TY - JOUR
AU - Stuendl, Anne
AU - Kunadt, Marcel
AU - Kruse, Niels
AU - Bartels, Claudia
AU - Moebius, Wiebke
AU - Danzer, Karin M
AU - Mollenhauer, Brit
AU - Schneider, Anja
TI - Induction of α-synuclein aggregate formation by CSF exosomes from patients with Parkinson's disease and dementia with Lewy bodies.
JO - Brain
VL - 139
IS - 2
SN - 0006-8950
CY - Oxford
PB - Oxford Univ. Press
M1 - DZNE-2020-04699
SP - 481-494
PY - 2016
AB - Extracellular α-synuclein has been proposed as a crucial mechanism for induction of pathological aggregate formation in previously healthy cells. In vitro, extracellular α-synuclein is partially associated with exosomal vesicles. Recently, we have provided evidence that exosomal α-synuclein is present in the central nervous system in vivo. We hypothesized that exosomal α-synuclein species from patients with α-synuclein related neurodegeneration serve as carriers for interneuronal disease transmission. We isolated exosomes from cerebrospinal fluid from patients with Parkinson's disease, dementia with Lewy bodies, progressive supranuclear palsy as a non-α-synuclein related disorder that clinically overlaps with Parkinson's disease, and neurological controls. Cerebrospinal fluid exosome numbers, α-synuclein protein content of cerebrospinal fluid exosomes and their potential to induce oligomerization of α-synuclein were analysed. The quantification of cerebrospinal fluid exosomal α-synuclein showed distinct differences between patients with Parkinson's disease and dementia with Lewy bodies. In addition, exosomal α-synuclein levels correlated with the severity of cognitive impairment in cross-sectional samples from patients with dementia with Lewy bodies. Importantly, cerebrospinal fluid exosomes derived from Parkinson's disease and dementia with Lewy bodies induce oligomerization of α-synuclein in a reporter cell line in a dose-dependent manner. Our data suggest that cerebrospinal fluid exosomes from patients with Parkinson's disease and dementia with Lewy bodies contain a pathogenic species of α-synuclein, which could initiate oligomerization of soluble α-synuclein in target cells and confer disease pathology.
KW - Cerebrospinal Fluid: metabolism
KW - Cohort Studies
KW - Cross-Sectional Studies
KW - Exosomes: metabolism
KW - Female
KW - Follow-Up Studies
KW - Humans
KW - Lewy Body Disease: cerebrospinal fluid
KW - Lewy Body Disease: metabolism
KW - Longitudinal Studies
KW - Male
KW - Parkinson Disease: cerebrospinal fluid
KW - Parkinson Disease: metabolism
KW - Protein Aggregates: physiology
KW - alpha-Synuclein: biosynthesis
KW - alpha-Synuclein: cerebrospinal fluid
KW - Protein Aggregates (NLM Chemicals)
KW - alpha-Synuclein (NLM Chemicals)
LB - PUB:(DE-HGF)16
C6 - pmid:26647156
C2 - pmc:PMC4805087
DO - DOI:10.1093/brain/awv346
UR - https://pub.dzne.de/record/138377
ER -