Reducing α-synuclein pathology constitutes a plausible strategy against Parkinson’s disease. As we recently demonstrated, the β-wrapin protein AS69 binds an N-terminal region in monomeric α-synuclein, interferes with fibril nucleation, and reduces α ...
Éva M. Szegő +16 more
doaj +1 more source
p62/SQSTM1-dependent autophagy of Lewy body-like α-synuclein inclusions. [PDF]
α-Synuclein is the main component of Lewy bodies, the intraneuronal inclusion bodies characteristic of Parkinson's disease. Although α-synuclein accumulation is caused by inhibition of proteasome and autophagy-lysosome, the degradation of α-synuclein ...
Yoshihisa Watanabe +7 more
doaj +1 more source
Detection of disease-associated α-synuclein in the cerebrospinal fluid: a feasibility study [PDF]
With the aim to evaluate the significance and reliability of detecting disease-specific α-synuclein in the cerebrospinal fluid (CSF) we developed an ELISA and bead-assay. We used a commercial antibody (5G4) that does not bind to the physiological monomeric form of α-synuclein, but is highly specific for the disease-associated forms, including high ...
Unterberger, Ursula +9 more
openaire +2 more sources
Lysosomes and α-synuclein form a dangerous duet leading to neuronal cell death [PDF]
Neurodegenerative diseases are (i) characterized by a selective neuronal vulnerability to degeneration in specific brain regions; and (ii) likely to be caused by disease-specific protein misfolding. Parkinson's disease (PD) is characterized by the presence of intraneuronal proteinacious cytoplasmic inclusions, called Lewy Bodies (LB).
Mathieu eBourdenx +5 more
openaire +5 more sources
Novel subcellular localization for α-synuclein: possible functional consequences [PDF]
α-synuclein (α-syn) is one of the genes that when mutated or overexpressed causes Parkinson's Disease (PD). Initially, it was described as a synaptic terminal protein and later was found to be localized at mitochondria. Mitochondria-associated membranes (MAM) have emerged as a central endoplasmic reticulum (ER) subcellular compartments where key ...
Cristina eGuardia-Laguarta +4 more
openaire +3 more sources
Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillization. [PDF]
Amyloid fibrils of α-synuclein are the main constituent of Lewy bodies deposited in substantial nigra of Parkinson's disease brains. α-Synuclein is an intrinsically disordered protein lacking compact secondary and tertiary structures.
Winny Ariesandi +3 more
doaj +1 more source
Synucleinopathies represent a group of neurodegenerative disorders which are characterized by intracellular accumulation of aggregated α-synuclein. α-synuclein misfolding and oligomer formation is considered a major pathogenic trigger in these disorders.
Martin Kallab +8 more
doaj +1 more source
Chicago sky blue 6B inhibits α-synuclein aggregation and propagation
Abnormal deposition of α-synuclein aggregates in Lewy bodies and Lewy neurites is the hallmark lesion in Parkinson’s disease (PD). These aggregates, thought to be the culprit of disease pathogenesis, spread throughout the brain as the disease progresses.
Joo-Ok Min +4 more
doaj +1 more source
Nutrient deprivation induces α-synuclein aggregation through endoplasmic reticulum stress response and SREBP2 pathway [PDF]
Abnormal accumulation of filamentous α-synuclein (α-syn) in neurons, regarded as Lewy bodies (LBs), are a hallmark of Parkinson disease (PD). Although the exact mechanism(s) underlying LBs formation remains unknown, autophagy and ER stress response have emerged as two important pathways affecting α-syn aggregation.
Jiang, Peizhou +3 more
openaire +3 more sources
Extracellular α-synuclein levels are regulated by neuronal activity
Background α-Synuclein is a presynaptic protein abundant in the cytoplasmic compartment of neurons, whereas its presence in the extracellular space has also been observed under physiological conditions.
Kaoru Yamada, Takeshi Iwatsubo
doaj +1 more source

