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Transforming growth factor, beta 3

From Wikipedia, the free encyclopedia
(Redirected fromAvotermin)
Protein-coding gene in the species Homo sapiens
TGFB3
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

1KTZ,1TGJ,1TGK,2PJY,3EO1,4UM9

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
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for TGFB3
Genomic location for TGFB3
Band14q24.3Start75,958,097bp[1]
End75,983,011bp[1]
Gene location (Mouse)
Chromosome 12 (mouse)
Chr.Chromosome 12 (mouse)[2]
Chromosome 12 (mouse)
Genomic location for TGFB3
Genomic location for TGFB3
Band12 D2|12 40.09 cMStart86,103,519bp[2]
End86,125,815bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
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
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
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 aprotein that in humans is encoded by theTGFB3gene.[5][6]

It is a type of protein, known as acytokine, which is involved incell differentiation,embryogenesis anddevelopment. It belongs to a large family of cytokines called theTransforming growth factor beta superfamily, which includes theTGF-β family,Bone morphogenetic proteins (BMPs),growth and differentiation factors (GDFs),inhibins andactivins.[7]

TGF-β3 is believed to regulate molecules involved incellular adhesion andextracellular matrix (ECM) formation during the process ofpalate development. Without TGF-β3, mammals develop a deformity known as acleft palate.[8][9] This is caused by failure ofepithelial cells in both sides of the developing palate to fuse. TGF-β3 also plays an essential role in controlling the development oflungs in mammals, by also regulating cell adhesion and ECM formation in this tissue,[10] and controls wound healing by regulating the movements ofepidermal anddermal cells in injured skin.[5]

Interactions

[edit]

Transforming growth factor, beta 3 has been shown tointeract withTGF beta receptor 2.[11][12][13][14]

Clinical research

[edit]

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

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000119699Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000021253Ensembl, 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. ^abBandyopadhyay 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.doi:10.1242/dev.126.17.3869.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.S2CID 22365206.
  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.S2CID 13322593.
  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.S2CID 35671002.
  16. ^Renovo shares plummet 75% as scar revision product Juvista fails to meet study endpoints, 14 February 2011

Further reading

[edit]

External links

[edit]
PDB gallery
  • 1ktz: Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex with TGF-beta3
    1ktz: Crystal Structure of the Human TGF-beta Type II Receptor Extracellular Domain in Complex with TGF-beta3
  • 1tgj: HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE
    1tgj: HUMAN TRANSFORMING GROWTH FACTOR-BETA 3, CRYSTALLIZED FROM DIOXANE
  • 1tgk: HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000
    1tgk: HUMAN TRANSFORMING GROWTH FACTOR BETA 3, CRYSTALLIZED FROM PEG 4000
TGF beta superfamily of ligands
Ligand ofACVR orTGFBR
Ligand ofBMPR
TGF beta receptors
(Activin,BMP,family)
TGFBR1:
TGFBR2:
TGFBR3:
Transducers/SMAD
Ligand inhibitors
Coreceptors
Other
Fibroblast
FGF receptor ligands:
KGF
FGF homologous factors:
hormone-like:FGF15/19
EGF-like domain
TGFβ pathway
Insulin/IGF/
Relaxin family
Insulin andInsulin-like growth factor
Relaxin family peptide hormones
Platelet-derived
Vascular endothelial
Other
Type I
ALK1 (ACVRL1)
ALK2 (ACVR1A)
ALK3 (BMPR1A)
ALK4 (ACVR1B)
ALK5 (TGFβR1)
ALK6 (BMPR1B)
ALK7 (ACVR1C)
Type II
TGFβR2
BMPR2
ACVR2A (ACVR2)
ACVR2B
AMHR2 (AMHR)
Type III
TGFβR3 (β-glycan)
Unsorted
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