Real-Time Kinetics of Ligand/Cell Surface Receptor Interactions in Living Cells:  Binding of Epidermal Growth Factor to the Epidermal Growth Factor Receptor†

Biochemistry ◽  
2001 ◽  
Vol 40 (34) ◽  
pp. 10230-10242 ◽  
Author(s):  
John C. Wilkinson ◽  
Richard A. Stein ◽  
Cheryl A. Guyer ◽  
Joseph M. Beechem ◽  
James V. Staros
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Living Cells ◽  
Cell Surface Receptor ◽  
Receptor Interactions ◽  
Surface Receptor ◽  
Epidermal Growth ◽  
Kinetics Of

scholarly journals Inhibition of epidermal growth factor receptor (EGFR) expression by human cytomegalovirus correlates with an increase in the expression and binding of Wilms' Tumour 1 protein to the EGFR promoter

2009 ◽  
Vol 90 (7) ◽  
pp. 1569-1574 ◽  
Author(s):  
Insiya Jafferji ◽  
Mark Bain ◽  
Christine King ◽  
John H. Sinclair
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Human Cytomegalovirus ◽  
Growth Factor Receptor ◽  
Cell Surface Receptor ◽  
Wilms Tumour ◽  
Promote Cell Proliferation ◽  
Egfr Expression ◽  
Epidermal Growth

Infection with human cytomegalovirus (HCMV) modulates the expression of a number of cellular receptors and is known to inhibit expression of the epidermal growth factor receptor (EGFR), a cell surface receptor that can promote cell proliferation through a cascade of intracellular signalling events. We have examined the mechanisms by which HCMV mediates downregulation of EGFR expression and show that virus infection results in the profound upregulation of Wilms' Tumour 1 (WT1) protein, a transcription factor associated with the negative regulation of a number of growth factors and growth factor receptors, including EGFR. Moreover, chromatin immunoprecipitation experiments also show that HCMV infection results in increased binding of WT1 to the EGFR promoter. Finally, we show that depleting the cell of WT1 using small interfering RNA abrogates virus-mediated downregulation of EGFR. Taken together, our observations suggest that HCMV-mediated repression of EGFR expression results from a virus-mediated increase in cellular WT1, a known pleiotropic regulator of mitogenesis, apoptosis and differentiation.

Mechanisms of human cytomegalovirus infection with a focus on epidermal growth factor receptor interactions

2017 ◽  
Vol 27 (6) ◽  
pp. e1955 ◽  
Author(s):  
Aline Semblano Carreira Falcão ◽  
Pedro Fernando da Costa Vasconcelos ◽  
Dorotéa de Fátima Lobato da Silva ◽  
João de Jesus Viana Pinheiro ◽  
Luiz Fábio Magno Falcão ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Human Cytomegalovirus ◽  
Cytomegalovirus Infection ◽  
Growth Factor Receptor ◽  
Receptor Interactions ◽  
Epidermal Growth ◽  
Human Cytomegalovirus Infection

scholarly journals Formation of an RNA Quadruplex-Duplex Hybrid in Living Cells between mRNA of the Epidermal Growth Factor Receptor (EGFR) and a G-Rich Antisense Oligoribonucleotide

Cells ◽  
2020 ◽  
Vol 9 (11) ◽  
pp. 2375
Author(s):  
Dorota Gudanis ◽  
Damian Kaniowski ◽  
Katarzyna Kulik ◽  
Daniel Baranowski ◽  
Zofia Gdaniec ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Messenger Rna ◽  
Growth Factor Receptor ◽  
Living Cells ◽  
Cellular Systems ◽  
Mrna Levels ◽  
Epidermal Growth

Antisense DNA oligonucleotides, short interfering RNAs (siRNAs), and CRISPR/Cas9 genetic tools are the most useful therapeutic nucleic acids regulating gene expression based on the antisense specificity towards messenger RNA. Here, we present an effective novel strategy for inhibiting translation based on the antisense-controlled formation of an RNA quadruplex-duplex hybrid (QDH) between a G-rich RNA antisense oligoribonucleotide (Q-ASO) and specific mRNA, comprising two distant G-tracts. We selected epidermal growth factor receptor (EGFR) as a well-established target protein in anticancer therapy. The chemically modified, bi-functional anti-EGFR Q-ASO and a 56-nt long EGFR mRNA fragment, in the presence of potassium ions, were shown to form in vitro very stable parallel G-quadruplex containing a 28-nt long external loop folding to two duplex-stem structure. Besides, the Q-ASOs effectively reduced EGFR mRNA levels compared to the non-modified RNA and DNA antisense oligonucleotides (rASO, dASO). In addition, the hybridization specificity of Q-ASO comprising a covalently attached fluorescent tag was confirmed in living cells by visualization of the G4 green fluorescent species in the presence of other antisense inhibitors under competitive conditions. The results presented here offer novel insights into the potential application of Q-ASOs for the detection and/or alteration of (patho)biological processes through RNA:RNA quadruplex-duplex formation in cellular systems.

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