Polymorphic and amyloid natures of neuronal inclusions in Huntington’s disease brain revealed by IR microspectroscopy.
Résumé
Huntington’s disease (HD) is a neurodegenerative disease characterized by the formation of protein aggregates in certain regions of the brain; some of these aggregates can reach microscopic size (inclusions). Studies in cells and animals have shown that aggregates are polymorphic and that their secondary structure is likely to condition their toxicity [1]. However, the secondary structure of proteins in the inclusions found in the brain of patients is still unknown. We show by using synchrotron Fourier-transform infrared microspectroscopy (sFTIR), that the brain of HD patients contains structurally different inclusions, some of which are amyloid. As one category of amyloid inclusions is characteristic of severely affected brain regions, it may be particularly toxic to neurons.