Biology:TGF beta 2

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

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). It is an extracellular glycosylated 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 (i.e., TGFB2).

Further reading

• "Transforming growth factor-beta (TGF-beta).". Int. J. Biochem. Cell Biol. 30 (3): 293–8. 1998. doi:10.1016/S1357-2725(97)00128-3. PMID 9611771. 
• "Glioma cell invasion: regulation of metalloproteinase activity by TGF-beta.". J. Neurooncol. 53 (2): 177–85. 2002. doi:10.1023/A:1012209518843. PMID 11716069. 
• Bissell DM (2002). "Chronic liver injury, TGF-beta, and cancer.". Experimental & Molecular Medicine 33 (4): 179–90. doi:10.1038/emm.2001.31. PMID 11795478. 
• "Epithelial-mesenchymal transition and its implications for fibrosis.". J. Clin. Invest. 112 (12): 1776–84. 2004. doi:10.1172/JCI20530. PMID 14679171. 
• "Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.". Science 257 (5068): 369–73. 1992. doi:10.1126/science.1631557. PMID 1631557. Bibcode: 1992Sci...257..369D. https://zenodo.org/record/1230942. 
• "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. 1992. doi:10.1038/358430a0. PMID 1641027. Bibcode: 1992Natur.358..430S. 
• "Molecular cloning and structure of the human transforming growth factor-beta 2 gene promoter.". Growth Factors 4 (4): 247–55. 1992. doi:10.3109/08977199109043910. PMID 1764261. 
• "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. 1990. doi:10.1016/0006-291X(90)91229-L. PMID 2119582. 
• "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. 1989. doi:10.1089/dna.1.1988.7.493. PMID 2850146. 
• "Transforming growth factor-beta 2: cDNA cloning and sequence analysis.". DNA 7 (1): 1–8. 1988. doi:10.1089/dna.1988.7.1. PMID 3162414. 
• "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. 1989. PMID 3226728. 
• "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. 1988. doi:10.1002/j.1460-2075.1987.tb02700.x. PMID 3322813. 
• "Complete amino acid sequence of human transforming growth factor type beta 2.". J. Biol. Chem. 262 (25): 12127–31. 1987. doi:10.1016/S0021-9258(18)45325-2. PMID 3476488. 
• "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. 1994. doi:10.1111/j.1432-1033.1994.tb18781.x. PMID 7513640. 
• "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. 1995. doi:10.1074/jbc.270.6.2747. PMID 7852346. 
• "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta.". Biochem. J.. 302 ( Pt 2) (2): 527–34. 1994. doi:10.1042/bj3020527. PMID 8093006. 
• "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. 1994. doi:10.1083/jcb.124.4.557. PMID 8106553. 
• "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. 1998. doi:10.1002/(SICI)1097-4644(19980315)68:4<411::AID-JCB2>3.0.CO;2-T. PMID 9493905. 
• "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. 1999. doi:10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K. PMID 10457363.