Epidermal Growth Factor Receptor

EGFR epidermal growth factor receptor exists on the cell surface and is activated by binding of its critical ligands, within epidermal growth factor and transforming growth factor TGF note, a full list regarding the ligands can activate EGFR and other members regarding the ErbB family is provided within the ErbB article. ErbB2 has no known direct activating ligand, and should be in an activated state constitutively or grow to active upon heterodimerization with other family members for example EGFR. Upon activation by its growth factor ligands, EGFR undergoes a transition from an inactive monomeric shape to an active homodimer - consequently there is some evidence that preformed inactive dimers shall also exist prior to ligand binding[citation needed]. In addition to forming homodimers subsequent to ligand binding, EGFR shall pair with another member regarding the ErbB receptor family, for example ErbB2 or Her2 or neu, to make an activated heterodimer. There molecule diagram evidence to suggest that clusters of activated EGFRs form, consequently it remains unclear whether this clustering is important for activation itself or occurs subsequent to activation of lone dimers[citation needed].

Diagram regarding the EGF receptor highlighting important domains. EGFR dimerization stimulates its intrinsic intracellular protein-tyrosine kinase activity. Like a result, autophosphorylation of multiple tyrosine Y residues within the C-terminal website of EGFR occurs. These with Y992, Y1045, Y1068, Y1148 and Y1173 as shown within the diagram to left. This autophosphorylation elicits downstream activation and signaling by multiple other proteins that associate with the phosphorylated tyrosines through their own phosphotyrosine-binding SH2 domains.

These downstream signaling proteins initiate multiple signal transduction cascades, principally the MAPK, Akt and JNK pathways, leading to DNA synthesis and cell proliferation. Such proteins modulate phenotypes for example cell migration, adhesion, and proliferation. Activation regarding the receptor is important for the innate immune response in person skin. The kinase website of EGFR should possibly cross-phosphorylate tyrosine residues of other receptors it is aggregated with, and can itself be activated in that manner. Clinical applications.

Mutations that lead to EGFR over[removed]known as upregulation or overactivity have been associated with a many cancers, within lung cancer, anal cancers and glioblastoma multiforme. In this latter case a more or fewer critical mutation of EGFR, called EGFRvIII is often observed. Mutations, amplifications or misregulations of EGFR or family members are implicated in about 30% of all epithelial cancers. Mutations involving EGFR should lead to its constant activation which should result in uncontrolled cell division a predisposition for cancer. Consequently, mutations of EGFR have been identified in multiple variations of cancer, and it is the target of an expanding class of anticancer therapies.

The identification of EGFR as an oncogene has led to development of anticancer therapeutics directed against EGFR, within gefitinib and erlotinib for lung cancer, and cetuximab for colon cancer. Many therapeutic approaches are aimed at the EGFR. Cetuximab and panitumumab are examples of monoclonal antibody inhibitors. However the former is regarding the IgG1 type, the latter regarding the IgG2 type; consequences on antibody dependent cellular cytotoxicity should be barely different. Other monoclonals in clinical development are zalutumumab, nimotuzumab, and matuzumab.

Gefitinib, erlotinib, and lapatinib mixed EGFR and ERBB2 inhibitor are examples of mini molecule kinase inhibitors. The monoclonal antibodies block the extracellular ligand binding domain. With the binding location blocked, signal molecules can no detailed attach there and activate the tyrosine kinase. Another method is creating use of mini molecules to inhibit the EGFR tyrosine kinase, that is on the cytoplasmic side regarding the receptor. Without kinase activity, EGFR is unable to activate itself, that is a prerequisite for binding of downstream adaptor proteins.

Ostensibly by halting the signaling cascade in cells that rely on this pathway for growth, tumor proliferation and migration is diminished. There exists multiple quantitative methods available that use protein phosphorylation detection to identify EGFR family inhibitors. Efficient conversion of strongly absorbed light by plasmonic gold nanoparticles to heat life and their easy bioconjugation suggest their use as selective photothermal agents in molecular cancer cell targeting. 3 oral squamous carcinoma cell lines HSC 313 and HOC 4 Clone 8 and one benign epithelial cell line HaCaT were incubated with anti-epithelial growth factor receptor EGFR antibody conjugated gold nanoparticles and then exposed to continuous visible argon ion laser at 514nm. It is located that the malignant cells need fewer than 1/2 the laser life to be killed than the benign cells subsequent to incubation with anti-EGFR antibody conjugated Au nanoparticles.

No photothermal destruction is observed for all variations of cells within the absence of nanoparticles at 4 times life compulsory to kill the malignant cells with anti-EGFR or Au conjugates bonded. Au nanoparticles thus release a novel class of selective photothermal agents creating use of a CW laser at little powers. In July 2007 it was discovered that the blood clotting protein fibrinogen activates EGFR, thereby blocking regrowth of injured neuronal cells within the spine. Other natural inhibitors with potato carboxypeptidase inhibitor PCI, which contains a mini cysteine-rich module, called a T-knot scaffold, that is shared by multiple different protein families, within the EGF family. Structural similarities with these factors can explain the antagonistic effect of PCI.

New drugs for example Tarceva directly target the EGFR. Patients have been divided into EGFR positive and negative, based upon whether a tissue test shows a mutation. EGFR positive patients have shown an impressive 60% response rate which exceeds the response rate for conventional chemotherapy. Epidermal growth factor receptor was shown to interact with PLCG1, NCK1, Janus kinase 2, CDC25A, MUC1, Caveolin 1, STAT5A, PTPN1, CRK, SHC1, Beta-catenin, PTPN11, PTPN6, STAT1, CBLC, Src, Androgen receptor, STAT3, GRB14, Grb2, PLSCR1, Wiskott-Aldrich syndrome protein, SH2D3A, Epidermal growth factor, CBLB, Cbl gene, ARF4, PKC alpha, SOS1, SH3KBP1, Caveolin 3, Decorin, NCK2 and Ubiquitin C. Review of epidermal growth factor receptor biology.

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A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. United States 21 3? 3158. ^ Oneyama, Chitose; Nakano Hirofumi, Sharma Sreenath V Mar. UCS15A, a novel mini molecule, SH3 domain-mediated protein-protein interaction blocking drug. Oncogene England 21 13? 203750.

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A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells. UNITED STATES 269 12? 901923. ^ Lowenstein, E J; Daly R J, Batzer A G, Li W, Margolis B, Lammers R, Ullrich A, Skolnik E Y, Bar-Sagi D, Schlessinger J Aug. The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell UNITED STATES 70 3? 43142.

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Role regarding the N-terminus of epidermal growth factor in ErbB-2 or ErbB-3 binding studied by phage display. Biochemistry United States 41 27? 873241. ^ a be Ettenberg, S A; Keane M M, Nau M M, Frankel M, Wang L M, Pierce J H, Lipkowitz S Mar. cbl-b inhibits epidermal growth factor receptor signaling. Oncogene ENGLAND 18 10? 185566.

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MeSH Epidermal Growth Factor Receptor. Receptors for epidermal growth factor and other polypeptide mitogens. Boonstra J, Rijken P, Humbel B, et al. The epidermal growth factor. The EGF receptor: a nexus for trafficking and signaling.

Bioessays 22 8? 697707. 1002 or 1521-1878 200008 22:8 and lt;697::AID-BIES3 and gt;3. Epidermal growth factor receptor EGFR transactivation by estrogen via the G-protein-coupled receptor, GPR30: a novel signaling pathway with potential significance for breast cancer. 1016 or S0960-0760 01 00190-X. Protein tyrosine phosphatases: dephosphorylating the epidermal growth factor receptor.

1080 or 15216540210811. Di Fiore PP, Scita G 2002. Eps8 within the midst of GTPases. 1016 or S1357-2725 02 00064-X. Benaim G, Villalobo A 2002.

Phosphorylation of calmodulin. Functional implications. Functional implication regarding the interaction between EGF receptor and c-Src. Anderson NL, Anderson NG 2003. The person plasma proteome: history, character, and diagnostic prospects.

Cell Proteomics two 11? 84567. Kari C, Chan TO, Rocha de Quadros M, Rodeck U 2003. Targeting the epidermal growth factor receptor in cancer: apoptosis takes center stage. Bonaccorsi L, Muratori M, Carloni V, et al. Androgen receptor and prostate cancer invasion.

Reiter JL, Maihle NJ 2003. Characterization and expression of novel 60-kDa and 110-kDa EGFR isoforms in person placenta. Adams TE, McKern NM, Ward CW 2005. Signalling by the kind two insulin-like growth factor receptor: interplay with the epidermal growth factor receptor. Growth Factors 22 2? 8995.

Active and inactive conformations regarding the epidermal growth factor receptor. Chao C, Hellmich MR 2005. Bi-directional signaling between gastrointestinal peptide hormone receptors and epidermal growth factor receptor. Growth Factors 22 4? 2618. 1080 or 08977190412331286900.

Carlsson J, Ren ZP, Wester K, et al. Planning for intracavitary anti-EGFR radionuclide therapy of gliomas. Literature review and data on EGFR expression. 1007 or s11060-005-7410-z. Scartozzi M, Pierantoni C, Berardi R, et al.

Epidermal growth factor receptor: a promising therapeutic target for colorectal cancer. Prudkin L, Wistuba II 2006. Epidermal growth factor receptor abnormalities in lung cancer. Pathogenetic and clinical implications. Annals of diagnostic pathology 10 5? 30615.

Ahmed SM, Salgia R 2007. Epidermal growth factor receptor mutations and susceptibility to targeted therapy in lung cancer. Respirology 11 6? 68792. Zhang X, Chang A 2007. Somatic mutations regarding the epidermal growth factor receptor and non-small-cell lung cancer.

Cohenuram M, Saif MW 2007. Epidermal growth factor receptor inhibition strategies in pancreatic cancer: past, present and the future. Mellinghoff IK, Cloughesy TF, Mischel PS 2007. PTEN-mediated resistance to epidermal growth factor receptor kinase inhibitors. The epidermal growth factor receptor in malignant gliomas: pathogenesis and therapeutic implications.

1ivo: Crystal Structure regarding the Complex of Person Epidermal Growth Factor and Receptor Extracellular Domains. 1m14: Tyrosine Kinase Website from Epidermal Growth Factor Receptor. 1m17: Epidermal Growth Factor Receptor tyrosine kinase website with 4-anilinoquinazoline inhibitor erlotinib. 1mox: Crystal Structure of Person Epidermal Growth Factor Receptor residues 1-501 in complex with TGF-alpha. 1nql: Structure regarding the extracellular website of person epidermal growth factor EGF receptor in an inactive little pH complex with EGF.

1xkk: EGFR kinase website complexed with a quinazoline inhibitor- GW572016. 1yy9: Structure regarding the extracellular website regarding the epidermal growth factor receptor in complex with the Fab fragment of cetuximab or Erbitux or IMC-C225. 1z9i: A Structural Model for the Membrane-Bound Shape regarding the Juxtamembrane Website regarding the Epidermal Growth Factor Receptor. 2gs2: Crystal Structure regarding the active EGFR kinase website. 2gs6: Crystal Structure regarding the active EGFR kinase website in complex with an ATP analog-peptide conjugate.

2gs7: Crystal Structure regarding the inactive EGFR kinase website in complex with AMP-PNP. 2itn: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN G719S MUTATION IN COMPLEX WITH AMP-PNP. 2ito: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN G719S MUTATION IN COMPLEX WITH IRESSA. 2itp: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN G719S MUTATION IN COMPLEX WITH AEE788. 2itq: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN G719S MUTATION IN COMPLEX WITH AFN941.

2itt: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN COMPLEX WITH AEE788. 2itu: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN COMPLEX WITH AFN941. 2itv: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN COMPLEX WITH AMP-PNP. 2itw: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN COMPLEX WITH AFN941. 2itx: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN COMPLEX WITH AMP-PNP.

2ity: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN COMPLEX WITH IRESSA. 2itz: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN L858R MUTATION IN COMPLEX WITH IRESSA. 2j5e: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN COMPLEX WITH AN IRREVERSIBLE INHIBITOR 13-JAB. 2j5f: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN COMPLEX WITH AN IRREVERSIBLE INHIBITOR 34-JAB. 2j6m: CRYSTAL STRUCTURE OF EGFR KINASE DOMAIN IN COMPLEX WITH AEE788.

Protein kinases: tyrosine kinases EC 2. Receptor tyrosine kinases EC 2. EGFR ERBB2 ERBB3 ERBB4. Insulin receptor family. CSF1R FLT3 KIT PDGFR PDGFRA, PDGFRB.

FGFR1 FGFR2 FGFR3 FGFR4. VEGF receptors family. VEGFR1 VEGFR2 VEGFR3 VEGFR4. EPHA1 EPHA2 EPHA3 EPHA4 EPHA5 EPHA6 EPHA7 EPHA8 EPHB1 EPHB2 EPHB3 EPHB4 EPHB5 EPHB6 EPHX. AATYK receptor family.

Non-receptor tyrosine kinases EC 2. Neoplasm: Oncogenes or Proto-oncogenes. receptor or tyrosine kinases. ErbB or c-ErbB HER2 or neu, Her 4 - c-Kit - c-Met - c-Ret - Flt3. MAPK or ERK pathway c-Ras or HRAS, c-Raf.

Akt or PKB signaling pathway c-Akt. Wnt signaling pathway Beta-catenin. Nucleus or Transcription factors. AP-1 c-Fos, c-Jun - c-Myc - c-Mdm2. c-Bcl-2 - Notch - Stathmin.

see also tumor suppressor genes. Receptors: growth factor receptors. Low affinity or p75 - high affinity Trk TrkA, TrkB, TrkC - Ciliary neurotrophic factor. Insulin-like growth factor two - Insulin-like growth factor 2. Stem cell factor - Erythropoietin.

TGF-beta 1, 3 - Activin 1, 3 - Bone morphogenetic protein 1, 3. Hepatocyte growth factor - ErbB or Epidermal growth factor - Fibroblast growth factor 1, 2, 3, 5 - Platelet-derived growth factor A, Be - VEGF 1, 2, 4. see also growth factors. Categories: Person proteins | Tyrosine kinase receptors | OncogenesHidden categories: All articles with unsourced statements | Articles with unsourced statements from October 2009 | Articles with unsourced statements from December 2009.