In Vivo Protein Complementation Demonstrates Presynaptic α-Synuclein Oligomerization and Age-Dependent Accumulation of 8–16-mer Oligomer Species

Martin Kiechle, Bjoern von Einem, Lennart Höfs, Patrizia Voehringer, Veselin Grozdanov, Daniel Markx, Rosanna Parlato, Diana Wiesner, Benjamin Mayer, Olena Sakk, Bernd Baumann, Soeren Lukassen, Birgit Liss, Arif B. Ekici, Albert C. Ludolph, Paul Walther, Boris Ferger, Pamela J. McLean, Björn H. Falkenburger, Jochen H. WeishauptKarin M. Danzer

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Kiechle et al. present two transgenic mouse models that allow direct quantitative and spatial detection of α-synuclein (α-syn) oligomers in vivo. They demonstrate α-syn aggregation at the synapse, age-dependent accumulation of 8–16-mer α-syn oligomer species, and trans-cellular oligomer spreading from forebrain to hindbrain neurons.

Original languageEnglish (US)
Pages (from-to)2862-2874.e9
JournalCell reports
Volume29
Issue number9
DOIs
StatePublished - Nov 26 2019

Keywords

  • Parkinson's disease
  • aging
  • alpha-synuclein
  • neurodegeneration
  • oligomerization
  • progressive phenotype
  • protein-fragment complementation
  • spreading
  • synaptic oligomers
  • transgenic mouse model

ASJC Scopus subject areas

  • General Biochemistry, Genetics and Molecular Biology

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