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Human SNCA Protein expressed in Escherichia coli (E. coli) - ABIN2005039
Lee, Choi, Lee: Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. in The Journal of biological chemistry 2002
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Rat (Rattus) SNCA Protein expressed in Rabbit - ABIN1742284
Jüttner, Moré, Das, Babich, Meier, Henning, Erdmann, Mu Ller, Otto, Grantyn, Rathjen: Impaired synapse function during postnatal development in the absence of CALEB, an EGF-like protein processed by neuronal activity. in Neuron 2005
study examined the spatial and temporal expression patterns of three synuclein genes (snca, sncbb, sncg) during embryogenesis
alpha-synucleinA53T overexpression caused p38 MAPK activation, then p38 MAPK directly phosphorylated Parkin at serine 131 to disrupt the Parkin's protective function.
The map and model allow the assessment of selective vulnerability to alpha-synuclein pathology development and neuron death
Our results demonstrated a reduction in both ethanol intake and preference and also a lack of sensitivity to the anxiolytic effects of ethanol in alpha-synuclein mutant mice
results indicate that seipin deficiency causes an age-related loss of dopaminergic neurons and impairment of motor coordination through reducing PPARgamma to enhance aggregation and phosphorylation of alphaSyn and neuroinflammation.
this complementary, bidirectional genetic approach implicates alphaSyn as an essential mediator of key phenotypes in AD and offers new functional insight into alphaSyn pathophysiology
Syn III constitutes a crucial mediator of alpha-synuclein aggregation and toxicity and identify Syn III as a novel therapeutic target for Parkinson's disease
activation of the microglial NLR family pyrin domain containing 3 (NLRP3) inflammasome is a common pathway triggered by both fibrillar alpha-synuclein and dopaminergic degeneration in the absence of alpha-synuclein aggregates.
Only neurons expressing A53T alpha-synuclein mutation exhibit tau phosphorylation-dependent postsynaptic dysfunction.
It has been proposed that MsrA-dependent 14-3-3 zeta ubiquitination affects the regulation of alpha synuclein degradation and dopamine synthesis in the brain.
The familial mutant, A30P, of alpha-synuclein induces stronger gene expression deregulation, leading to endoplasmic reticulum and Golgi dysfunction.
variations of amyloid fibrillar morphologies among the aggregates of a-syn mutants, mainly categorized into two groups: twisted fibrils observed for both WT and E46K while straight fibrils for the other mutants.
tetramers are required for normal alpha-Synuclein homeostasis and chronically shifting tetramers to monomers may result in Parkinson's disease
compromising the capacity to scavenge free radicals can exacerbate alpha-synuclein aggregation, indicating that elevated levels of oxidative stress could modulate the progression of Parkinson disease
Math2-expressing neurons in the hippocampal Cornu ammonis (CA) highly susceptible to pathological seeding with pre-formed fibrils (PFFs) in contrast to dentate gyrus neurons, which are relatively spared. Math2(+) neurons exhibited more rapid and severe cell loss in both in vitro and in vivo models of synucleinopathy. aSyn expression levels strongly correlate with relative vulnerability among hippocampal neuron subtypes.
iron overload due to impaired ferritinophagy or other cause(s) is likely to initiate prion-like spread of alpha-syn and ferritin, creating retinal iron dyshomeostasis and associated cytotoxicity. Since over-expression of alpha-syn is a known cause of Parkinson's disease.
Previously reported the progressive spreading of alpha-synuclein aggregates, between 1 and 12 months following alpha-synuclein fibril injections, and now report how far the pathology has spread 18- and 23-month post-injection in this model. Between 12 and 18 months, there is a further increase in the number of brain regions exhibiting pathology after human, and to a lesser extent mouse, alpha-synuclein fibril injections.
Mutation of LRRK2 induces modest but significant changes in lysosomal morphology and acidification, and decreased basal autophagic flux. These changes were associated with an accumulation of detergent-insoluble alpha-synuclein and increased neuronal release of alpha-synuclein and were reversed by pharmacologic inhibition of LRRK2 kinase activity.
Wild-type mice were exposed to multiple regimens of repetitive mild traumatic brain injury. There was a highly significant main effect of impact energy, frequency, and duration of exposure on Abeta1-42, tau, and alpha-synuclein levels (P < .001), and a significant interaction between impact energy and duration of exposure for Abeta1-42 and tau (P < .001), but not for alpha-synuclein.
a potential role for alpha-synuclein in vesicular trafficking in leukocytes
Common variation at SNCA might modulate PD risk.
In humans, we found a significant association of the rs356219 SNP of SNCA with a high level of anxiety and the rs356200 SNP with a positive familial history of
Our results highlight the importance of mitochondria-associated alpha-synuclein in human disease, and present Miro as a novel therapeutic target
Longitudinal studies using retinal imaging in mice expressing a hASYN::GFP fusion protein revealed that 2 months of once daily administration of NPT200-11 (5 mg/kg IP) resulted in a time-dependent and progressive reduction in retinal ASYN pathology.
site-specific oxidation kinetics point out a minor delay in Met-127 modification, likely due to the effects of alpha-Synuclein intrinsic structure.
We found that SNCA oligomerization has a profound impact on protein-lipid interaction, altering binding affinity and/or curvature sensitivity depending on membrane composition
Parkinson's disease patients with orthostatic hypotension showed a wide involvement of alpha-synuclein deposits in skin nerves when compared to Parkinson's disease patients without orthostatic hypotension.
All oligomeric constructs remained largely disordered in solution, as determined from dynamic light scattering and size-exclusion chromatography. Electron microscopy revealed that each construct could aggregate to form fibrils similar to those formed by monomeric alpha-synuclein
Cortical thinning associated with age and CSF biomarkers in early Parkinson's Disease Is modified by the SNCA rs356181 polymorphism
Expression analysis to further our understanding regarding the GATA and ELK family members that are potentially relevant for SNCA transcriptional regulation in health and disease.
In this study, we present a novel human Tet-on human neural stem cell (hNSC) line, in which aSyn timing and level of expression can be tightly experimentally tuned. Induction of aSyn in self-renewing hNSCs leads to progressive formation of aSyn aggregates and impairs their proliferation and cell survival.
In this work, scanning ion conductance microscopy was used to monitor the effect of alpha-synuclein aggregates on the integrity of cell membranes. Disruption was detected in cells pre-incubated with alpha-synuclein aggregates and observed in situ upon addition of the aggregates, although the interaction varied among different cells.
The surface of soluble SNCA oligomers is more hydrophobic than fibrils and populates a diverse range of coexisting states. Overall, the data show that the conversion of oligomers to fibril-like aggregates and ultimately to fibrils results in a reduction in both hydrophobicity and the variation in hydrophobicity.
A53E enriches alpha-synuclein oligomers and fibrils dependent on the phosphorylation state
alpha-Synuclein (alphaS) is the major component of the filamentous inclusions that constitute the defining characteristic of neurodegenerative synucleinopathies.
Pathological alpha-synuclein (alphaSyn) has been shown to retain the ability to propagate as prions in humans and animals.
This study combines high- and low-field nuclear spin relaxation, nanosecond fluorescence correlation spectroscopy and long molecular dynamics simulations of alpha-synuclein, an intrinsically disordered protein involved in Parkinson disease, to obtain a comprehensive picture of its conformational dynamics.
In the present work, for the first time it was demonstrated that alpha-synuclein can be efficiently modified by the intermediate product of glycolysis glyceraldehyde-3-phosphate.
We established that DNA hypermethylation at SNCA intron 1 allows an effective and sufficient tight downregulation of SNCA expression levels, suggesting the potential of this target sequence combined with the CRISPR-dCas9 technology as a novel epigenetic-based therapeutic approach for Parkinson's disease
Longitudinal increases in total apha-synuclein predicted progression of cognitive decline in Parkinson's disease patients.
animal alpha-synucleins (aSNs) share three substitutions compared to human aSN: A53T, G68E, and V95G
analysis of membrane curvature sensing by amphipathic helices using alpha-synuclein and annexin B12 [ANXB12]
Immunocytochemistry shows alpha synuclein localized to the Golgi apparatus and vesicles of bovine adrenal medullary chromaffin cells, consistent with its putative role in vesicular function within synapses.
Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Four alternatively spliced transcripts encoding two different isoforms have been identified for this gene.
, alpha SYN
, non-A beta component of AD amyloid
, non-A4 component of amyloid
, non A-beta component of AD amyloid
, synuclein alpha-140
, alpha synuclein