Factor de crecemento transformante beta 2
| |
| TGFB2 procedente de PDB 1tfg . | |
| Identificadores | |
| Símbolo | TGFB2 |
| Símbolos alt. | LDS4; TGF-beta2 |
| Entrez | 7042 |
| OMIM | |
| RefSeq | NP_001129071 |
| UniProt | P61812 |
| Outros datos | |
| Locus | Cr. 1 :(218.35 – 218.44 Mb) |
O factor de crecemento transformante beta 2 (TGF-β2) é unha proteína segregada que funciona como citocina e realiza moitas funcións celulares e ten un papel vital durante o desenvolvemento embrionario. Outros nomes que recibe son: factor supresor de células T derivado do glioblastoma[1], G-TSF, inhibidor do crecemento das células BSC-1, polierxina, cetermina. Está codificado polo xene TGFB2 do cromosoma 1 humano. Trátase dunha proteína extracelular glicosilada. Suprime os efectos dos tumores de células T dependentes de interleucina. Hai dúas variantes desta proteína, xeradas por empalme alternativo a partir de transcritos do mesmo xene.
A estrutura do TGF-2 foi determinada e o seu monómero ten un núcleo hidrofóbico e un pregamento non globular alongado. Presenta oito cisteínas que forman 4 pontes disulfuro intracadea agrupadas na rexión central formando unha rede complementaria de pontes de hidróxeno. Unha novena cisteína serve para formar un dímero mediante unha ponte de hidróxeno, o cal está estabilizado por dúas caras hidrofóbicas.[2][3]
Notas[editar | editar a fonte]
- ↑ 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. PMC 553836. PMID 3322813.
- ↑ 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. doi:10.1126/science.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. PMID 1641027. doi:10.1038/358430a0.
Véxase tamén[editar | editar a fonte]
Outros artigos[editar | editar a fonte]
Bibliografía[editar | editar a fonte]
- Clark DA, Coker R (1998). "Transforming growth factor-beta (TGF-beta).". Int. J. Biochem. Cell Biol. 30 (3): 293–8. PMID 9611771. doi:10.1016/S1357-2725(97)00128-3.
- 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. doi:10.1023/A:1012209518843.
- Bissell DM (2002). "Chronic liver injury, TGF-beta, and cancer.". Experimental & Molecular Medicine 33 (4): 179–90. PMID 11795478. doi:10.1038/emm.2001.31.
- Kalluri R, Neilson EG (2004). "Epithelial-mesenchymal transition and its implications for fibrosis.". J. Clin. Invest. 112 (12): 1776–84. PMC 297008. PMID 14679171. doi:10.1172/JCI20530.
- 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. doi:10.3109/08977199109043910.
- 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. doi:10.1016/0006-291X(90)91229-L.
- 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. doi:10.1089/dna.1.1988.7.493.
- 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. doi:10.1089/dna.1988.7.1.
- 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.
- 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. doi:10.1111/j.1432-1033.1994.tb18781.x.
- 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. doi:10.1074/jbc.270.6.2747.
- 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. PMC 1137259. 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. PMC 2119924. PMID 8106553. doi:10.1083/jcb.124.4.557.
- 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. doi:10.1002/(SICI)1097-4644(19980315)68:4<411::AID-JCB2>3.0.CO;2-T.
- 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. PMID 10457363. doi:10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K.
