TGF beta 2

From Wikipedia, the free encyclopedia


Transforming growth factor, beta 2
PDB rendering based on 1tfg.
Available structures: 1tfg, 2tgi
Identifiers
Symbol(s) TGFB2; MGC116892; TGF-beta2
External IDs OMIM: 190220 MGI: 98726 HomoloGene: 2432
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 7042 21808
Ensembl ENSG00000092969 ENSMUSG00000039239
Uniprot P61812 Q3TWH5
Refseq NM_003238 (mRNA)
NP_003229 (protein)		 NM_009367 (mRNA)
NP_033393 (protein)
Location Chr 1: 216.59 - 216.68 Mb Chr 1: 188.32 - 188.41 Mb
Pubmed search [1] [2]

Transforming growth factor-beta 2 (TGF-β2) is a secreted protein known as a cytokine that performs many cellular functions and has a vital role during embryonic development (alternative names: Glioblastoma-derived T-cell suppressor factor, G-TSF, BSC-1 cell growth inhibitor, Polyergin, Cetermin). This is an extracellular glycosilated protein. It is known to suppress the effects of interleukin dependent T-cell tumors. There are two named isoforms of this protein, created by alternative splicing of the same gene.


[edit] Further reading

  • Clark DA, Coker R (1998). "Transforming growth factor-beta (TGF-beta).". Int. J. Biochem. Cell Biol. 30 (3): 293–8. PMID 9611771. 
  • Wick W, Platten M, Weller M (2002). "Glioma cell invasion: regulation of metalloproteinase activity by TGF-beta.". J. Neurooncol. 53 (2): 177–85. PMID 11716069. 
  • Bissell DM (2002). "Chronic liver injury, TGF-beta, and cancer.". Exp. Mol. Med. 33 (4): 179–90. PMID 11795478. 
  • 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. 
  • Daopin S, Piez KA, Ogawa Y, Davies DR (1992). "Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.". Science 257 (5068): 369–73. PMID 1631557. 
  • Schlunegger MP, Grütter MG (1992). "An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2.". Nature 358 (6385): 430–4. doi:10.1038/358430a0. PMID 1641027. 
  • Noma T, Glick AB, Geiser AG, et al. (1992). "Molecular cloning and structure of the human transforming growth factor-beta 2 gene promoter.". Growth Factors 4 (4): 247–55. PMID 1764261. 
  • Bodmer S, Podlisny MB, Selkoe DJ, et al. (1990). "Transforming growth factor-beta bound to soluble derivatives of the beta amyloid precursor protein of Alzheimer's disease.". Biochem. Biophys. Res. Commun. 171 (2): 890–7. PMID 2119582. 
  • Webb NR, Madisen L, Rose TM, Purchio AF (1989). "Structural and sequence analysis of TGF-beta 2 cDNA clones predicts two different precursor proteins produced by alternative mRNA splicing.". DNA 7 (7): 493–7. PMID 2850146. 
  • Madisen L, Webb NR, Rose TM, et al. (1988). "Transforming growth factor-beta 2: cDNA cloning and sequence analysis.". DNA 7 (1): 1–8. PMID 3162414. 
  • 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. 
  • de Martin R, Haendler B, Hofer-Warbinek R, et al. (1988). "Complementary DNA for human glioblastoma-derived T cell suppressor factor, a novel member of the transforming growth factor-beta gene family.". EMBO J. 6 (12): 3673–7. PMID 3322813. 
  • Marquardt H, Lioubin MN, Ikeda T (1987). "Complete amino acid sequence of human transforming growth factor type beta 2.". J. Biol. Chem. 262 (25): 12127–31. PMID 3476488. 
  • Philip A, Bostedt L, Stigbrand T, O'Connor-McCourt MD (1994). "Binding of transforming growth factor-beta (TGF-beta) to pregnancy zone protein (PZP). Comparison to the TGF-beta-alpha 2-macroglobulin interaction.". Eur. J. Biochem. 221 (2): 687–93. PMID 7513640. 
  • 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. 
  • 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. 
  • Fromigué O, Marie PJ, Lomri A (1998). "Bone morphogenetic protein-2 and transforming growth factor-beta2 interact to modulate human bone marrow stromal cell proliferation and differentiation.". J. Cell. Biochem. 68 (4): 411–26. PMID 9493905. 
  • 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. 




v • d • e
Cell signaling: TGF beta signaling pathway
TGF beta superfamily of ligands
TGF beta receptors
Transducers/SMAD
Ligand Inhibitors
Coreceptors
Other