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Epidermal growth factor

Epidermal growth factor (beta-urogastrone)
PDB rendering based on 1ivo.
Available structures: 1ivo, 1jl9, 1nql, 1p9j
Symbol(s) EGF; URG
External IDs OMIM: 131530 MGI: 95290 Homologene: 1483
RNA expression pattern

More reference expression data

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]



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 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:


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]


  1. ^ Carpenter G, and Cohen S. (1990). "Epidermal growth factor". J. Biol. Chem. 265 (14): 7709-7712. PMID 2186024.
  2. ^ Fallon JH, Seroogy al (1984). "Epidermal growth factor immunoreactive material in the central nervous system: location and development". Science 224 (4653): 1107-1109. PMID 6144184.
  3. ^ 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.
  4. ^ Harris RC, Chung E, and Coffey RJ. (2003). "EGF receptor ligands". Exp. Cell. Res. 284 (1): 2-13. PMID 12648462.
  5. ^ Frew S, Rezaie al (2007). "India’s health biotech sector at a crossroads". Nature Biotechnology 25 (4).
  6. ^ a b Lopez E, Acevedo 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.

This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Epidermal_growth_factor". A list of authors is available in Wikipedia.
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