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.

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 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.

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