Epidermal Growth Factor Tethered through Coiled-Coil Interactions Induces Cell Surface Receptor Phosphorylation

2009 ◽  
Vol 20 (8) ◽  
pp. 1569-1577 ◽  
Author(s):  
Cyril Boucher ◽  
Benoît Liberelle ◽  
Mario Jolicoeur ◽  
Yves Durocher ◽  
Gregory De Crescenzo
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Surface ◽  
Coiled Coil ◽  
Cell Surface Receptor ◽  
Receptor Phosphorylation ◽  
Surface Receptor ◽  
Epidermal Growth

scholarly journals Specific radiolabeling of a cell surface receptor for epidermal growth factor.

1977 ◽  
Vol 74 (7) ◽  
pp. 2790-2794 ◽  
Author(s):  
M. Das ◽  
T. Miyakawa ◽  
C. F. Fox ◽  
R. M. Pruss ◽  
A. Aharonov ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cell Surface ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
A Cell ◽  
Epidermal Growth

scholarly journals Tissue distribution of mRNA for heparin-binding epidermal growth factor

1992 ◽  
Vol 287 (3) ◽  
pp. 681-684 ◽  
Author(s):  
T J Vaughan ◽  
J C Pascall ◽  
K D Brown
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Diphtheria Toxin ◽  
Cell Surface Receptor ◽  
Heparin Binding ◽  
Reverse Transcription Pcr ◽  
Body Tissues ◽  
Wide Range ◽  
Surface Receptor ◽  
Epidermal Growth

Heparin-binding epidermal growth factor (HB-EGF) is a recently identified member of the EGF family. Mature HB-EGF is processed from a larger transmembrane precursor which can itself act as a cell-surface receptor for the internalization of diphtheria toxin into eukaryotic cells. However, to date there is no information available on the distribution of HB-EGF in mammalian tissues. We have therefore used reverse-transcription PCR to analyse the expression of HB-EGF mRNA in a wide range of tissues. HB-EGF transcripts were detected in RNA isolated from 15 of the 22 tissues obtained from adult pigs, which is consistent with the ability of diphtheria toxin to affect many body tissues.

scholarly journals A novel endothelial cell surface receptor tyrosine kinase with extracellular epidermal growth factor homology domains.

1992 ◽  
Vol 12 (4) ◽  
pp. 1698-1707 ◽  
Author(s):  
J Partanen ◽  
E Armstrong ◽  
T P Mäkelä ◽  
J Korhonen ◽  
M Sandberg ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Kinase ◽  
Cell Lines ◽  
Receptor Tyrosine Kinase ◽  
Cell Surface Receptor ◽  
Endothelial Cell Surface ◽  
Surface Receptor ◽  
Epidermal Growth

Endothelial cell surfaces play key roles in several important physiological and pathological processes such as blood clotting, angiogenic responses, and inflammation. Here we describe the cloning and characterization of tie, a novel type of human endothelial cell surface receptor tyrosine kinase. The extracellular domain of the predicted tie protein product has an exceptional multidomain structure consisting of a cluster of three epidermal growth factor homology motifs embedded between two immunoglobulinlike loops, which are followed by three fibronectin type III repeats next to the transmembrane region. Additionally, a cDNA form lacking the first of the three epidermal growth factor homology domains was isolated, suggesting that alternative splicing creates different tie-type receptors. Cells transfected with tie cDNA expression vector produce glycosylated polypeptides of 117 kDa which are reactive to antisera raised against the tie carboxy terminus. The tie gene was located in chromosomal region 1p33 to 1p34. Expression of the tie gene appeared to be restricted in some cell lines; large amounts of tie mRNA were detected in endothelial cell lines and in some myeloid leukemia cell lines with erythroid and megakaryoblastoid characteristics. In addition, mRNA in situ studies further indicated the endothelial expression of the tie gene. The tie receptor tyrosine kinase may have evolved for multiple protein-protein interactions, possibly including cell adhesion to the vascular endothelium.

scholarly journals A novel endothelial cell surface receptor tyrosine kinase with extracellular epidermal growth factor homology domains

1992 ◽  
Vol 12 (4) ◽  
pp. 1698-1707
Author(s):  
J Partanen ◽  
E Armstrong ◽  
T P Mäkelä ◽  
J Korhonen ◽  
M Sandberg ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Kinase ◽  
Cell Lines ◽  
Receptor Tyrosine Kinase ◽  
Cell Surface Receptor ◽  
Endothelial Cell Surface ◽  
Surface Receptor ◽  
Epidermal Growth

Endothelial cell surfaces play key roles in several important physiological and pathological processes such as blood clotting, angiogenic responses, and inflammation. Here we describe the cloning and characterization of tie, a novel type of human endothelial cell surface receptor tyrosine kinase. The extracellular domain of the predicted tie protein product has an exceptional multidomain structure consisting of a cluster of three epidermal growth factor homology motifs embedded between two immunoglobulinlike loops, which are followed by three fibronectin type III repeats next to the transmembrane region. Additionally, a cDNA form lacking the first of the three epidermal growth factor homology domains was isolated, suggesting that alternative splicing creates different tie-type receptors. Cells transfected with tie cDNA expression vector produce glycosylated polypeptides of 117 kDa which are reactive to antisera raised against the tie carboxy terminus. The tie gene was located in chromosomal region 1p33 to 1p34. Expression of the tie gene appeared to be restricted in some cell lines; large amounts of tie mRNA were detected in endothelial cell lines and in some myeloid leukemia cell lines with erythroid and megakaryoblastoid characteristics. In addition, mRNA in situ studies further indicated the endothelial expression of the tie gene. The tie receptor tyrosine kinase may have evolved for multiple protein-protein interactions, possibly including cell adhesion to the vascular endothelium.

Immunogenic properties of outer membrane protein of Acinetobacter baumannii that loaded on chitosan nanoparticles

2017 ◽  
Vol 5 (1) ◽  
pp. 32-44
Author(s):  
Grace Hullmann ◽  
Michael A. Azfer
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Chitosan Nanoparticles ◽  
Growth Factor Receptor ◽  
Common Adverse Effect ◽  
Progression Free Survival ◽  
Cell Surface Receptor ◽  
Surface Receptor ◽  
Epidermal Growth ◽  
Egf Family

The epidermal growth factor receptor (EGFR; ErbB-1; HER1 in humans) is the cell-surface receptor for members of the epidermal growth factor family (EGF-family) of extracellular protein ligands. The identification of EGFR as an oncogene has led to the development of anticancer therapeutics directed against EGFR. The most common adverse effect of EGFR inhibitors, found in more than 90% of patients, is a papulopustular rash and in 10% to 15% of patients the effects can be serious and require treatment. While the risk of neutropenic fever toxicity has only recently been recognized. A total of 279 patients were enrolled in the present study. Progression-free survival (PFS) and overall survival (OS) of patients with a lowh grade of neutropnic fever were significantly longer than those with a high grade of neutropnic fever (median PFS: 3.6 months vs 8.4 months, P<0.001; median OS: 7.6 months vs 17.1 months, P=0.006, respectively).

scholarly journals Epidermal Growth Factor Signaling towards Proliferation: Modeling and Logic Inference Using Forward and Backward Search

2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Adrián Riesco ◽  
Beatriz Santos-Buitrago ◽  
Javier De Las Rivas ◽  
Merrill Knapp ◽  
Gustavo Santos-García ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Cellular Proliferation ◽  
Cell Surface Receptor ◽  
Growth Factor Signaling ◽  
Development Environment ◽  
Final State ◽  
Novel Approach ◽  
Surface Receptor ◽  
Epidermal Growth

In biological systems, pathways define complex interaction networks where multiple molecular elements are involved in a series of controlled reactions producing responses to specific biomolecular signals. These biosystems are dynamic and there is a need for mathematical and computational methods able to analyze the symbolic elements and the interactions between them and produce adequate readouts of such systems. In this work, we use rewriting logic to analyze the cellular signaling of epidermal growth factor (EGF) and its cell surface receptor (EGFR) in order to induce cellular proliferation. Signaling is initiated by binding the ligand protein EGF to the membrane-bound receptor EGFR so as to trigger a reactions path which have several linked elements through the cell from the membrane till the nucleus. We present two different types of search for analyzing the EGF/proliferation system with the help of Pathway Logic tool, which provides a knowledge-based development environment to carry out the modeling of the signaling. The first one is a standard (forward) search. The second one is a novel approach based onnarrowing, which allows us to trace backwards the causes of a given final state. The analysis allows the identification of critical elements that have to be activated to provoke proliferation.

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