ArticlePloS one2011
Comparing the epidermal growth factor interaction with four different cell lines: intriguing effects imply strong dependency of cellular context.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 53 citations in OpenAlex.
- Searching for EGF Fragments Recreating the Outer Sphere of the Growth Factor Involved in Receptor Interactions.International journal of molecular sciences · 2024Article
- Modelling ligand depletion for simultaneous affinity and binding site quantification on cells and tissue.Scientific reports · 2023Article
- Lipocalin 2 receptors: facts, fictions, and myths.Frontiers in immunology · 2023Review
- Potential of Epidermal Growth Factor-like Peptide from the Sea CucumberMarine drugs · 2022Article
- Physiological Considerations for ModelingFrontiers in pharmacology · 2022Review
- KEuropean biophysics journal : EBJ · 2021Article
- Radionuclide Molecular Imaging of EpCAM Expression in Triple-Negative Breast Cancer Using the Scaffold Protein DARPin Ec1.Molecules (Basel, Switzerland) · 2020Article
- Synthesis and Characterization of an Epidermal Growth Factor Receptor-Selective RuChembiochem : a European journal of chemical biology · 2020Article
- Versatile Bispidine-Based Bifunctional Chelators forChemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Novel Graphene Biosensor Based on the Functionalization of Multifunctional Nano-bovine Serum Albumin for the Highly Sensitive Detection of Cancer Biomarkers.Nano-micro letters · 2019Article
- Counting growth factors in single cells with infrared quantum dots to measure discrete stimulation distributions.Nature communications · 2019Article
- Detecting ligand interactions in real time on living bacterial cells.Applied microbiology and biotechnology · 2018Article
- Characterization of EGF-guided MDA-MB-231 cell chemotaxis in vitro using a physiological and highly sensitive assay system.PloS one · 2018Article
- Multivalent Fcγ-receptor engagement by a hexameric Fc-fusion protein triggers Fcγ-receptor internalisation and modulation of Fcγ-receptor functions.Scientific reports · 2017Article
- Impact of assay temperature on antibody binding characteristics in living cells: A case study.Biomedical reports · 2017Article
- Liquid-phase electron microscopy of molecular drug response in breast cancer cells reveals irresponsive cell subpopulations related to lack of HER2 homodimers.Molecular biology of the cell · 2017Article
- Rinsing paired-agent model (RPAM) to quantify cell-surface receptor concentrations in topical staining applications of thick tissues.Physics in medicine and biology · 2017Article
- Real-time Characterization of Antibody Binding to Receptors on Living Immune Cells.Frontiers in immunology · 2017Article
- Synthesis and biochemical characterization of EGF receptor in a water-soluble membrane model system.PloS one · 2017Article
- High Contrast PET Imaging of GRPR Expression in Prostate Cancer Using Cobalt-Labeled Bombesin Antagonist RM26.Contrast media & molecular imaging · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction of the epidermal growth factor (EGF) with its receptor (EGFR) is known to be complex, and the common over-expression of EGF receptor family members in a multitude of tumors makes it important to decipher this interaction and the following signaling pathways. We have investigated the affinity and kinetics of (125)I-EGF binding to EGFR in four human tumor cell lines, each using four culturing conditions, in real time by use of LigandTracer®.Highly repeatable and precise measurements show that the overall apparent affinity of the (125)I-EGF - EGFR interaction is greatly dependent on cell line at normal culturing conditions, ranging from K(D) ≈ 200 pM on SKBR3 cells to K(D)≈8 nM on A431 cells. The (125)I-EGF - EGFR binding curves (irrespective of cell line) have strong signs of multiple simultaneous interactions. Furthermore, for the cell lines A431 and SKOV3, gefitinib treatment increases the (125)I-EGF - EGFR affinity, in particular when the cells are starved. The (125)I-EGF - EGFR interaction on cell line U343 is sensitive to starvation while as on SKBR3 it is insensitive to gefitinib and starvation.The intriguing pattern of the binding characteristics proves that the cellular context is important when deciphering how EGF interacts with EGFR. From a general perspective, care is advisable when generalizing ligand-receptor interaction results across multiple cell-lines.
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