TGF beta 1

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Protein TGFB1 PDB 1kla.png
Available structures
PDBOrtholog search: PDBe RCSB
AliasesTGFB1, CED, DPD1, LAP, TGFB, TGFbeta, transforming growth factor beta 1, IBDIMDE, TGF-beta1
External IDsOMIM: 190180 MGI: 98725 HomoloGene: 540 GeneCards: TGFB1
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 19: 41.3 – 41.35 MbChr 7: 25.39 – 25.4 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Transforming growth factor beta 1 or TGF-β1 is a polypeptide member of the transforming growth factor beta superfamily of cytokines. It is a secreted protein that performs many cellular functions, including the control of cell growth, cell proliferation, cell differentiation, and apoptosis. In humans, TGF-β1 is encoded by the TGFB1 gene.[5][6]


TGF-β is a multifunctional set of peptides that controls proliferation, differentiation, and other functions in many cell types. TGF-β acts synergistically with transforming growth factor-alpha (TGF-α) in inducing transformation. It also acts as a negative autocrine growth factor. Dysregulation of TGF-β activation and signaling may result in apoptosis. Many cells synthesize TGF-β and almost all of them have specific receptors for this peptide. TGF-β1, TGF-β2, and TGF-β3 all function through the same receptor signaling systems.[7]

TGF-β1 was first identified in human platelets as a protein with a molecular mass of 25 kilodaltons with a potential role in wound healing.[8] It was later characterized as a large protein precursor (containing 390 amino acids) that was proteolytically processed to produce a mature peptide of 112 amino acids.[9]

TGF-β1 plays an important role in controlling the immune system, and shows different activities on different types of cell, or cells at different developmental stages. Most immune cells (or leukocytes) secrete TGF-β1.[10]

T cells[edit]

Some T cells (e.g. regulatory T cells) release TGF-β1 to inhibit the actions of other T cells. Specifically, TGF-β1 prevents the interleukin(IL)-1- & interleukin-2-dependent proliferation in activated T cells,[11][12] as well as the activation of quiescent helper T cells and cytotoxic T cells.[13][14] Similarly, TGF-β1 can inhibit the secretion and activity of many other cytokines including interferon-γ, tumor necrosis factor-alpha (TNF-α), and various interleukins. It can also decrease the expression levels of cytokine receptors, such as the IL-2 receptor to down-regulate the activity of immune cells. However, TGF-β1 can also increase the expression of certain cytokines in T cells and promote their proliferation,[15] particularly if the cells are immature.[10]

B cells[edit]

TGF-β1 has similar effects on B cells that also vary according to the differentiation state of the cell. It inhibits proliferation, stimulates apoptosis of B cells,[16] and controls the expression of antibody, transferrin and MHC class II proteins on immature and mature B cells.[10][16]

Myeloid cells[edit]

The effects of TGF-β1 on macrophages and monocytes are predominantly suppressive; this cytokine can inhibit the proliferation of these cells and prevent their production of reactive oxygen (e.g. superoxide (O2)) and nitrogen (e.g. nitric oxide (NO)) intermediates. However, as with other cell types, TGF-β1 can also have the opposite effect on cells of myeloid origin. For example, TGF-β1 acts as a chemoattractant, directing an immune response to certain pathogens. Likewise, macrophages and monocytes respond to low levels of TGF-β1 in a chemotactic manner. Furthermore, the expression of monocytic cytokines (such as interleukin(IL)-1α, IL-1β, and TNF-α),[14] and macrophage's phagocytic can be increased by the action of TGF-β1.[10]

TGF-β1 reduces the efficacy of the MHC II in astrocytes and dendritic cells, which in turn decreases the activation of appropriate helper T cell populations.[17][18]


TGF beta 1 has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105329 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000002603 - Ensembl, May 2017
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  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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  7. ^ "Entrez Gene: TGFB1 transforming growth factor, beta 1".{{cite web}}: CS1 maint: url-status (link)
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  15. ^ Zhu H, Wang Z, Yu J, Yang X, He F, Liu Z, Che F, Chen X, Ren H, Hong M, Wang J (March 2019). "Role and mechanisms of cytokines in the secondary brain injury after intracerebral hemorrhage". Prog. Neurobiol. 178: 101610. doi:10.1016/j.pneurobio.2019.03.003. PMID 30923023. S2CID 85495400.
  16. ^ a b Lebman DA, Edmiston JS (1999). "The role of TGF-beta in growth, differentiation, and maturation of B lymphocytes". Microbes Infect. 1 (15): 1297–304. doi:10.1016/S1286-4579(99)00254-3. PMID 10611758.
  17. ^ Rodríguez LS, Narváez CF, Rojas OL, Franco MA, Ángel J (2012-01-01). "Human myeloid dendritic cells treated with supernatants of rotavirus infected Caco-2 cells induce a poor Th1 response". Cellular Immunology. 272 (2): 154–61. doi:10.1016/j.cellimm.2011.10.017. PMID 22082567.
  18. ^ Dong Y, Tang L, Letterio JJ, Benveniste EN (July 2001). "The Smad3 protein is involved in TGF-beta inhibition of class II transactivator and class II MHC expression". Journal of Immunology. 167 (1): 311–9. doi:10.4049/jimmunol.167.1.311. PMID 11418665.
  19. ^ Hildebrand A, Romarís M, Rasmussen LM, Heinegård D, Twardzik DR, Border WA, Ruoslahti E (September 1994). "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta". Biochem. J. 302 (2): 527–34. doi:10.1042/bj3020527. PMC 1137259. PMID 8093006.
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  21. ^ Takeuchi Y, Kodama Y, Matsumoto T (Dec 1994). "Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity". J. Biol. Chem. 269 (51): 32634–8. doi:10.1016/S0021-9258(18)31681-8. PMID 7798269.
  22. ^ Choy L, Derynck R (November 1998). "The type II transforming growth factor (TGF)-beta receptor-interacting protein TRIP-1 acts as a modulator of the TGF-beta response". J. Biol. Chem. 273 (47): 31455–62. doi:10.1074/jbc.273.47.31455. PMID 9813058.
  23. ^ Saharinen J, Keski-Oja J (August 2000). "Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta". Mol. Biol. Cell. 11 (8): 2691–704. doi:10.1091/mbc.11.8.2691. PMC 14949. PMID 10930463.
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  25. ^ Oh SP, Seki T, Goss KA, Imamura T, Yi Y, Donahoe PK, Li L, Miyazono K, ten Dijke P, Kim S, Li E (March 2000). "Activin receptor-like kinase 1 modulates transforming growth factor-beta 1 signaling in the regulation of angiogenesis". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2626–31. Bibcode:2000PNAS...97.2626O. doi:10.1073/pnas.97.6.2626. PMC 15979. PMID 10716993.
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Further reading[edit]

External links[edit]

  • Overview of all the structural information available in the PDB for UniProt: P01137 (Transforming growth factor beta-1) at the PDBe-KB.