Jump to content

Transforming growth factor, beta 3

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by OAbot (talk | contribs) at 21:17, 15 April 2020 (Open access bot: doi added to citation with #oabot.). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

TGFB3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTGFB3, ARVD, ARVD1, RNHF, TGF-beta3, Transforming growth factor, beta 3, LDS5, transforming growth factor beta 3, TGF beta 3
External IDsOMIM: 190230; MGI: 98727; HomoloGene: 2433; GeneCards: TGFB3; OMA:TGFB3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

7043

21809

Ensembl

ENSG00000119699

ENSMUSG00000021253

UniProt

P10600

P17125

RefSeq (mRNA)

NM_003239
NM_001329938
NM_001329939

NM_009368

RefSeq (protein)

NP_001316867
NP_001316868
NP_003230

n/a

Location (UCSC)Chr 14: 75.96 – 75.98 MbChr 12: 86.1 – 86.13 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000119699 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021253 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ "Entrez Gene: TGFB3 transforming growth factor, beta 3".
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ 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.
  11. ^ 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.
  12. ^ 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.
  13. ^ 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.
  14. ^ 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.
  15. ^ 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.
  16. ^ Renovo shares plummet 75% as scar revision product Juvista fails to meet study endpoints, 14 February 2011

Further reading

Retrieved from "https://en.wikipedia.org/w/index.php?title=Transforming_growth_factor,_beta_3&oldid=951172634"