Epidermal growth factor
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Epidermal growth factor (beta-urogastrone)
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| PDB rendering based on 1ivo. |
| Available structures: 1ivo, 1jl9, 1nql, 1p9j |
| Identifiers |
| Symbol(s) |
EGF; URG |
| External IDs |
OMIM: 131530 MGI: 95290 Homologene: 1483 |
| Gene Ontology |
| Molecular Function: |
• epidermal growth factor receptor-activating ligand activity
• calcium ion binding
• protein binding
• growth factor activity
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| Cellular Component: |
• extracellular region
• extracellular space
• nucleus
• plasma membrane
• integral to membrane
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| Biological Process: |
• activation of MAPKK activity
• activation of MAPK activity
• DNA replication
• chromosome organization and biogenesis (sensu Eukaryota)
• epidermal growth factor receptor signaling pathway
• positive regulation of cell proliferation
• branching morphogenesis of a tube
• regulation of peptidyl-tyrosine phosphorylation
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| RNA expression pattern |
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More reference expression data
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| Orthologs |
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Human |
Mouse |
| Entrez |
1950 |
13645 |
| Ensembl |
ENSG00000138798 |
ENSMUSG00000028017 |
| Uniprot |
P01133 |
Q3UWD7 |
| Refseq |
NM_001963 (mRNA)
NP_001954 (protein) |
NM_010113 (mRNA)
NP_034243 (protein) |
| Location |
Chr 4: 111.05 - 111.15 Mb |
Chr 3: 129.67 - 129.75 Mb |
| Pubmed search |
[1] |
[2] |
Epidermal growth factor or EGF is a growth factor that plays an important role in the regulation of cell growth, proliferation, and differentiation. Human EGF is a 6045-Da protein with 53 amino acid residues and three intramolecular disulfide bonds.[1]
Function
EGF acts by binding with high affinity to epidermal growth factor receptor (EGFR) on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor (see the second diagram). The tyrosine kinase activity, in turn, initiates a signal transduction cascade that results in a variety of biochemical changes within the cell - a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR - that ultimately lead to DNA synthesis and cell proliferation.[2]
EGF-family
EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. Besides EGF itself other family members include:[3]
- Heparin-binding EGF-like growth factor (HB-EGF)
- transforming growth factor-α (TGF-α)
- Amphiregulin (AR)
- Epiregulin (EPR)
- Epigen
- Betacellulin (BTC)
- neuregulin-1 (NRG1)
- neuregulin-2 (NRG2)
- neuregulin-3 (NRG3)
- neureguline-4 (NRG4).
All family members contain one or more repeats of the conserved amino acid sequence:
CX7CX4-5CX10-13CXCX8GXRC
Where X represents any amino acid.[3]
This sequence contains 6 cysteine residues that form three intramolecular disulphide bonds. Disulphide bond formation generates three structural loops that are essential for high-affinity binding between members of the EGF-family and their cell-surface receptors.[4]
EGF as Therapeutic Protein
EGF is currently being marketed as a therapeutic protein for the treatment of diabetic foot ulcers by at least three companies. Bharat Biotech International, a company based in India, is marketing EGF as REGEN-D, Daewoong Pharmaceutical, based in South Korea, is marketing EGF as Easyef, and the Center for Genetic Engineering and Biotechnology, in Cuba, is marketing EGF as CITOPROT-P.[5] [6] EGF is also used in a burn treatment cream product, Hebermin, manufactured by Heber Biotec S. A. in Cuba.[6]
References
- ^ Carpenter G, and Cohen S. (1990). "Epidermal growth factor". J. Biol. Chem. 265 (14): 7709-7712. PMID 2186024.
- ^ Fallon JH, Seroogy KB.et al (1984). "Epidermal growth factor immunoreactive material in the central nervous system: location and development". Science 224 (4653): 1107-1109. PMID 6144184.
- ^ a b Dreux AC, Lamb DJ. et al. (2006). "The epidermal growth factor receptors and their family of ligands: their putative role in atherogenesis". Atherosclerosis 186 (1): 38-53. PMID 16076471.
- ^ Harris RC, Chung E, and Coffey RJ. (2003). "EGF receptor ligands". Exp. Cell. Res. 284 (1): 2-13. PMID 12648462.
- ^ Frew S, Rezaie R.et al (2007). "India’s health biotech sector at a crossroads". Nature Biotechnology 25 (4).
- ^ a b Lopez E, Acevedo B.et al (2002). "Development of Cuban Biotechnology". Journal of Commercial Biotechnology 9 (2).
Further reading
- Boonstra J, Rijken P, Humbel B, et al. (1995). "The epidermal growth factor.". Cell Biol. Int. 19 (5): 413-30. PMID 7640657.
- Dvorak B (2004). "Epidermal growth factor and necrotizing enterocolitis.". Clinics in perinatology 31 (1): 183-92. doi:10.1016/j.clp.2004.03.015. PMID 15183666.
- Howell WM (2004). "Epidermal growth factor gene polymorphism and development of cutaneous melanoma.". J. Invest. Dermatol. 123 (4): xx-xxi. doi:10.1111/j.0022-202X.2004.23308.x. PMID 15373802.
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