Epidermal growth factor: Difference between revisions

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{{Distinguish|EF-G}}
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'''Epidermal growth factor''' ('''EGF''') stimulates [[cell growth]] and [[Cellular differentiation|differentiation]] by binding to its receptor, [[Epidermal growth factor receptor|EGFR]]. Human EGF is a 6-k[[dalton (unit)|Da]] [[protein]]<ref name="pmid12648462">{{cite journal| vauthors = Harris RC, Chung E, Coffey RJ| title = EGF receptor ligands| journal = Experimental Cell Research| volume = 284| issue = 1| pages = 2–13| date = March 2003| pmid = 12648462| doi = 10.1016/S0014-4827(02)00105-2}}</ref> with 53 [[amino acid|amino acid residues]] and three intramolecular [[disulfide bond]]s.<ref name="pmid2186024">{{cite journal| vauthors = Carpenter G, Cohen S| title = Epidermal growth factor| journal = The Journal of Biological Chemistry| volume = 265| issue = 14| pages = 7709–12| date = May 1990| pmid = 2186024| doi = |url = http://www.jbc.org/cgi/reprint/265/14/7709}}</ref>
| require_manual_inspection = no
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
EGF was originally described as a secreted peptide found in the [[submaxillary gland]]s of [[Mus musculus|mice]] and in human [[urine]]. EGF has since been found in many human tissues including submandibular gland, parotid gland.<ref name=Venturi2009/> Initially, human EGF was known as '''urogastrone'''.<ref>{{cite journal|last1=Hollenberg|first1=MD|last2=Gregory|first2=H|title=Epidermal growth factor-urogastrone: biological activity and receptor binding of derivatives.|journal=Molecular Pharmacology|date=May 1980|volume=17|issue=3|pages=314–20|pmid=6248761|url=http://molpharm.aspetjournals.org/content/17/3/314}}</ref>
{{GNF_Protein_box
| image = PBB_Protein_EGF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ivo.
| PDB = {{PDB2|1ivo}}, {{PDB2|1jl9}}, {{PDB2|1nql}}, {{PDB2|1p9j}}
| Name = Epidermal growth factor (beta-urogastrone)
  | HGNCid = 3229
| Symbol = EGF
| AltSymbols =; URG
| OMIM = 131530
| ECnumber = 
| Homologene = 1483
| MGIid = 95290
| GeneAtlas_image1 = PBB_GE_EGF_206254_at_tn.png
| Function = {{GNF_GO|id=GO:0005155 |text = epidermal growth factor receptor-activating ligand activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000186 |text = activation of MAPKK activity}} {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}} {{GNF_GO|id=GO:0007173 |text = epidermal growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0048754 |text = branching morphogenesis of a tube}} {{GNF_GO|id=GO:0050730 |text = regulation of peptidyl-tyrosine phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1950
    | Hs_Ensembl = ENSG00000138798
    | Hs_RefseqProtein = NP_001954
    | Hs_RefseqmRNA = NM_001963
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 111053499
    | Hs_GenLoc_end = 111152860
    | Hs_Uniprot = P01133
    | Mm_EntrezGene = 13645
    | Mm_Ensembl = ENSMUSG00000028017
    | Mm_RefseqmRNA = NM_010113
    | Mm_RefseqProtein = NP_034243
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 129669600
    | Mm_GenLoc_end = 129747338
    | Mm_Uniprot = Q3UWD7
  }}
}}


[[Image:MAPKpathway.png|thumb|right|Diagram showing key components of the [[MAPK/ERK pathway]]. In the diagram, "P" represents  [[phosphate]]. Note EGF at the very top.]]
== Function ==
'''Epidermal growth factor''' or  '''EGF''' is a [[growth factor]] that plays an important role in the regulation of [[cell growth]], [[proliferation]], and [[Cellular differentiation|differentiation]]. Human EGF is a 6045-[[dalton (unit)|Da]] [[protein]] with 53 [[amino acid|amino acid residues]] and three intramolecular [[disulfide bond]]s.<ref>{{cite journal | author =Carpenter G, and Cohen S. | title =Epidermal growth factor | journal =J. Biol. Chem. | year=1990 | volume=265 | issue=14 | pages=7709-7712 | id = PMID 2186024}}</ref>
EGF [binding to EGFR] results in cellular proliferation, differentiation, and survival.<ref name="Herbst">{{cite journal | author = Herbst RS | title = Review of epidermal growth factor receptor biology | journal = International Journal of Radiation Oncology, Biology, Physics | volume = 59 | issue = 2 Suppl | pages = 21–6 | year = 2004 | pmid = 15142631 | doi = 10.1016/j.ijrobp.2003.11.041 }}</ref>


==Function==
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.<ref name=Venturi2009>{{cite journal | vauthors = Venturi S, Venturi M | title = Iodine in evolution of salivary glands and in oral health | journal = Nutrition and Health | volume = 20 | issue = 2 | pages = 119–134 | year = 2009 | pmid = 19835108 | doi = 10.1177/026010600902000204 }}</ref>
EGF acts by binding with high [[affinity]] to [[epidermal growth factor receptor]] (EGFR) on the [[plasma membrane|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 [[biochemistry|biochemical]] changes within the cell - a rise in intracellular [[calcium]] levels, increased [[glycolysis]] and [[protein synthesis]], and increases in the [[gene expression|expression]] of certain [[gene]]s including the gene for EGFR - that ultimately lead to [[DNA replication|DNA synthesis]] and cell proliferation.<ref>{{cite journal | author =Fallon JH, Seroogy KB.''et al'' | title=Epidermal growth factor immunoreactive material in the central nervous system: location and development | journal =Science | year=1984 | volume=224 | issue=4653 | pages=1107-1109 | id = PMID 6144184}}</ref>  


==EGF-family==
== Biological sources ==
EGF is the founding member of the [[EGF-like domain|EGF-family of proteins]]. Members of this protein family have highly similar structural and functional characteristics. Besides EGF itself other family members include:<ref name=dreux>{{cite journal | author =Dreux AC, Lamb DJ. ''et al.''  | title =The epidermal growth factor receptors and their family of ligands: their putative role in atherogenesis | journal =Atherosclerosis | year=2006 | volume=186 | issue=1 | pages=38-53 | id = PMID 16076471}}</ref>
Epidermal growth factor can be found in urine, saliva, milk, and plasma.<ref name="isbn0-7216-0187-1">{{cite book | author = Cotran, Ramzi S. | author2 = Kumar, Vinay | author3 = Fausto, Nelson | author4 = Nelso Fausto | author5 = Robbins, Stanley L. | author6 = Abbas, Abul K. | others = | title = Robbins and Cotran pathologic basis of disease | edition = | language = | publisher = Elsevier Saunders | location = St. Louis, Mo | year = 2005 | isbn = 0-7216-0187-1 }}</ref>
The production of epidermal growth factor has been found to be stimulated by testosterone.


== Mechanism ==
[[File:MAPKpathway diagram.svg|thumb|left|Diagram showing key components of the [[MAPK/ERK pathway]]. In the diagram, "P" represents  [[phosphate]]. Note EGF at the very top.]]
EGF acts by binding with high [[Affinity (pharmacology)|affinity]] to [[epidermal growth factor receptor]] (EGFR) on the [[plasma membrane|cell surface]]. This stimulates ligand-induced dimerization,<ref name="pmid16107719">{{cite journal | vauthors = Dawson JP, Berger MB, Lin CC, Schlessinger J, Lemmon MA, Ferguson KM | title = Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface | journal = Mol. Cell. Biol. | volume = 25 | issue = 17 | pages = 7734–42 | year = 2005 | pmid = 16107719 | pmc = 1190273 | doi = 10.1128/MCB.25.17.7734-7742.2005 }}</ref> activating 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 [[biochemistry|biochemical]] changes within the cell – a rise in intracellular [[calcium]] levels, increased [[glycolysis]] and [[protein synthesis]], and increases in the [[gene expression|expression]] of certain [[gene]]s including the gene for EGFR – that ultimately lead to [[DNA replication|DNA synthesis]] and cell proliferation.<ref name="pmid6144184">{{cite journal | vauthors = Fallon JH, Seroogy KB, Loughlin SE, Morrison RS, Bradshaw RA, Knaver DJ, Cunningham DD | title = Epidermal growth factor immunoreactive material in the central nervous system: location and development | journal = Science | volume = 224 | issue = 4653 | pages = 1107–9 | date = June 1984 | pmid = 6144184 | doi = 10.1126/science.6144184 }}</ref>
== EGF-family / EGF-like domain ==
EGF is the founding member of the [[EGF-like domain|EGF-family of proteins]]. Members of this protein family have highly similar structural and functional characteristics. Besides EGF itself other family members include:<ref name="dreux">{{cite journal | vauthors = Dreux AC, Lamb DJ, Modjtahedi H, Ferns GA | title = The epidermal growth factor receptors and their family of ligands: their putative role in atherogenesis | journal = Atherosclerosis | volume = 186 | issue = 1 | pages = 38–53 | date = May 2006 | pmid = 16076471 | doi = 10.1016/j.atherosclerosis.2005.06.038}}</ref>
*[[Heparin-binding EGF-like growth factor]] (HB-EGF)
*[[Heparin-binding EGF-like growth factor]] (HB-EGF)
*[[TGF alpha|transforming growth factor-α]] (TGF-α)  
*[[TGF alpha|transforming growth factor-α]] (TGF-α)
*[[Amphiregulin]] (AR)  
*[[Amphiregulin]] (AR)
*[[Epiregulin]] (EPR)
*[[Epiregulin]] (EPR)
*[[Epigen]]  
*[[Epigen]]
*[[Betacellulin]] (BTC)
*[[Betacellulin]] (BTC)
*[[neuregulin-1]] (NRG1)
*[[neuregulin-1]] (NRG1)
*[[neuregulin|neuregulin-2]] (NRG2)
*[[neuregulin|neuregulin-2]] (NRG2)
*[[neuregulin|neuregulin-3]] (NRG3)
*[[neuregulin|neuregulin-3]] (NRG3)
*[[neuregulin|neureguline-4]] (NRG4).
*[[neuregulin|neuregulin-4]] (NRG4).


All family members contain one or more repeats of the [[conserved sequence|conserved]] amino acid sequence:
All family members contain one or more repeats of the [[conserved sequence|conserved]] amino acid sequence:


<font 16>'''[[cysteine|C]]X<sub>7</sub>[[cysteine|C]]X<sub>4-5</sub>[[cysteine|C]]X<sub>10-13</sub>[[cysteine|C]]X[[cysteine|C]]X<sub>8</sub>[[glycine|G]]X[[arginine|R]][[cysteine|C]]'''</font 16>
'''[[cysteine|C]]X<sub>7</sub>[[cysteine|C]]X<sub>4-5</sub>[[cysteine|C]]X<sub>10-13</sub>[[cysteine|C]]X[[cysteine|C]]X<sub>8</sub>[[glycine|G]]X[[arginine|R]][[cysteine|C]]'''


Where <font 16>'''X'''</font 16> represents any [[amino acid]].<ref name=dreux/>
Where '''X''' represents any [[amino acid]].<ref name=dreux/>


This sequence contains 6 [[cysteine]] residues that form three intramolecular [[disulphide bond]]s. 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.<ref name=harris>{{cite journal | author =Harris RC, Chung E, and Coffey RJ. | title =EGF receptor ligands | journal =Exp. Cell. Res. | year=2003 | volume=284 | issue=1 | pages=2-13 | id = PMID 12648462}}</ref>
This sequence contains 6 [[cysteine]] residues that form three intramolecular [[disulfide bond]]s. Disulfide bond formation generates three structural loops that are essential for high-affinity binding between members of the EGF-family and their [[cell-surface]] receptors.<ref name=harris>{{cite journal | vauthors = Harris RC, Chung E, Coffey RJ | title = EGF receptor ligands | journal = Exp. Cell Res. | volume = 284 | issue = 1 | pages = 2–13 | year = 2003 | pmid = 12648462 | doi = 10.1016/S0014-4827(02)00105-2 }}</ref>


==EGF as Therapeutic Protein==
==Interactions==
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.<ref>{{cite journal | author =Frew S, Rezaie R.''et al'' | title=India’s health biotech sector at a crossroads | journal =Nature Biotechnology | year=2007 | volume=25 | issue=4}}</ref> <ref name="cuba">{{cite journal | author =Lopez E, Acevedo B.''et al'' | title=Development of Cuban Biotechnology | journal =Journal of Commercial Biotechnology | year=2002 | volume=9 | issue=2}}</ref>  EGF is also used in a burn treatment cream product, Hebermin, manufactured by Heber Biotec S. A. in Cuba.<ref name="cuba"/>
Epidermal growth factor has been shown to [[Protein-protein interaction|interact]] with [[epidermal growth factor receptor]].<ref name="pmid12093292">{{cite journal | vauthors = Stortelers C, Souriau C, van Liempt E, van de Poll ML, van Zoelen EJ | title = Role of the N-terminus of epidermal growth factor in ErbB-2/ErbB-3 binding studied by phage display | journal = Biochemistry | volume = 41 | issue = 27 | pages = 8732–41 | date = July 2002 | pmid = 12093292 | doi = 10.1021/bi025878c }}</ref><ref name="pmid10085134">{{cite journal | vauthors = Wong L, Deb TB, Thompson SA, Wells A, Johnson GR | title = A differential requirement for the COOH-terminal region of the epidermal growth factor (EGF) receptor in amphiregulin and EGF mitogenic signaling | journal = J. Biol. Chem. | volume = 274 | issue = 13 | pages = 8900–9 | date = March 1999 | pmid = 10085134 | doi = 10.1074/jbc.274.13.8900 }}</ref>


==References==
==Medical uses==
{{reflist|2}}
[[Recombinant protein|Recombinant]] human epidermal growth factor, sold under the brand name Heberprot-P, is used to treat [[diabetic foot ulcer]]s. It can be given by injection into the wound site,<ref name=Ber2013>{{cite journal |title=Heberprot-P: a novel product for treating advanced diabetic foot ulcer |last=Berlanga |first=J. |last2=Fernández |first2=J. I. |last3=López |first3=E. |last4=López |first4=P. A. |last5=del Río |first5=A. |last6=Valenzuela |first6=C. |last7=Baldomero |first7=J. |last8=Muzio |first8=V. |last9=Raíces |first9=M. |last10=Silva |first10=R. |last11=Acevedo |first11=B. E. |last12=Herrera |first12=L. |journal=[[MEDICC|MEDICC Review]] |year=2013 |volume=15 |issue=1 |pages=11–15 |pmid=23396236 |doi=10.1590/s1555-79602013000100004}}</ref> or may be used topically.<ref>{{cite journal|last1=Yang|first1=S|last2=Geng|first2=Z|last3=Ma|first3=K|last4=Sun|first4=X|last5=Fu|first5=X|title=Efficacy of Topical Recombinant Human Epidermal Growth Factor for Treatment of Diabetic Foot Ulcer: A Systematic Review and Meta-Analysis.|journal=The International Journal of Lower Extremity Wounds|date=June 2016|volume=15|issue=2|pages=120–5|pmid=27151755|doi=10.1177/1534734616645444}}</ref> Tentative evidence shows improved wound healing.<ref name=Mar2015>{{cite journal|last1=Martí-Carvajal|first1=AJ|last2=Gluud|first2=C|last3=Nicola|first3=S|last4=Simancas-Racines|first4=D|last5=Reveiz|first5=L|last6=Oliva|first6=P|last7=Cedeño-Taborda|first7=J|title=Growth factors for treating diabetic foot ulcers.|journal=The Cochrane Database of Systematic Reviews|date=28 October 2015|volume=10|pages=CD008548|pmid=26509249|doi=10.1002/14651858.CD008548.pub2}}</ref> Safety has been poorly studied.<ref name=Mar2015/>


==External links==
== References ==
*EGF at the [http://www.hprd.org/protein/00578 Human Protein Reference Database].
{{reflist|35em}}
* {{MeshName|Epidermal+growth+factor}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin|35em}}
{{PBB_Further_reading
*{{cite journal | vauthors = Boonstra J, Rijken P, Humbel B, Cremers F, Verkleij A, van Bergen en Henegouwen P | title = The epidermal growth factor | journal = Cell Biol. Int. | volume = 19 | issue = 5 | pages = 413–30 | year = 1995 | pmid = 7640657 | doi = 10.1006/cbir.1995.1086 }}
| citations =
*{{cite journal | author = Dvorak B | title = Epidermal growth factor and necrotizing enterocolitis | journal = Clinics in Perinatology | volume = 31 | issue = 1 | pages = 183–92 | year = 2004 | pmid = 15183666 | doi = 10.1016/j.clp.2004.03.015 }}
*{{cite journal | author=Boonstra J, Rijken P, Humbel B, ''et al.'' |title=The epidermal growth factor. |journal=Cell Biol. Int. |volume=19 |issue= 5 |pages= 413-30 |year= 1995 |pmid= 7640657 |doi= }}
*{{cite journal | author = Howell WM | title = Epidermal growth factor gene polymorphism and development of cutaneous melanoma | journal = J. Invest. Dermatol. | volume = 123 | issue = 4 | pages = xx–xxi | year = 2004 | pmid = 15373802 | doi = 10.1111/j.0022-202X.2004.23308.x }}
*{{cite journal | author=Dvorak B |title=Epidermal growth factor and necrotizing enterocolitis. |journal=Clinics in perinatology |volume=31 |issue= 1 |pages= 183-92 |year= 2004 |pmid= 15183666 |doi= 10.1016/j.clp.2004.03.015 }}
*{{cite journal | author=Howell WM |title=Epidermal growth factor gene polymorphism and development of cutaneous melanoma. |journal=J. Invest. Dermatol. |volume=123 |issue= 4 |pages= xx-xxi |year= 2004 |pmid= 15373802 |doi= 10.1111/j.0022-202X.2004.23308.x }}
}}
{{refend}}
{{refend}}


== External links ==
{{Commons category|Epidermal growth factor, EGF}}
* [http://www.zbfarm.com Shaanxi Zhongbang Pharma-Tech Co., Ltd.-Supply of Epidermal Growth Factor]
* EGF at the [http://www.hprd.org/protein/00578 Human Protein Reference Database].
* {{MeshName|Epidermal+growth+factor}}
* [http://www.ebi.ac.uk/biomodels-main/static-pages.do?page=ModelMonth%252FAugust2006%2FBIOMD0000000048_MM EGF model in BioModels database]


{{PDB Gallery|geneid=1950}}
{{Signaling proteins}}
{{Signaling proteins}}
{{Gastrointestinal hormones}}
{{Gastrointestinal hormones}}
{{Growth factor receptor modulators}}


[[Category:Growth factors]]
[[Category:Growth factors]]
[[Category:Morphogens]]
[[Category:Morphogens]]
[[de:Epidermaler Wachstumsfaktor]]
[[fr:Facteur de croissance épidermique]]
[[ja:上皮成長因子]]
[[zh:表皮生长因子]]
{{WikiDoc Sources}}

Revision as of 16:37, 4 October 2017

Not to be confused with EF-G.
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Epidermal growth factor (EGF) stimulates cell growth and differentiation by binding to its receptor, EGFR. Human EGF is a 6-kDa protein[1] with 53 amino acid residues and three intramolecular disulfide bonds.[2]

EGF was originally described as a secreted peptide found in the submaxillary glands of mice and in human urine. EGF has since been found in many human tissues including submandibular gland, parotid gland.[3] Initially, human EGF was known as urogastrone.[4]

Function

EGF [binding to EGFR] results in cellular proliferation, differentiation, and survival.[5]

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.[3]

Biological sources

Epidermal growth factor can be found in urine, saliva, milk, and plasma.[6] The production of epidermal growth factor has been found to be stimulated by testosterone.

Mechanism

File:MAPKpathway diagram.svg
Diagram showing key components of the MAPK/ERK pathway. In the diagram, "P" represents phosphate. Note EGF at the very top.

EGF acts by binding with high affinity to epidermal growth factor receptor (EGFR) on the cell surface. This stimulates ligand-induced dimerization,[7] activating 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.[8]

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:[9]

All family members contain one or more repeats of the conserved amino acid sequence:

CX7CX4-5CX10-13CXCX8GXRC

Where X represents any amino acid.[9]

This sequence contains 6 cysteine residues that form three intramolecular disulfide bonds. Disulfide bond formation generates three structural loops that are essential for high-affinity binding between members of the EGF-family and their cell-surface receptors.[10]

Interactions

Epidermal growth factor has been shown to interact with epidermal growth factor receptor.[11][12]

Medical uses

Recombinant human epidermal growth factor, sold under the brand name Heberprot-P, is used to treat diabetic foot ulcers. It can be given by injection into the wound site,[13] or may be used topically.[14] Tentative evidence shows improved wound healing.[15] Safety has been poorly studied.[15]

References

  1. ↑ Harris RC, Chung E, Coffey RJ (March 2003). "EGF receptor ligands". Experimental Cell Research. 284 (1): 2–13. doi:10.1016/S0014-4827(02)00105-2. PMID 12648462.
  2. ↑ Carpenter G, Cohen S (May 1990). "Epidermal growth factor". The Journal of Biological Chemistry. 265 (14): 7709–12. PMID 2186024.
  3. ↑ 3.0 3.1 Venturi S, Venturi M (2009). "Iodine in evolution of salivary glands and in oral health". Nutrition and Health. 20 (2): 119–134. doi:10.1177/026010600902000204. PMID 19835108.
  4. ↑ Hollenberg, MD; Gregory, H (May 1980). "Epidermal growth factor-urogastrone: biological activity and receptor binding of derivatives". Molecular Pharmacology. 17 (3): 314–20. PMID 6248761.
  5. ↑ Herbst RS (2004). "Review of epidermal growth factor receptor biology". International Journal of Radiation Oncology, Biology, Physics. 59 (2 Suppl): 21–6. doi:10.1016/j.ijrobp.2003.11.041. PMID 15142631.
  6. ↑ Cotran, Ramzi S.; Kumar, Vinay; Fausto, Nelson; Nelso Fausto; Robbins, Stanley L.; Abbas, Abul K. (2005). Robbins and Cotran pathologic basis of disease. St. Louis, Mo: Elsevier Saunders. ISBN 0-7216-0187-1.
  7. ↑ Dawson JP, Berger MB, Lin CC, Schlessinger J, Lemmon MA, Ferguson KM (2005). "Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface". Mol. Cell. Biol. 25 (17): 7734–42. doi:10.1128/MCB.25.17.7734-7742.2005. PMC 1190273. PMID 16107719.
  8. ↑ Fallon JH, Seroogy KB, Loughlin SE, Morrison RS, Bradshaw RA, Knaver DJ, Cunningham DD (June 1984). "Epidermal growth factor immunoreactive material in the central nervous system: location and development". Science. 224 (4653): 1107–9. doi:10.1126/science.6144184. PMID 6144184.
  9. ↑ 9.0 9.1 Dreux AC, Lamb DJ, Modjtahedi H, Ferns GA (May 2006). "The epidermal growth factor receptors and their family of ligands: their putative role in atherogenesis". Atherosclerosis. 186 (1): 38–53. doi:10.1016/j.atherosclerosis.2005.06.038. PMID 16076471.
  10. ↑ Harris RC, Chung E, Coffey RJ (2003). "EGF receptor ligands". Exp. Cell Res. 284 (1): 2–13. doi:10.1016/S0014-4827(02)00105-2. PMID 12648462.
  11. ↑ Stortelers C, Souriau C, van Liempt E, van de Poll ML, van Zoelen EJ (July 2002). "Role of the N-terminus of epidermal growth factor in ErbB-2/ErbB-3 binding studied by phage display". Biochemistry. 41 (27): 8732–41. doi:10.1021/bi025878c. PMID 12093292.
  12. ↑ Wong L, Deb TB, Thompson SA, Wells A, Johnson GR (March 1999). "A differential requirement for the COOH-terminal region of the epidermal growth factor (EGF) receptor in amphiregulin and EGF mitogenic signaling". J. Biol. Chem. 274 (13): 8900–9. doi:10.1074/jbc.274.13.8900. PMID 10085134.
  13. ↑ Berlanga, J.; Fernández, J. I.; López, E.; López, P. A.; del Río, A.; Valenzuela, C.; Baldomero, J.; Muzio, V.; Raíces, M.; Silva, R.; Acevedo, B. E.; Herrera, L. (2013). "Heberprot-P: a novel product for treating advanced diabetic foot ulcer". MEDICC Review. 15 (1): 11–15. doi:10.1590/s1555-79602013000100004. PMID 23396236.
  14. ↑ Yang, S; Geng, Z; Ma, K; Sun, X; Fu, X (June 2016). "Efficacy of Topical Recombinant Human Epidermal Growth Factor for Treatment of Diabetic Foot Ulcer: A Systematic Review and Meta-Analysis". The International Journal of Lower Extremity Wounds. 15 (2): 120–5. doi:10.1177/1534734616645444. PMID 27151755.
  15. ↑ 15.0 15.1 Martí-Carvajal, AJ; Gluud, C; Nicola, S; Simancas-Racines, D; Reveiz, L; Oliva, P; Cedeño-Taborda, J (28 October 2015). "Growth factors for treating diabetic foot ulcers". The Cochrane Database of Systematic Reviews. 10: CD008548. doi:10.1002/14651858.CD008548.pub2. PMID 26509249.

Further reading

External links

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