The epidermal growth factor receptor (EGFR) belongs to the ErbB family of receptor tyrosine kinases. EGFR activation upon binding of ligands (such as EGF and TGF-α) results in cell signaling cascades that promote cell proliferation, survival and apoptosis inhibition. As reported for many solid tumors, EGFR overactivation is associated with tumor development and progression, resistance to cancer therapies and poor prognosis. Therefore, inhibition of EGFR function is a rational cancer therapy approach. We have shown previously that UV illumination of two cancer cell lines overexpressing EGFR could prevent phosphorylation of EGFR and of its downstream signalling molecules despite the presence of EGF. Our earlier studies demonstrated that UV illumination of aromatic residues in proteins leads to the disruption of nearby disulphide bridges. Since human EGFR is rich in disulphide bridges and aromatic residues, it is likely that structural changes can be induced upon UV excitation of its pool of aromatic residues (Trp, Tyr and Phe). Such changes impair the correct binding of ligands to EGFR which will halt the process of tumor growth. Our recent results confirm structural changes induced by UV light on the extracellular domain of human which impair e.g. binding of EGF to EGFR. Moreover, this new treatment activated the cell’s own cell death program and recently my group has observed that it prevents the formation of metastasis. We realized that UV light chemically modifies the same receptor protein that many cancer therapeutic treatments are trying to target chemically. We believe that this new photonic therapy holds promise for a totally new approach to treat some types of localized cancer, alone or in combination with other therapies to improve treatment outcome.


Wednesday, September 18, 2013, 10:30. Seminar Room

Hosted by Prof. Romain Quidant