↑ 1.0 1.1 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.
  2. ↑ "Entrez Gene: TGFB3 transforming growth factor, beta 3".
  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.
  4. ↑ Taya Y, O'Kane S, Ferguson MW (Sep 1999). "Pathogenesis of cleft palate in TGF-beta3 knockout mice". Development. 126 (17): 3869–79. PMID 10433915.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 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.
  10. ↑ 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.
  11. ↑ 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.
  12. ↑ Renovo shares plummet 75% as scar revision product Juvista fails to meet study endpoints, 14 February 2011

Further reading

External links

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