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SUMMARY:New insights into protein misfolding in Alzheimer’s and Parkinso
 n’s diseases using in vivo systems - Prof Dennis Selkoe\, Harvard Medica
 l School and Brigham and Women's Hospital
DTSTART:20170217T140000Z
DTEND:20170217T150000Z
UID:TALK71221@talks.cam.ac.uk
CONTACT:Priyanka Joshi
DESCRIPTION:Misfolding and progressive aggregation of specific proteins ma
 y be etiologic in several human neurodegenerative diseases. Many studies h
 ave examined the process in vitro\, resulting in valuable insights\, but t
 o what extent findings in relatively pure in vitro systems reflect the sit
 uation in the patient’s brain is unclear. Here\, we have focused on livi
 ng cells\, mice\, and human brain tissue to learn more about the character
 istics and bioactivities of various endogenous forms of amyloid β-protein
  (Aβ) and α-synculein (αSyn). We will describe recent work on the effec
 ts of natural oligomers of Aβ isolated from AD cortex on iPSC-derived hum
 an neurons\, including protection by certain antibodies. We will then prov
 ide further evidence that αSyn occurs normally as helical tetramers in in
 tact cells\, but these rapidly disassemble upon cell lysis\, yielding the 
 unfolded monomers that have been the focus of in vitro studies. Mice expre
 ssing tetramer-abrogating αSyn mutations develop nigrostriatal and cortic
 al lesions\, decreased tyrosine hydroxylase\, and a progressive motor phen
 otype that includes tremor and gait defects which respond in part to L-DOP
 A. These new findings have implications for the initiation of PD and other
  human synucleinopathies and their potential prevention by compounds which
  stabilize the physiological tetramers.         
LOCATION:Department of Chemistry\, Cambridge\, Pfizer lecture theatre
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