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SUMMARY:BMI Seminar // The role of proteolytic processing of the prion pro
 tein in neurodegenerative diseases
DTSTART:20170913T121500
DTEND:20170913T131500
DTSTAMP:20260428T175022Z
UID:e3cba4b2b4dce9261730126207485e13e81201cd6b373efce52618fa
CATEGORIES:Conferences - Seminars
DESCRIPTION:Markus Glatzel Institute of Neuropathology\, University Medica
 l Center Hamburg-Eppendorf\, Germany\n\nNeurodegenerative diseases such as
  Alzheimer’s disease or prion diseases are untreatable debilitating dise
 ases occurring mainly in the elderly.\nFor these diseases\, molecular mech
 anisms of neurodegeneration are only partially understood. Aberrant proteo
 lytic processing of neuronally expressed proteins leading to disturbed neu
 ronal protein homeostasis represents one mechanism leading to neurodegener
 ation.\nThe membrane-anchored cellular prion protein plays detrimental rol
 es in neurodegeneration by its ability to misfold into a pathogenic isofor
 m (in prion diseases) and by acting as a neuronal receptor for toxic prote
 in oligomers (e.g.\, in Alzheimer's disease). The mature form of the prion
  protein is processed by a variety of proteolytic cleavage events includin
 g shedding by the metalloprotease ADAM10.\nUsing cellular models and genet
 ically modified mice\, we study the impact of proteolytic processing of th
 e cellular form of the prion protein on its physiological functions and it
 s influence on neurodegenerative diseases.\nHere\, we report our most rece
 nt findings on the physiological and pathological relevance of these proce
 ssing step and present an update on our experimental strategy of exploitin
 g these cleavage events as a therapeutic option in neurodegenerative disea
 ses.\n 
LOCATION:SV 1717 https://plan.epfl.ch/?room==SV%201717
STATUS:CONFIRMED
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