Epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein expressed in many types of mammalian cell surfaces. An EGFR monomer contains an intracellular domain with tyrosine kinase which can be specifically inhibited by an EGFR tyrosine kinase-specific inhibitor PD153035 to block EGFR activation and to prevent intracellular signal pathway.
Purified EGFR (5 mg/ml) or cells were divided into three groups: 1) sham-exposed group, 2) magnetic field-exposed group, or 3) the PD inhibitor pretreated group with different concentrations.
Exposure duration: continuous for 30 min
|Setup||The magnetic field was fairly uniform (± 0.012 mT) over the exposure area between the plates. The whole set-up was placed in a CO2 incubator maintained at 37°C and was shield from external field.|
|Sham exposure||A sham exposure was conducted.|
|magnetic flux density||0.4 mT||unspecified||measured||-||-|
The data showed that the magnetic field exposure induced purified EGF receptors to form clusters (i.e. at least two monomers form a cluster), free from cell membrane and EGF binding. The EGFR tyrosine kinase inhibitor evidently blocks the ligand-free-clustering effect.
The findings indicate that the tyrosine kinase domain of EGFR is a likely candidate site for the magnetic field interaction.