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Chelators specific copper - A potential application

Published on 3 October 2020

Research topics

In humans, the liver is the organ responsible for elimination of excess copper in the body. Cu(I) enters the hepatocytes where it binds to a Cu-ATPase called the Wilson's disease ATPase that excretes the Cu(I) to the bile canaliculus. Wilson's disease is caused by a defect in the ATP7B gene; this results in a poisoning of the patient by copper which accumulates in the liver and, in the absence of diagnosis, in a fatal outcome. Current treatments are aimed primarily to reduce the absorption of copper content in foods, but they are also struggling to mobilize stored copper in the liver. Our interest in the specific proteins that bind Cu(I) has led us to collaborate with a team of chemists to develop a molecule able of chelating Cu(I) in hepatocytes. Pascale Delangle and her group, in collaboration with the DCM (UJF) have designed a molecule specifically targeted to hepatocytes to chelate Cu(I) (Figure). We have shown recently that this molecule not only enters cultured hepatocytes, but also decreases the concentration of Cu(I) [Pujol et al., 2010]. The new compound will be tested in vivo on a mouse model for the Wilson's disease.

WIF-B9 cells in culture form a complex epithelium that resembles the organization of hepatocytes in the liver. Cells are associated around a space that mimics the bile canaliculus (cb). The chelator, tagged with a red fluorophore, rapidly enters the cells and accumulates in the cb spaces.


Molecular biology - cell culture - biochemistry - absorption spectroscopy - fluorescence - immunofluorescence - quantitative PCR.