Transforming growth factor, beta 3

From Wikipedia, the free encyclopedia

PDB rendering based on 1ktz.

Available structures: 1ktz, 1tgj, 1tgk

Identifiers

Symbol(s)

TGFB3; ARVD; FLJ16571; TGF-beta3

External IDs

OMIM: 190230 MGI: 98727 HomoloGene: 2433

Gene ontology
Molecular Function:	• transforming growth factor beta receptor binding • protein binding • growth factor activity
Biological Process:	• regulation of progression through cell cycle • in utero embryonic development • signal transduction • cell-cell signaling • cell proliferation • negative regulation of cell proliferation • embryonic development • organ morphogenesis • cell growth

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003239 (mRNA)
NP_003230 (protein)

XM_994378 (mRNA)
XP_999472 (protein)

Location

Chr 14: 75.49 - 75.52 Mb

Chr 12: 86.95 - 86.97 Mb

Pubmed search

[1]

[2]

Transforming growth factor, beta 3, also known as TGFB3, is a human gene.^[1]

[edit] References

^ Entrez Gene: TGFB3 transforming growth factor, beta 3.

[edit] Further reading

Kalluri R, Neilson EG (2004). "Epithelial-mesenchymal transition and its implications for fibrosis.". J. Clin. Invest. 112 (12): 1776–84. doi:10.1172/JCI200320530. PMID 14679171.
Arrick BA, Lee AL, Grendell RL, Derynck R (1991). "Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5' untranslated region.". Mol. Cell. Biol. 11 (9): 4306–13. PMID 1875922.
ten Dijke P, Hansen P, Iwata KK, et al. (1988). "Identification of another member of the transforming growth factor type beta gene family.". Proc. Natl. Acad. Sci. U.S.A. 85 (13): 4715–9. PMID 3164476.
Derynck R, Lindquist PB, Lee A, et al. (1989). "A new type of transforming growth factor-beta, TGF-beta 3.". EMBO J. 7 (12): 3737–43. PMID 3208746.
Barton DE, Foellmer BE, Du J, et al. (1989). "Chromosomal mapping of genes for transforming growth factors beta 2 and beta 3 in man and mouse: dispersion of TGF-beta gene family.". Oncogene Res. 3 (4): 323–31. PMID 3226728.
Kaartinen V, Voncken JW, Shuler C, et al. (1996). "Abnormal lung development and cleft palate in mice lacking TGF-beta 3 indicates defects of epithelial-mesenchymal interaction.". Nat. Genet. 11 (4): 415–21. doi:10.1038/ng1295-415. PMID 7493022.
Nishida K, Sotozono C, Adachi W, et al. (1995). "Transforming growth factor-beta 1, -beta 2 and -beta 3 mRNA expression in human cornea.". Curr. Eye Res. 14 (3): 235–41. PMID 7796607.
Lin HY, Moustakas A, Knaus P, et al. (1995). "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.". J. Biol. Chem. 270 (6): 2747–54. PMID 7852346.
Rampazzo A, Nava A, Danieli GA, et al. (1994). "The gene for arrhythmogenic right ventricular cardiomyopathy maps to chromosome 14q23-q24.". Hum. Mol. Genet. 3 (6): 959–62. PMID 7951245.
Zhao Y, Chegini N, Flanders KC (1994). "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.". J. Clin. Endocrinol. Metab. 79 (4): 1177–84. PMID 7962292.
Hildebrand A, Romarís M, Rasmussen LM, et al. (1994). "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta.". Biochem. J. 302 ( Pt 2): 527–34. PMID 8093006.
López-Casillas F, Payne HM, Andres JL, Massagué J (1994). "Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites.". J. Cell Biol. 124 (4): 557–68. PMID 8106553.
Mittl PR, Priestle JP, Cox DA, et al. (1997). "The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding.". Protein Sci. 5 (7): 1261–71. PMID 8819159.
Ambros RA, Kallakury BV, Malfetano JH, Mihm MC (1997). "Cytokine, cell adhesion receptor, and tumor suppressor gene expression in vulvar squamous carcinoma: correlation with prominent fibromyxoid stromal response.". Int. J. Gynecol. Pathol. 15 (4): 320–5. PMID 8886879.
Djonov V, Ball RK, Graf S, et al. (1997). "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.". Prostate 31 (2): 103–9. PMID 9140123.
Jin L, Qian X, Kulig E, et al. (1997). "Transforming growth factor-beta, transforming growth factor-beta receptor II, and p27Kip1 expression in nontumorous and neoplastic human pituitaries.". Am. J. Pathol. 151 (2): 509–19. PMID 9250163.
Lidral AC, Romitti PA, Basart AM, et al. (1998). "Association of MSX1 and TGFB3 with nonsyndromic clefting in humans.". Am. J. Hum. Genet. 63 (2): 557–68. PMID 9683588.
Barbara NP, Wrana JL, Letarte M (1999). "Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily.". J. Biol. Chem. 274 (2): 584–94. PMID 9872992.
Lux A, Attisano L, Marchuk DA (1999). "Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1.". J. Biol. Chem. 274 (15): 9984–92. PMID 10187774.
Mori T, Kawara S, Shinozaki M, et al. (1999). "Role and interaction of connective tissue growth factor with transforming growth factor-beta in persistent fibrosis: A mouse fibrosis model.". J. Cell. Physiol. 181 (1): 153–9. doi:10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K. PMID 10457363.