13 December 2013

Misfolded Proteins: Prion-Like Propagation and Potential Cure. Implication for Neurodegenerative Diseases

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SCI's Biotechnology Group in conjunction with the University of Westminster

University of Westminster

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Deposition of proteins of aberrant conformation is the hallmark of many neurodegenerative diseases. Misfolding of the normally globular mutant superoxide dismutase-1 (SOD1) is a central, early, but poorly misunderstood event in the pathogenic cascade leading to familial forms of ALS. We found that mutant SOD1 aggregates self-propogate in a prion-like manner. Dr Bertolotti will discuss the implications of these observations for ALS.

While it is now well established that misfolded proteins cause diverse neurodegenerative diseases, why they accumulate remains unclear. All cells have powerful and sophisticated protein quality control systems that very efficiently handle potentially harmful proteins for decades. These cellular defence systems seem to gradually fail with age. In principle, improving the cells' ability to deal with misfolded proteins could represent a generic approach to reduce the pathology in these diverse neurodegenerative diseases. Dr Bertolotti will present two novel strategies to increase the cells' ability to cope with quality control failure.

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University of Westminster

University of Westminster, School of Life Sciences, 115 New Cavendish Street London W1W 6UW

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Dr Anne Bertolotti, MRC Laboratory for Molecular Biology, Cambridge