scholarly journals Sustained epidermal growth factor receptor levels and activation by tethered ligand binding enhances osteogenic differentiation of multi-potent marrow stromal cells

2009 ◽  
Vol 221 (2) ◽  
pp. 306-317 ◽  
Author(s):  
Manu O. Platt ◽  
Arian J. Roman ◽  
Alan Wells ◽  
Douglas A. Lauffenburger ◽  
Linda G. Griffith
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Ligand Binding ◽  
Osteogenic Differentiation ◽  
Stromal Cells ◽  
Growth Factor Receptor ◽  
Marrow Stromal Cells ◽  
Tethered Ligand ◽  
Epidermal Growth

Ligand binding induces a conformational change in epidermal growth factor receptor dimers

2012 ◽  
Vol 30 (6) ◽  
pp. 394-409 ◽  
Author(s):  
Francesca Walker ◽  
Julie Rothacker ◽  
Christine Henderson ◽  
Edouard C. Nice ◽  
Bruno Catimel ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Ligand Binding ◽  
Conformational Change ◽  
Growth Factor Receptor ◽  
Epidermal Growth ◽  
Receptor Dimers

Expression and localisation of epidermal growth factor receptors and their ligands in the lower genital tract of cycling cows

2019 ◽  
Vol 31 (11) ◽  
pp. 1692
Author(s):  
Hakan Saǧsöz ◽  
Narin Liman ◽  
Berna Güney Saruhan ◽  
Mehmet E. Akbalık ◽  
Muzaffer A. Ketani ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Stromal Cells ◽  
Growth Factor Receptor ◽  
Oestrous Cycle ◽  
Epidermal Growth Factor Receptors ◽  
Cellular Processes ◽  
Lower Genital Tract ◽  
Epidermal Growth

The epidermal growth factor receptor (ErbB) family and its ligands are essential for the regulation of multiple cellular processes required for mammalian reproduction. The objectives of this study were to investigate the expression and localisation of ErbB subtypes (ErbB1–4) and selected ligands, namely epidermal growth factor (EGF), amphiregulin (AREG) and neuregulin (NRG), in the cervix and vagina of cycling cows and to determine possible steroid hormone-dependence of their expression using immunohistochemistry. All four ErbBs and EGF, AREG and NRG proteins were found to be localised in the nucleus and cytoplasm of different cells in the cervix and vagina, and their expression differed during the oestrous cycle. During the follicular phase, in both the cervix and vagina, ErbB1, ErbB2, ErbB3, ErbB4 and EGF expression was higher in the luminal epithelium (LE) than in stromal and smooth muscle (SM) cells (P<0.05). During the luteal phase, the expression of ErbB1, ErbB3 and EGF in the LE was significantly different from that in stromal and SM cells in the cervix, whereas the expression of EGF and AREG differed in the vagina compared to the cervix (P<0.05). Throughout the oestrous cycle, in both the cervix and vagina, although ErbB2/human epidermal growth factor receptor 2 expression in the LE and SM cells was significantly higher than in the stromal cells (P<0.05), NRG expression was similar in the LE, stromal and SM cells (P>0.05). Overall, these results suggest that all four ErbBs and the EGF, AREG and NRG proteins may collectively contribute to several cellular processes in the bovine cervix and vagina during the oestrous cycle.

scholarly journals The epidermal growth factor receptor (EGFR)-S442F mutant displays increased affinity for neuregulin-2β and agonist-independent coupling with downstream signalling events

2006 ◽  
Vol 396 (1) ◽  
pp. 79-88 ◽  
Author(s):  
Jennifer L. Gilmore ◽  
Richard M. Gallo ◽  
David J. Riese
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Ligand Binding ◽  
Growth Factor Receptor ◽  
Egfr Mutations ◽  
Genetic Changes ◽  
Egfr Ligand ◽  
Epidermal Growth ◽  
Stimulation Of

The EGFR (epidermal growth factor receptor; ErbB1) is frequently the subject of genetic changes in human tumours which contribute to the malignant phenotype by altering EGFR signalling. Examples of such genetic changes include overexpression, extracellular domain deletions and point mutations, and small deletions in the tyrosine kinase domain. We hypothesized that a point mutation in one of the EGFR ligand-binding domains would increase the affinity of EGFR for NRG2β (neuregulin-2β), which is not a potent stimulus of signalling by EGFR-Wt (wild-type EGFR). This mutation would permit NRG2β stimulation of EGFR signalling in settings in which NRG2β does not normally do so. To test this hypothesis, we have generated and evaluated various EGFR alleles containing mutations at Val441 and Ser442. NRG2β is a much more potent stimulus of the EGFR-S442F mutant than of EGFR-Wt. Furthermore, the affinity of NRG2β for the EGFR-S442F mutant is greater than the affinity of NRG2β for EGFR-Wt. Finally, the EGFR-S442F mutant constitutively suppresses apoptosis via phosphoinositide 3-kinase and Akt signalling but is not highly tyrosine phosphorylated in the absence of ligand. These results suggest that mutations in the EGFR ligand-binding domain in tumours may permit potent stimulation of EGFR signalling by ligands that are not normally potent EGFR agonists, thereby providing for a novel mechanism by which EGFR signalling may be deregulated. These results also suggest that novel EGFR mutations and signalling activities may be responsible for deregulated EGFR signalling in tumour cells.

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