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SUMMARY:Uncovering the role of misfolded SOD1 in the pathogenesis of Amyot
 rophic Lateral Sclerosis
DTSTART:20150112T103000
DTEND:20150112T113000
DTSTAMP:20260916T153726Z
UID:07785cfd7b38714785657f81b08d09e37a60b2a5b641dd1a85c00147
CATEGORIES:Conferences - Seminars
DESCRIPTION:Sarah Pickles\, Ph.D.\, University of Montréal (Can)\nSEMINAR
  of the LAUSANNE INTEGRATIVE METABOLISM and NUTRITION ALLIANCE (LIMNA)Abst
 ract:\nALS is a neurodegenerative disorder characterized by the loss of mo
 tor neurons resulting in paralysis and death. Some Familial ALS cases are 
 caused by mutations in SOD1\, which lead to misfolding of the SOD1 protein
 \, and gain of a toxic function. Several antibodies have been generated th
 at are specific for the misfolded protein\, and have been used for therape
 utics. We used one antibody\, B8H10\, to demonstrate that misfolded SOD1 a
 ssociates with mitochondria and those mitochondria have a significantly la
 rger volume and produce more reactive oxygen species. We have demonstrated
  that not all misfolded SOD1 specific antibodies detect misfolded SOD1 at 
 mitochondria. This finding suggests that there may be multiple misfolded S
 OD1 conformers. Using a panel of antibodies specific against misfolded SOD
 1 we aim to reveal which misfolded SOD1 confomers are relevant to mitochon
 drial dysfunction versus other mechanisms of disease. These studies will a
 id in identifying which misfolded SOD1 antibodies will be effective in the
 rapeutics\, and which SOD1 antibodies will be useful as markers of patholo
 gy.   
LOCATION:AI 1153 https://plan.epfl.ch/?room==AI%201153
STATUS:CONFIRMED
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