TGF alpha

Transforming growth factor, alpha

PDB rendering based on 1mox.

Available structures
PDB	1GK5, 1MOX, 1YUF, 1YUG, 2TGF, 3E50, 3TGF, 4TGF

Identifiers

Symbols

TGFA; TFGA

External IDs

OMIM: 190170 MGI: 98724 HomoloGene: 2431 GeneCards: TGFA Gene

Gene Ontology
Molecular function	• glycoprotein binding • MAP kinase kinase activity • signal transducer activity • epidermal growth factor receptor binding • protein binding • growth factor activity
Cellular component	• extracellular region • extracellular space • nucleus • plasma membrane • cell surface • integral to membrane
Biological process	• activation of MAPK activity • angiogenesis • positive regulation of protein phosphorylation • anti-apoptosis • signal transduction • epidermal growth factor receptor signaling pathway • cell proliferation • wound healing • response to drug • negative regulation of neuron apoptosis • neuroprotection • positive regulation of epidermal growth factor receptor activity • positive regulation of mitosis • negative regulation of cellular process • positive regulation of epithelial cell proliferation • cytosolic calcium ion homeostasis • positive regulation of cell division • mammary gland alveolus development
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
70.67 – 70.78 Mb

Chr 6:
86.15 – 86.23 Mb

PubMed search

[1]

[2]

Transforming growth factor alpha (TGF-α) is upregulated in some human cancers. It is produced in macrophages, brain cells, and keratinocytes, and induces epithelial development. It is closely related to EGF, and can also bind to the EGF receptor with similar effects . TGFα stimulates neural cell proliferation in the adult injured brain.^[1]

TGFα was cited in the 2001 NIH Stem Cell report to the U.S. Congress as promising evidence for the ability of adult stem cells to restore function in neurodegenerative disorders.

1 Interactions
2 See also
3 References
4 Further reading
5 External links

Interactions

TGF alpha has been shown to interact with GORASP1^[2] and GORASP2.^[2]

References

^ In vivo induction of massive proliferation, directed migration, and differentiation of neural cells in the adult mammalian brain. Proc Natl Acad Sci USA. 2000 Dec 19; 97(26): 14686-91; PubMed Full text at PMC: 11121069
^ ^a ^b Barr, F A; Preisinger C, Kopajtich R, Körner R (Dec. 2001). "Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus". J. Cell Biol. (United States) 155 (6): 885–91. doi:10.1083/jcb.200108102. ISSN 0021-9525. PMC 2150891. PMID 11739402. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2150891.

Luetteke NC, Lee DC (1991). "Transforming growth factor alpha: expression, regulation and biological action of its integral membrane precursor". Semin. Cancer Biol. 1 (4): 265–75. PMID 2103501.
Greten FR, Wagner M, Weber CK, et al. (2002). "TGF alpha transgenic mice. A model of pancreatic cancer development". Pancreatology 1 (4): 363–8. doi:10.1159/000055835. PMID 12120215.
Vieira AR (2006). "Association between the transforming growth factor alpha gene and nonsyndromic oral clefts: a HuGE review". Am. J. Epidemiol. 163 (9): 790–810. doi:10.1093/aje/kwj103. PMID 16495466.
Nasim MM, Thomas DM, Alison MR, Filipe MI (1992). "Transforming growth factor alpha expression in normal gastric mucosa, intestinal metaplasia, dysplasia and gastric carcinoma--an immunohistochemical study". Histopathology 20 (4): 339–43. doi:10.1111/j.1365-2559.1992.tb00991.x. PMID 1577411.
Thomas DM, Nasim MM, Gullick WJ, Alison MR (1992). "Immunoreactivity of transforming growth factor alpha in the normal adult gastrointestinal tract". Gut 33 (5): 628–31. doi:10.1136/gut.33.5.628. PMC 1379291. PMID 1612477. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1379291.
Bean MF, Carr SA (1992). "Characterization of disulfide bond position in proteins and sequence analysis of cystine-bridged peptides by tandem mass spectrometry". Anal. Biochem. 201 (2): 216–26. doi:10.1016/0003-2697(92)90331-Z. PMID 1632509.
Lei ZM, Rao CV (1992). "Expression of epidermal growth factor (EGF) receptor and its ligands, EGF and transforming growth factor-alpha, in human fallopian tubes". Endocrinology 131 (2): 947–57. doi:10.1210/en.131.2.947. PMID 1639032.
Werner S, Roth WK, Bates B, et al. (1991). "Fibroblast growth factor 5 proto-oncogene is expressed in normal human fibroblasts and induced by serum growth factors". Oncogene 6 (11): 2137–44. PMID 1658709.
Saeki T, Cristiano A, Lynch MJ, et al. (1992). "Regulation by estrogen through the 5'-flanking region of the transforming growth factor alpha gene". Mol. Endocrinol. 5 (12): 1955–63. doi:10.1210/mend-5-12-1955. PMID 1791840.
Harvey TS, Wilkinson AJ, Tappin MJ, et al. (1991). "The solution structure of human transforming growth factor alpha". Eur. J. Biochem. 198 (3): 555–62. doi:10.1111/j.1432-1033.1991.tb16050.x. PMID 2050136.
Kline TP, Brown FK, Brown SC, et al. (1991). "Solution structures of human transforming growth factor alpha derived from 1H NMR data". Biochemistry 29 (34): 7805–13. doi:10.1021/bi00486a005. PMID 2261437.
Jakowlew SB, Kondaiah P, Dillard PJ, et al. (1989). "A novel low molecular weight ribonucleic acid (RNA) related to transforming growth factor alpha messenger RNA". Mol. Endocrinol. 2 (11): 1056–63. doi:10.1210/mend-2-11-1056. PMID 2464748.
Jakobovits EB, Schlokat U, Vannice JL, et al. (1989). "The human transforming growth factor alpha promoter directs transcription initiation from a single site in the absence of a TATA sequence". Mol. Cell. Biol. 8 (12): 5549–54. PMC 365660. PMID 2907605. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=365660.
Tricoli JV, Nakai H, Byers MG, et al. (1986). "The gene for human transforming growth factor alpha is on the short arm of chromosome 2". Cytogenet. Cell Genet. 42 (1–2): 94–8. doi:10.1159/000132258. PMID 3459638.
Lee DC, Rose TM, Webb NR, Todaro GJ (1985). "Cloning and sequence analysis of a cDNA for rat transforming growth factor-alpha". Nature 313 (6002): 489–91. doi:10.1038/313489a0. PMID 3855503.
Derynck R, Roberts AB, Winkler ME, et al. (1984). "Human transforming growth factor-alpha: precursor structure and expression in E. coli". Cell 38 (1): 287–97. doi:10.1016/0092-8674(84)90550-6. PMID 6088071.
Ogbureke KU, MacDaniel RK, Jacob RS, Durban EM (1995). "Distribution of immunoreactive transforming growth factor-alpha in non-neoplastic human salivary glands". Histol. Histopathol. 10 (3): 691–6. PMID 7579819.
Walz TM, Malm C, Nishikawa BK, Wasteson A (1995). "Transforming growth factor-alpha (TGF-alpha) in human bone marrow: demonstration of TGF-alpha in erythroblasts and eosinophilic precursor cells and of epidermal growth factor receptors in blastlike cells of myelomonocytic origin". Blood 85 (9): 2385–92. PMID 7727772.
Patel B, Hiscott P, Charteris D, et al. (1994). "Retinal and preretinal localisation of epidermal growth factor, transforming growth factor alpha, and their receptor in proliferative diabetic retinopathy". The British journal of ophthalmology 78 (9): 714–8. doi:10.1136/bjo.78.9.714. PMC 504912. PMID 7947554. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=504912.

PDB gallery

1mox: Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha

1yuf: TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 16 MODELS WITHOUT ENERGY MINIMIZATION

1yug: TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 15 MODELS AFTER ECEPP/3 ENERGY MINIMIZATION

2tgf: THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA

3tgf: THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA

4tgf: SOLUTION STRUCTURES OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA DERIVED FROM 1*H NMR DATA

External links

MeSH Transforming+Growth+Factor+alpha

Growth factors

Fibroblast	FGF receptor ligands: FGF1/FGF2/FGF5 · FGF3/FGF4/FGF6 · KGF (FGF7/FGF10/FGF22) · FGF8/FGF17/FGF18 · FGF9/FGF16/FGF20 FGF homologous factors: FGF11 · FGF12 · FGF13 · FGF14 hormone-like: FGF19 · FGF21 · FGF23

EGF-like domain	TGF-α · EGF · HB-EGF

TGFβ pathway	TGF-β (TGF-β1, TGF-β2, TGF-β3)

Insulin-like	IGF-1 · IGF-2

Platelet-derived	PDGFA · PDGFB · PDGFC · PDGFD

Vascular endothelial	VEGF-A · VEGF-B · VEGF-C · VEGF-D · PGF

Other	Nerve · Hepatocyte

B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

TGF alpha

Contents

Interactions

See also

References

Further reading

External links