Gustafsson, G. 2017. Alpha-Synuclein Oligomers. Cellular Mechanisms and Aspects of Antibody Treatment. Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Medicine 1344. 64 pp. Uppsala: Acta Universitatis Upsaliensis. ISBN 978-91-513-0008-5. In Parkinson’s disease (PD) and dementia with Lewy bodies (DLB), aggregated α-synuclein deposit inside cells within the brain. Sma...

Parkinson's disease (PD) is associated with perturbed mitochondria function and alpha-synuclein fibrillization. We evaluated potential mechanistic links between mitochondrial dysfunction and alpha-synuclein aggregation. We studied a PD cytoplasmic hybrid (cybrid) cell line in which platelet mitochondria from a PD subject were transferred to NT2 neuronal cells previously depleted of endogenous m...

Genetics and neuropathology strongly link α-synuclein aggregation and neurotoxicity to the pathogenesis of Parkinson's disease and related α-synucleinopathies. Here we describe a new Drosophila model of α-synucleinopathy based on widespread expression of wild-type human α-synuclein, which shows robust neurodegeneration, early-onset locomotor deficits, and abundant α-synuclein aggregation. We us...

ARTICLE HISTORY Received 7 November 2016 Accepted 23 November 2016 ABSTRACT The partitioning between tubulin dimers and microtubules is fundamental for the regulation of several neuronal activities, from neuronal polarization and processes extension to growth cone remodelling. This phenomenon is modulated by several proteins, including the well-known microtubule destabilizer Stathmin. We recent...

alpha-Synuclein is a major constituent of glial cytoplasmic inclusions (GCIs), which are pathognomic for multiple system atrophy (MSA). We have previously demonstrated that in normal human brain, alpha-synuclein mRNA has a restricted pattern of neuronal expression and no apparent glial expression. The current study used double-label in situ hybridization to determine if alpha-synuclein mRNA is ...

The inhibition of amyloid fibril and/or oligomer formation allows a novel therapeutic approach to neurodegenerative diseases such as Parkinson’s disease. We have previously reported that pyrroloquinoline quinone (PQQ), a cofactor in the bacterial oxidative metabolism of alcohols, prevents the amyloid formation of -synuclein, which is the causative factor of Parkinson’s disease. Moreover, PQQ-mo...

Real-time monitoring of stimulated dopamine release in mice with different -synuclein expression was used to study the role of -synuclein in presynaptic dopamine recruitment. Repeated electrical stimulations of ascending dopaminergic pathways decreased the capacity of the readily releasable pool (RRP) and temporarily increased its refilling rate, significantly slowing the rate of dopamine decli...

Dear Editor Alpha‐synuclein is a widespread neuronal presynaptic protein found predominantly in the central nervous system, and it is an element of the neuropathological features of several neurodegenerative disorders including the dementia with Lewy bodies and the Parkinson’s disease. At the extra‐ neural tissue, the normal distribution and functions of α‐ synuclein remain especially elusive. ...

α-synuclein pathology presenting as tiny dots, thin neurites, and larger amorphous deposits in the subependymal area, as well as tiny dots between ependymal cells in the brains of individuals with neuropathologically proven Parkinson`s disease (Braak stages 5 and 6). Immunostaining was performed using antibody 5G4 (Roboscreen, Leipzig, Germany; we applied 1 : 2,000 dilution and a pretreatment o...

Aggregated α-synuclein in Lewy bodies is one of the hallmarks of Parkinson’s disease (PD). Earlier observations of α-synuclein aggregates in neurons grafted into brains of PD patients suggested cell-to-cell transfer of α-synuclein and a prion-like mechanism. This prompted the current investigation of whether α-synuclein passes over model phospholipid bilayers. We generated giant unilamellar ves...