A new study from EPFL reveals novel insights into the ultrastructure and biochemical composition of huntingtin aggregates, the mark of Huntington's disease, pointing to new avenues for treatment strategies. Huntington's disease is a progressively debilitating brain disease that causes uncontrolled movements, psychological problems, and loss of cognition. Huntington's is caused by a mutation in the gene that encodes huntingtin, a protein that normally plays important roles in keeping brain cells healthy and active. But the mutation "gives" huntingtin an abnormally long tail of glutamine amino acids, which cause huntingtin to aggregate inside neurons and eventually kill them. These aggregates, or "inclusion bodies", of huntingtin have been the subject of a lot of research efforts in the attempt to find a way to understand and treat Huntington's. What has been missing though is a deep analysis of the inclusions' ultrastructure - a term that describes the level of structure that lies beyond the capacity of a conventional microscope to observe. Looking deep Using advanced microscopy and proteomics, scientists led by Hilal Lashuel at EPFL, in collaboration with the Biological Electron Microscopy Facility, have now successfully carried out the first study that interrogates both the ultrastructure of huntingtin inclusion bodies and their composition in cells that model the pathological formation of Huntington's disease.
TO READ THIS ARTICLE, CREATE YOUR ACCOUNT
And extend your reading, free of charge and with no commitment.
