Epidermal growth factor
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Location (UCSC) | Chr 4: 109.91 – 110.01 Mb | Chr 3: 129.47 – 129.55 Mb | |||||||
PubMed search | [3] | [4] |
View/Edit Human | View/Edit Mouse |
Epidermal growth factor (EGF) is a
EGF was originally described as a secreted peptide found in the
Structure
This section is missing information about the entire 1207-aa long gene product: the pro-pre-EGF; what happens if things go wrong (renal hypomagnesemia 4, OMIM 611718).(December 2023) |
In
Function
EGF, via binding to its cognate receptor, results in cellular proliferation, differentiation, and survival.[10]
Salivary EGF, which seems to be regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. The biological effects of salivary EGF include healing of oral and gastroesophageal ulcers, inhibition of gastric acid secretion, stimulation of DNA synthesis as well as mucosal protection from intraluminal injurious factors such as gastric acid, bile acids, pepsin, and trypsin and to physical, chemical and bacterial agents.[8]
Biological sources
The Epidermal growth factor can be found in platelets,[7] urine, saliva, milk, tears, and blood plasma.[11] It can also be found in the submandibular glands,[8][12] and the parotid gland.[8][12] The production of EGF has been found to be stimulated by testosterone.[citation needed]
Polypeptide growth factors
It has been suggested that portions of this section be split out into another article titled Growth factor. (Discuss) (August 2022) |
Polypeptide growth factors include:[13]
Sr.No | Growth factor | Source | Major function |
---|---|---|---|
1 | Epidermal growth factor (EGF) | Salivary gland | Stimulates growth of epidermal and epithelial cells |
2 | Platelet derived growth factor
|
Platelets | Stimulates growth of mesenchymal cells, promotes wound healing |
3 | Transforming growth factor-alpha (TGF-α) | Epithelial cell | Similar to EGF |
4 | Transforming growth factor-beta (TGF-β)
|
Platelets, Kidney, Placenta | Inhibitory effect on cultures tumor cell |
5 | Erythropoietin | Kidney | Stimulates development of erythropoietic cells |
6 | Nerve growth factor (NGF) | Salivary gland | Stimulates the growth of sensory nerves |
7 | Insulin-like growth factor | Serum | Stimulates incorporation of sulfates into cartilage, exerts insulin-like action on certain cells |
8 | Tumor necrosis factor | Monocytes | Necrosis of tumor cells |
9 | Interleukin-1 | Monocytes, Leukocytes | Stimulates synthesis of IL-2 |
10 | Interleukin-2 | Lymphocytes | Stimulates growth and maturation of T-cells |
Mechanism
EGF acts by binding with high
EGF-family / EGF-like domain
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:[16]
- 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)
- neuregulin-4 (NRG4).
All family members contain one or more repeats of the conserved amino acid sequence:
CX7CX4-5CX10-13CXCX8GXRC
Where C is cysteine, G is glycine, R is arginine, and X represents any amino acid.[16]
This sequence contains six cysteine residues that form three intramolecular
Interactions
Epidermal growth factor has been shown to
Medical uses
EGF is used to modify synthetic scaffolds for manufacturing of bioengineered grafts by emulsion electrospinning or surface modification methods.[22][23]
Bone regeneration
EGF plays an enhancer role on the osteogenic differentiation of
History
EGF was the second growth factor to be identified.[25] Initially, human EGF was known as urogastrone.[9] Stanley Cohen discovered EGF while working with Rita Levi-Montalcini at the Washington University in St. Louis during experiments researching nerve growth factor. For these discoveries Levi-Montalcini and Cohen were awarded the 1986 Nobel Prize in Physiology or Medicine.
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000138798 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028017 - Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ PMID 12648462.
- ^ PMID 2186024.
- ^ PMID 35909816.
- ^ S2CID 25710052.
- ^ PMID 6248761.
- PMID 15142631.
- ISBN 978-0-7216-0187-8.
- ^ ISBN 978-0-12-382219-2
- OCLC 71209231.
- PMID 16107719.
- PMID 6144184.
- ^ PMID 16076471.
- PMID 12093292.
- PMID 10085134.
- PMID 23396236.
- S2CID 43897291.
- ^ PMID 26509249.
- PMID 27740881.
- S2CID 90593089.
- PMID 26334535.
- ISBN 978-0-12-370879-3. Retrieved 2020-11-30.)
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Further reading
- Boonstra J, Rijken P, Humbel B, Cremers F, Verkleij A, van Bergen en Henegouwen P (May 1995). "The epidermal growth factor". Cell Biology International. 19 (5): 413–30. S2CID 20186286.
- Dvorak B (March 2004). "Epidermal growth factor and necrotizing enterocolitis". Clinics in Perinatology. 31 (1): 183–92. PMID 15183666.
- Howell WM (October 2004). "Epidermal growth factor gene polymorphism and development of cutaneous melanoma". The Journal of Investigative Dermatology. 123 (4): xx–xxi. PMID 15373802.
External links
- Shaanxi Zhongbang Pharma-Tech Co., Ltd.-Supply of Epidermal Growth Factor
- EGF at the Human Protein Reference Database Archived 2005-05-03 at the Wayback Machine.
- Epidermal+growth+factor at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EGF model in BioModels database