Epidermal Growth Factor Receptor Structure
Published by Anonymous on 2007/9/29 (2396 reads)
1: Ugeskr Laeger. 2006 Jun 12;168(24):2354-61.
[Mutations in the epidermal growth factor receptor: structure and biological function in human tumors]
[Article in Danish]
Pedersen MW, Poulsen HS.
H:S Rigshospitalet, Finsencentret, Strålebiologisk Laboratorium, Afsnit 6321, DK-2100 København Ø.
The epidermal growth factor receptor (EGFR) plays an important role in the regulation of normal cell proliferation, differentiation and survival. For this reason EGFR status is often altered in a range of human tumor types and generally correlates with a poor prognosis. In recent years a number of mutations in the EGFR gene have been noted that lead to the expression of overactive or constitutively active aberrant receptors. These receptors have been shown to participate actively in the process of tumor genesis. This review provides an overview of the structure of these mutations and their biological function in human tumors plus the potentials of anticancer therapy.
Publication Types:
English Abstract
Research Support, Non-U.S. Gov't
Review
PMID: 16822420 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Anticancer Res. 2001 Jul-Aug;21(4A):2769-75.
Epidermal growth factor receptor structure, regulation, mitogenic signalling and effects of activation.
Boulougouris P, Elder J.
Academic Department of Surgery, Keele University, Stoke-on Trent, Staffordshire, UK.
The biological effects of epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha) are mediated by an interaction with a specific cell surface receptor having both intra- and extracellular domains. The structure of the intracellular domain can be closely aligned with retroviral protein tyrosine kinases. Upon ligand-binding there is a change in conformation of the extracellular domain, the receptor being converted to dimeric. Dimeric receptor has a higher rate of catalysis than monomeric and rapidly becomes phosphorylated. This form of the receptor now associates with and phosphorylates enzymes such as phospholipase-C, altering their catalytic activity and subcellular distribution This system appears to stimulate the effects of epidermal growth factor receptor(EGFr) activation, notably proliferation, morphology, paracrine effects and differentation.
Publication Types:
Review
PMID: 11724353 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Nippon Rinsho. 1992 Aug;50(8):1885-92.
[Epidermal growth factor and its receptor: the structure and function]
[Article in Japanese]
Gamou S, Shimizu N.
Department of Molecular Biology, Keio University School of Medicine.
Epidermal growth factor (EGF) binds to the specific membrane receptor and subsequently activates the signal transduction pathway through intrinsic tyrosine kinase activity. To elucidate the mechanism in which structural alteration of the EGF may affect functional properties including its receptor binding ability, site-directed mutagenesis has been employed. The functional significance of structural characteristics of the EGF receptor has been studied also by mutant receptor constructs in the transfected cells. Recent progress on the studies of the EGF and EGF receptor interaction are reviewed.
Publication Types:
English Abstract
Review
PMID: 1433980 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Mol Cell Endocrinol. 1990 May 7;70(3):205-16.
Structure, function and transforming potential of the epidermal growth factor receptor.
Velu TJ.
Laboratory of Cellular Oncology, National Cancer Institute, NIH, Bethesda, MD 20892.
Publication Types:
Review
PMID: 2193842 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Cytotechnology. 1990 May;3(3):279-93.
Monoclonal antibodies to epidermal growth factor receptors in studies of receptor structure and function.
Kawamoto T, Sato GH, Takahashi K, Nishi M, Taniguchi S, Sato JD.
Department of Biochemistry, Okayama University Dental School, Japan.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 1366662 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Contrib Gynecol Obstet. 1989;17:44-8.
Epidermal growth factor receptor proto-oncogene. Structure, evolution of properties of receptor mutants.
Schlessinger J.
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
Publication Types:
Review
PMID: 2650999 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Biochimie. 1984 Jul-Aug;66(7-8):515-30.
[Epidermal growth factor: structure, location, phosphorylation and regulation of its receptor]
[Article in French]
St-Arnaud R, Chabot JG, Pelletier G, Labrie F, Walker P.
Epidermal growth factor (EGF) is a Mr 6045 polypeptide first characterized for its ability to stimulate mitogenesis in epidermal and epithelial cells. The first step in the action of the growth factor is its binding to specific, high affinity membrane receptors. These receptors have been studied in a number of tissues and cell culture lines. The level of EGF receptors is modulated by many agents. EGF down-regulates its receptor. In addition, the number of EGF receptors is decreased by other growth factors (platelet-derived growth factor; transforming growth factor), by many tumor promoters and by viral transformation. Several hormones also can regulate EGF binding in its target tissues.
Publication Types:
English Abstract
Research Support, Non-U.S. Gov't
Review
PMID: 6099148 [PubMed - indexed for MEDLINE]
[Mutations in the epidermal growth factor receptor: structure and biological function in human tumors]
[Article in Danish]
Pedersen MW, Poulsen HS.
H:S Rigshospitalet, Finsencentret, Strålebiologisk Laboratorium, Afsnit 6321, DK-2100 København Ø.
The epidermal growth factor receptor (EGFR) plays an important role in the regulation of normal cell proliferation, differentiation and survival. For this reason EGFR status is often altered in a range of human tumor types and generally correlates with a poor prognosis. In recent years a number of mutations in the EGFR gene have been noted that lead to the expression of overactive or constitutively active aberrant receptors. These receptors have been shown to participate actively in the process of tumor genesis. This review provides an overview of the structure of these mutations and their biological function in human tumors plus the potentials of anticancer therapy.
Publication Types:
English Abstract
Research Support, Non-U.S. Gov't
Review
PMID: 16822420 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Anticancer Res. 2001 Jul-Aug;21(4A):2769-75.
Epidermal growth factor receptor structure, regulation, mitogenic signalling and effects of activation.
Boulougouris P, Elder J.
Academic Department of Surgery, Keele University, Stoke-on Trent, Staffordshire, UK.
The biological effects of epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha) are mediated by an interaction with a specific cell surface receptor having both intra- and extracellular domains. The structure of the intracellular domain can be closely aligned with retroviral protein tyrosine kinases. Upon ligand-binding there is a change in conformation of the extracellular domain, the receptor being converted to dimeric. Dimeric receptor has a higher rate of catalysis than monomeric and rapidly becomes phosphorylated. This form of the receptor now associates with and phosphorylates enzymes such as phospholipase-C, altering their catalytic activity and subcellular distribution This system appears to stimulate the effects of epidermal growth factor receptor(EGFr) activation, notably proliferation, morphology, paracrine effects and differentation.
Publication Types:
Review
PMID: 11724353 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Nippon Rinsho. 1992 Aug;50(8):1885-92.
[Epidermal growth factor and its receptor: the structure and function]
[Article in Japanese]
Gamou S, Shimizu N.
Department of Molecular Biology, Keio University School of Medicine.
Epidermal growth factor (EGF) binds to the specific membrane receptor and subsequently activates the signal transduction pathway through intrinsic tyrosine kinase activity. To elucidate the mechanism in which structural alteration of the EGF may affect functional properties including its receptor binding ability, site-directed mutagenesis has been employed. The functional significance of structural characteristics of the EGF receptor has been studied also by mutant receptor constructs in the transfected cells. Recent progress on the studies of the EGF and EGF receptor interaction are reviewed.
Publication Types:
English Abstract
Review
PMID: 1433980 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Mol Cell Endocrinol. 1990 May 7;70(3):205-16.
Structure, function and transforming potential of the epidermal growth factor receptor.
Velu TJ.
Laboratory of Cellular Oncology, National Cancer Institute, NIH, Bethesda, MD 20892.
Publication Types:
Review
PMID: 2193842 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Cytotechnology. 1990 May;3(3):279-93.
Monoclonal antibodies to epidermal growth factor receptors in studies of receptor structure and function.
Kawamoto T, Sato GH, Takahashi K, Nishi M, Taniguchi S, Sato JD.
Department of Biochemistry, Okayama University Dental School, Japan.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 1366662 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Contrib Gynecol Obstet. 1989;17:44-8.
Epidermal growth factor receptor proto-oncogene. Structure, evolution of properties of receptor mutants.
Schlessinger J.
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
Publication Types:
Review
PMID: 2650999 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Biochimie. 1984 Jul-Aug;66(7-8):515-30.
[Epidermal growth factor: structure, location, phosphorylation and regulation of its receptor]
[Article in French]
St-Arnaud R, Chabot JG, Pelletier G, Labrie F, Walker P.
Epidermal growth factor (EGF) is a Mr 6045 polypeptide first characterized for its ability to stimulate mitogenesis in epidermal and epithelial cells. The first step in the action of the growth factor is its binding to specific, high affinity membrane receptors. These receptors have been studied in a number of tissues and cell culture lines. The level of EGF receptors is modulated by many agents. EGF down-regulates its receptor. In addition, the number of EGF receptors is decreased by other growth factors (platelet-derived growth factor; transforming growth factor), by many tumor promoters and by viral transformation. Several hormones also can regulate EGF binding in its target tissues.
Publication Types:
English Abstract
Research Support, Non-U.S. Gov't
Review
PMID: 6099148 [PubMed - indexed for MEDLINE]
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