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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
Show all 2 Pubmed References
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
Taken together, these data suggest that PREP can enhance alpha-synuclein toxicity in vivo.
oligodendrocytes but not neurons transform misfolded alpha-Syn into a glial cytoplasmic inclusions-like strain, highlighting the fact that distinct alpha-Syn strains are generated by different intracellular milieus
Cardiolipin exposure on the outer mitochondrial membrane modulates alpha-synuclein in Parkinson's disease and cultured cardiomyocyte models.
A53T SNCA missense mutation caused impaired light entrainment of the circadian system in mice.
Induction of the Immunoproteasome Subunit Lmp7 Links Proteostasis and Immunity in alpha-Synuclein Aggregation Disorders
In this study, we assessed the spread of pathology following a localized induction of alphaS inclusions in the lumbar spinal cord following a unilateral injection in the sciatic nerve. Using this paradigm, we demonstrated the ability for alphaS inclusion spread and/or induction along neuroanatomical tracts within the CNS of two alphaS-overexpressing mouse models.
These results indicated that integrin CD11b mediates alpha-synuclein-induced NOX2 activation through a RhoA-dependent pathway.
High SNCA expression is associated with Parkinson's disease.
Snca regulates bone network homeostasis and ovariectomy-induced bone loss
These findings provide evidence for a novel mechanism underlying the protective effects of PINK1 against alpha-syn-induced neurodegeneration and highlight a novel therapeutic target for Parkinson's disease treatment.
study demonstrates that PLK-2 activity can rapidly change cellular alpha-synuclein levels in cell models and in mice brains, but this process does not require phosphorylation of S129. Instead, it operates via regulation of alpha-synuclein mRNA transcription in an open reading frame-dependent manner
the presented data link the Parkinson's disease-associated gene alpha-synuclein to the neuronal cell fate determinant TRIM32.
alpha-synuclein levels can be reduced in neurons without impairing (or improving) mitochondrial bioenergetics or distribution
Study shows that the age-dependent alpha-syn accumulation is correlated with an elevation of TRPC3 in the mitochondrial fractions isolated from monkey and mouse brains. In animal and cell models, alpha-syn overexpression was accompanied by an elevation of alpha-syn and TRPC3 in the mitochondrial fractions, and alpha-syn downregulation was associated with a reduction of the mitochondrial alpha-syn and TRPC3.
plasma concentrations of alpha-synuclein were significantly higher in exercising mice compared to control mice. Our results suggest that exercise may slow the progression of Parkinson's disease by preventing abnormal protein aggregation in brain
revealed a prominent modulating effect of alpha-synuclein on the developing DA neurons in substantia nigra (SN) which is the most affected region in PD patients. Yet, alpha-synuclein had no effect on the formation of DA neurons in ventral tegmental area which is much less susceptible to degeneration in PD patients.
These new mouse lines are invaluable for fast identification of cells with inactivation of Snca by Cre-recombination and represent useful tools for in vivo studies of alpha-synuclein function and dysfunction.
Retinal iron dyshomeostasis due to impaired or altered function of alpha-syn contributes to the visual symptoms associated with Parkinson disease.
Results obtained with immuno-spin trapping and immunoprecipitation experiments confirmed formation of alpha-synuclein radicals in dopaminergic neurons of maneb and paraquat exposed mice.
Study showed that intracerebral injection of synthetic alpha-synuclein fibrils into adult wild-type marmoset brains (caudate nucleus and/or putamen) resulted in spreading of abundant alpha-synuclein pathologies, which were positive for various antibodies to alpha-synuclein, including phospho Ser129-specific antibody, anti-ubiquitin and anti-p62 antibodies, at three months after injection.
the association of alphaSyn with the mitochondria, which is modulated by protein mutation and dosage, influences mitochondrial transport and morphology, highlighting its relevance in a common pathway impaired in Parkinson's disease.
Fibril binding may represent a generic mechanism by which chaperone-active sHsps interact with aggregation-prone proteins, highlighting the potential to target sHsp activity to prevent or disrupt the onset and progression of alpha-syn aggregation associated with alpha-synucleinopathies
Pathogenic Parkinson's disease-linked DNAJC13 mutation induces aberrant endosomal retention of alpha-synuclein, which might predispose to the neurodegenerative process that leads to Parkinson's disease.
Elevated sPD-1 concentration in the blood blocks PD-1/PD-L1 signaling pathway.
This meta-analysis further indicates that the SNCA rs11931074 polymorphism contributes to PD susceptibility.
The structure of the alpha-synuclein fibril polymorphs.
TPPP/p25 is co-enriched and co-localized with alpha-synuclein in brain inclusions of Parkinson's disease patients. Interaction of alpha-synuclein with various deletion mutants and fragments of TPPP/p25 were characterized.
Calcium binds to the C terminus of alpha-synuclein, therewith increasing its lipid-binding capacity. Using CEST-NMR, we reveal that alpha-synuclein interacts with isolated synaptic vesicles with two regions, the N terminus, already known from studies on SUVs, and additionally via its C terminus, which is regulated by the binding of calcium.
Extracellular vesicles can mediate spreading of harmful alpha-syn species and thereby contribute to the pathology in alpha-synucleinopathies.
The expression of programmed cell death protein-1 in tumor-infiltrating lymphocytes is related to immune disorder.
this is the first report showing endogenous monitoring of a-SYN transcription, thus making it an efficient drug screening tool that can be used for therapeutic intervention in PD.
Study found that lipid vesicles affect the aggregation process of the modified oligomeric species under acidic conditions and that monomeric alpha-syn also plays a role in this mechanism. Furthermore, we demonstrate that the degree of toxicity of 4-hydroxy-2-nonenal-alpha-syn is related to the level of aggregation.
In this study, CMAP correction of CHARMM27 force field is found to overestimate the helical conformation, while GROMOS96 53A6 is found to most successfully capture the conformational dynamics of a-syn b-hairpin fragment as elicited from NMR.
The activation of PD-1 and TIGIT may exert negative regulatory effects and inhibit the immune response to cancer cells, resulting in immune escape of cancer cells.
nicotine also exerts a beneficial effect on aggregation of alpha-synuclein. The alkaloid increases the lag time of the nucleation step and reduces the build-up of the more toxic oligomeric species in a concentration-dependent manner.
We have also demonstrated that UCHL1 S-nitrosylation provides seeding for faster aggregation of a-synuclein. Finally, the in vitro nitrosylation of UCHL1 was corroborated with rotenone induced mouse model of PD
The results of this pilot study suggest that quantitative measurement of immunoreactivity to alpha-synuclein in nerve fibers from minor salivary glands in Parkinson's disease.
PD-1 expression was augmented on CD8+ T cells in BALF of a patient with smoldering adult T-cell lymphoma and Pneumocystis jiroveci pneumonia. This suggested that the PD-1-PD-L1 system may suppress not only antitumor immunity but also host defense against pathogens and thereby allow establishment of chronic HTLV-1 infection and immunodeficiency.
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