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Journal articles on the topic 'Β-synuclein'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Surguchev, Alexei A., Fatemeh Nouri Emamzadeh, and Andrei Surguchov. "Cell Responses to Extracellular α-Synuclein." Molecules 24, no. 2 (January 15, 2019): 305. http://dx.doi.org/10.3390/molecules24020305.

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Synucleins are small naturally unfolded proteins involved in neurodegenerative diseases and cancer. The family contains three members: α-, β-, and -synuclein. α-Synuclein is the most thoroughly investigated because of its close association with Parkinson's disease (PD), dementia with Lewy bodies and multiple system atrophy. Until recently, the synuclein's research was mainly focused on their intracellular forms. However, new studies highlighted the important role of extracellular synucleins. Extracellular forms of synucleins propagate between various types of cells, bind to cell surface receptors and transmit signals, regulating numerous intracellular processes. Here we give an update of the latest results about the mechanisms of action of extracellular synucleins, their binding to cell surface receptors, effect on biochemical pathways and the role in neurodegeneration and neuroinﬂammation.

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2

JENSEN, Poul H., Peter HØJRUP, Henrik HAGER, Morten S. NIELSEN, Linda JACOBSEN, Ole F. OLESEN, Jørgen GLIEMANN, and Ross JAKES. "Binding of Aβ to α- and β-synucleins: identification of segments in α-synuclein/NAC precursor that bind Aβ and NAC." Biochemical Journal 323, no. 2 (April 15, 1997): 539–46. http://dx.doi.org/10.1042/bj3230539.

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NAC, a 35-residue peptide derived from the neuronal protein α-synuclein/NAC precursor, is tightly associated with Aβ fibrils in Alzheimer's disease amyloid, and α-synuclein has recently been shown to bind Aβ in vitro. We have studied the interaction between Aβ and synucleins, aiming at determining segments in α-synuclein that can account for the binding, as well as identifying a possible interaction between Aβ and the β-type synuclein. We report that Aβ binds to native and recombinant α-synuclein, and to β-synuclein in an SDS-sensitive interaction (IC50 approx. 20 μM), as determined by chemical cross-linking and solid-phase binding assays. α-Synuclein and β-synuclein were found to stimulate Aβ-aggregation in vitro to the same extent. The synucleins also displayed Aβ-inhibitable binding of NAC and they were capable of forming dimers. Using proteolytic fragmentation of α-synuclein and cross-linking to 125I-Aβ, we identified two consecutive binding domains (residues 1–56 and 57–97) by Edman degradation and mass spectrometric analysis, and a synthetic peptide comprising residues 32–57 possessed Aβ-binding activity. To test further the possible significance in pathology, α-synuclein was biotinylated and shown to bind specifically to amyloid plaques in a brain with Alzheimer's disease. It is proposed that the multiple Aβ-binding sites in α-synuclein are involved in the development of amyloid plaques.

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3

Wilson, Christina A., Diane D. Murphy, Benoit I. Giasson, Bin Zhang, John Q. Trojanowski, and Virginia M. Y. Lee. "Degradative organelles containing mislocalized α- and β-synuclein proliferate in presenilin-1 null neurons." Journal of Cell Biology 165, no. 3 (May 3, 2004): 335–46. http://dx.doi.org/10.1083/jcb.200403061.

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Presenilin-1 null mutation (PS1 −/−) in mice is associated with morphological alterations and defects in cleavage of transmembrane proteins. Here, we demonstrate that PS1 deficiency also leads to the formation of degradative vacuoles and to the aberrant translocation of presynaptic α- and β-synuclein proteins to these organelles in the perikarya of primary neurons, concomitant with significant increases in the levels of both synucleins. Stimulation of autophagy in control neurons produced a similar mislocalization of synucleins as genetic ablation of PS1. These effects were not the result of the loss of PS1 γ-secretase activity; however, dysregulation of calcium channels in PS1 −/− cells may be involved. Finally, colocalization of α-synuclein and degradative organelles was observed in brains from patients with the Lewy body variant of AD. Thus, aberrant accumulation of α- and β-synuclein in degradative organelles are novel features of PS1 −/− neurons, and similar events may promote the formation of α-synuclein inclusions associated with neurodegenerative diseases.

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4

Hashimoto, Makoto, Edward Rockenstein, Michael Mante, Margaret Mallory, and Eliezer Masliah. "β-Synuclein Inhibits α-Synuclein Aggregation." Neuron 32, no. 2 (October 2001): 213–23. http://dx.doi.org/10.1016/s0896-6273(01)00462-7.

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5

Somayaji, Mahalakshmi, Stefano Cataldi, Se Joon Choi, Robert H. Edwards, Eugene V. Mosharov, and David Sulzer. "A dual role for α-synuclein in facilitation and depression of dopamine release from substantia nigra neurons in vivo." Proceedings of the National Academy of Sciences 117, no. 51 (December 3, 2020): 32701–10. http://dx.doi.org/10.1073/pnas.2013652117.

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α-Synuclein is expressed at high levels at presynaptic terminals, but defining its role in the regulation of neurotransmission under physiologically relevant conditions has proven elusive. We report that, in vivo, α-synuclein is responsible for the facilitation of dopamine release triggered by action potential bursts separated by short intervals (seconds) and a depression of release with longer intervals between bursts (minutes). These forms of presynaptic plasticity appear to be independent of the presence of β- and γ-synucleins or effects on presynaptic calcium and are consistent with a role for synucleins in the enhancement of synaptic vesicle fusion and turnover. These results indicate that the presynaptic effects of α-synuclein depend on specific patterns of neuronal activity.

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6

Sriwimol, Wilaiwan, and Pornprot Limprasert. "Significant Changes in Plasma Alpha-Synuclein and Beta-Synuclein Levels in Male Children with Autism Spectrum Disorder." BioMed Research International 2018 (2018): 1–7. http://dx.doi.org/10.1155/2018/4503871.

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Alpha-synuclein (α-synuclein) and beta-synuclein (β-synuclein) are presynaptic proteins playing important roles in neuronal plasticity and synaptic vesicle regulation. To evaluate the association of these two proteins and autism spectrum disorder (ASD), we investigated the plasma α-synuclein and β-synuclein levels in 39 male children with ASD (2 subgroups: 25 autism and 14 pervasive developmental disorder-not otherwise specified (PDD-NOS)) comparing with 29 sex- and age-matched controls by using enzyme-linked immunosorbent assay (ELISA). We first determined the levels of these two proteins in the ASD subgroups and found that there were no significant differences in both plasma α-synuclein and β-synuclein levels in the autism and PDD-NOS groups. Thus, we could combine the 2 subgroups into one ASD group. Interestingly, the mean plasma α-synuclein level was significantly lower (P<0.001) in the ASD children (10.82±6.46 ng/mL) than in the controls (29.47±18.62 ng/mL), while the mean plasma β-synuclein level in the ASD children (1344.19±160.26 ng/mL) was significantly higher (P<0.05) than in the controls (1219.16±177.10 ng/mL). This is the first study examining the associations between α-synuclein and β-synuclein and male ASD patients. We found that alterations in the plasma α-synuclein and β-synuclein levels might be implicated in the association between synaptic abnormalities and ASD pathogenesis.

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7

Hosford, Patrick S., Natalia Ninkina, Vladimir L. Buchman, Jeffrey C. Smith, Nephtali Marina, and Shahriar SheikhBahaei. "Synuclein Deficiency Results in Age-Related Respiratory and Cardiovascular Dysfunctions in Mice." Brain Sciences 10, no. 9 (August 24, 2020): 583. http://dx.doi.org/10.3390/brainsci10090583.

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Synuclein (α, β, and γ) proteins are highly expressed in presynaptic terminals, and significant data exist supporting their role in regulating neurotransmitter release. Targeting the gene encoding α-synuclein is the basis of many animal models of Parkinson’s disease (PD). However, the physiological role of this family of proteins in not well understood and could be especially relevant as interfering with accumulation of α-synuclein level has therapeutic potential in limiting PD progression. The long-term effects of their removal are unknown and given the complex pathophysiology of PD, could exacerbate other clinical features of the disease, for example dysautonomia. In the present study, we sought to characterize the autonomic phenotypes of mice lacking all synucleins (α, β, and γ; αβγ−/−) in order to better understand the role of synuclein-family proteins in autonomic function. We probed respiratory and cardiovascular reflexes in conscious and anesthetized, young (4 months) and aged (18–20 months) αβγ−/− male mice. Aged mice displayed impaired respiratory responses to both hypoxia and hypercapnia when breathing activities were recorded in conscious animals using whole-body plethysmography. These animals were also found to be hypertensive from conscious blood pressure recordings, to have reduced pressor baroreflex gain under anesthesia, and showed reduced termination of both pressor and depressor reflexes. The present data demonstrate the importance of synuclein in the normal function of respiratory and cardiovascular reflexes during aging.

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8

Snyder, Heather, Kwame Mensah, Cindy Hsu, Makoto Hashimoto, Irina G. Surgucheva, Barry Festoff, Andrei Surguchov, Eliazer Masliah, Andreas Matouschek, and Benjamin Wolozin. "β-Synuclein Reduces Proteasomal Inhibition by α-Synuclein but Not γ-Synuclein." Journal of Biological Chemistry 280, no. 9 (December 9, 2004): 7562–69. http://dx.doi.org/10.1074/jbc.m412887200.

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9

Fan, Yuxin, Pornprot Limprasert, Ian V. J. Murray, Annette C. Smith, Virginia M. Y. Lee, John Q. Trojanowski, Bryce L. Sopher, and Albert R. La Spada. "β-synuclein modulates α-synuclein neurotoxicity by reducing α-synuclein protein expression." Human Molecular Genetics 15, no. 20 (September 7, 2006): 3002–11. http://dx.doi.org/10.1093/hmg/ddl242.

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10

Geng, Xuehui, Haiyan Lou, Jian Wang, Lehong Li, Alexandra L. Swanson, Ming Sun, Donna Beers-Stolz, Simon Watkins, Ruth G. Perez, and Peter Drain. "α-Synuclein binds the KATP channel at insulin-secretory granules and inhibits insulin secretion." American Journal of Physiology-Endocrinology and Metabolism 300, no. 2 (February 2011): E276—E286. http://dx.doi.org/10.1152/ajpendo.00262.2010.

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α-Synuclein has been studied in numerous cell types often associated with secretory processes. In pancreatic β-cells, α-synuclein might therefore play a similar role by interacting with organelles involved in insulin secretion. We tested for α-synuclein localizing to insulin-secretory granules and characterized its role in glucose-stimulated insulin secretion. Immunohistochemistry and fluorescent sulfonylureas were used to test for α-synuclein localization to insulin granules in β-cells, immunoprecipitation with Western blot analysis for interaction between α-synuclein and KATP channels, and ELISA assays for the effect of altering α-synuclein expression up or down on insulin secretion in INS1 cells or mouse islets, respectively. Differences in cellular phenotype between α-synuclein knockout and wild-type β-cells were found by using confocal microscopy to image the fluorescent insulin biosensor Ins-C-emGFP and by using transmission electron microscopy. The results show that anti-α-synuclein antibodies labeled secretory organelles within β-cells. Anti-α-synuclein antibodies colocalized with KATP channel, anti-insulin, and anti-C-peptide antibodies. α-Synuclein coimmunoprecipitated in complexes with KATP channels. Expression of α-synuclein downregulated insulin secretion at 2.8 mM glucose with little effect following 16.7 mM glucose stimulation. α-Synuclein knockout islets upregulated insulin secretion at 2.8 and 8.4 mM but not 16.7 mM glucose, consistent with the depleted insulin granule density at the β-cell surface membranes observed in these islets. These findings demonstrate that α-synuclein interacts with KATP channels and insulin-secretory granules and functionally acts as a brake on secretion that glucose stimulation can override. α-Synuclein might play similar roles in diabetes as it does in other degenerative diseases, including Alzheimer's and Parkinson's diseases.

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11

Liu, Hanhan, Karl Mercieca, Fabian Anders, and Verena Prokosch. "Hydrogen Sulfide and β-Synuclein Are Involved and Interlinked in the Aging Glaucomatous Retina." Journal of Ophthalmology 2020 (April 14, 2020): 1–12. http://dx.doi.org/10.1155/2020/8642135.

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Purpose. Glaucoma, one of the leading causes of irreversible blindness worldwide, is a group of disorders characterized by progressive retinal ganglion cell (RGC) loss. Synucleins, a family of small proteins, have been of interest in studies of neurodegeneration and CNS. However, their roles and functions in glaucoma are still not completely understood and remain to be explored. Our previous studies showed that α-synuclein and H2S play a pivotal role in glaucoma. This study aims to (1) elucidate the potential roles and functions of synucleins in glaucoma throughout aging, (2) investigate the interaction between the synucleins and H2S, and better understand the mechanism of H2S in neuroprotection. Methods. The chronic IOP elevation model was carried out in 12 animals at different ages (3 months and 14 months), and RGCs were quantified by Brn3a staining. Mass spectrometric-assisted proteomics analysis was employed to measure synuclein levels and H2S producing proteins in retina. Secondly, the acute IOP elevation model was carried out in 12 juvenile animals, with or without intravitreal injection of GYY4137 (a H2S donor). RGCs were quantified along with the abundancy of synucleins. Results. RGCs and β-synuclein (SNCB) are significantly changed in old animals. Under chronic IOP elevation, there is a significant RGC loss in old animals, whereas no significant change in young animals; SNCB is significantly downregulated and 3MST is significantly upregulated in young animals due to IOP, while no significant changes in old ones are notable. Under acute IOP elevation (approx. 55 mmHg), a significant RGC loss is observed; exogenous H2S significantly reduced RGC loss and downregulated SNCB levels. Conclusion. The present study indicates a strong link between ageing and SNCB regulation. In young animals SNCB is downregulated going along with less RGC loss. Furthermore, increasing endogenous H2S is effective to downregulate SNCB and is neuroprotective against acute IOP elevation.

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12

Lee, Daekyun, Seung R. Paik, and Kwan Yong Choi. "β-Synuclein exhibits chaperone activity more efficiently than α-synuclein." FEBS Letters 576, no. 1-2 (September 15, 2004): 256–60. http://dx.doi.org/10.1016/j.febslet.2004.08.075.

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13

Williams, Jonathan K., Xue Yang, and Jean Baum. "Interactions between the Intrinsically Disordered Proteins β-Synuclein and α-Synuclein." PROTEOMICS 18, no. 21-22 (September 9, 2018): 1800109. http://dx.doi.org/10.1002/pmic.201800109.

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14

Ducas, Vanessa C., and Elizabeth Rhoades. "Quantifying Interactions of β-Synuclein and γ-Synuclein with Model Membranes." Journal of Molecular Biology 423, no. 4 (November 2012): 528–39. http://dx.doi.org/10.1016/j.jmb.2012.08.008.

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15

Yamin, Ghiam, Larissa A. Munishkina, Mikhail A. Karymov, Yuri L. Lyubchenko, Vladimir N. Uversky, and Anthony L. Fink. "Forcing Nonamyloidogenic β-Synuclein To Fibrillate†." Biochemistry 44, no. 25 (June 2005): 9096–107. http://dx.doi.org/10.1021/bi048778a.

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16

Williams, Jonathan K., Xue Yang, Tamr B. Atieh, Michael P. Olson, Sagar D. Khare, and Jean Baum. "Multi-Pronged Interactions Underlie Inhibition of α-Synuclein Aggregation by β-Synuclein." Journal of Molecular Biology 430, no. 16 (August 2018): 2360–71. http://dx.doi.org/10.1016/j.jmb.2018.05.024.

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17

Landau, Meytal. "Getting in charge of β-synuclein fibrillation." Journal of Biological Chemistry 292, no. 39 (September 29, 2017): 16380–81. http://dx.doi.org/10.1074/jbc.h117.780528.

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18

Chia, Sean, Patrick Flagmeier, Johnny Habchi, Veronica Lattanzi, Sara Linse, Christopher M. Dobson, Tuomas P. J. Knowles, and Michele Vendruscolo. "Monomeric and fibrillar α-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Aβ42 aggregates." Proceedings of the National Academy of Sciences 114, no. 30 (July 11, 2017): 8005–10. http://dx.doi.org/10.1073/pnas.1700239114.

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The coaggregation of the amyloid-β peptide (Aβ) and α-synuclein is commonly observed in a range of neurodegenerative disorders, including Alzheimer’s and Parkinson’s diseases. The complex interplay between Aβ and α-synuclein has led to seemingly contradictory results on whether α-synuclein promotes or inhibits Aβ aggregation. Here, we show how these conflicts can be rationalized and resolved by demonstrating that different structural forms of α-synuclein exert different effects on Aβ aggregation. Our results demonstrate that whereas monomeric α-synuclein blocks the autocatalytic proliferation of Aβ42 (the 42-residue form of Aβ) fibrils, fibrillar α-synuclein catalyses the heterogeneous nucleation of Aβ42 aggregates. It is thus the specific balance between the concentrations of monomeric and fibrillar α-synuclein that determines the outcome of the Aβ42 aggregation reaction.

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19

Mori, Fumiaki, Makoto Nishie, Makoto Yoshimoto, Hitoshi Takahashi, and Koichi Wakabayashi. "Reciprocal accumulation of β-synuclein in α-synuclein lesions in multiple system atrophy." NeuroReport 14, no. 14 (October 2003): 1783–86. http://dx.doi.org/10.1097/00001756-200310060-00005.

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20

Yang, Xue, Jonathan K. Williams, and Jean Baum. "β-Synuclein Ameliorates α-Synuclein Toxicity by Modulating Fibril Shedding and Seeding Processes." Biophysical Journal 116, no. 3 (February 2019): 494a. http://dx.doi.org/10.1016/j.bpj.2018.11.2665.

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21

Shameli, Afshin, Wenbin Xiao, Clifford Harding, Howard Meyerson, John Sumodi, and Robert Maitta. "Development Of Mature T Lymphocytes Requires Alpha-Synuclein." Blood 122, no. 21 (November 15, 2013): 3490. http://dx.doi.org/10.1182/blood.v122.21.3490.3490.

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Abstract Synucleins (including α-, β- and γ-synucleins) are a group of proteins that are expressed at high levels in the central nervous system. The physiologic function of these proteins is unknown. Alpha-synuclein has been implicated in the pathogenesis of neurodegenerative disorders such as Parkinson's disease and Lewy body dementia, as it is highly expressed in the Lewy bodies from both disorders. The expression of α-synuclein in hematopoietic system has been shown in erythroid precursors and megakaryocytes in bone marrow, as well as erythrocytes and platelets in peripheral blood. Moreover, some studies demonstrated the expression of α-synuclein on peripheral blood mononuclear cells (PBMC), including B and T lymphocytes, NK cells and monocytes; and its expression is shown to be higher in PBMCs of individuals with Parkinson's disease compared to healthy controls. In order to study the role of α-synuclein in development of different hematopoietic elements, we compared bone marrow, peripheral blood and lymphoid organs of age and sex-matched α-synuclein knock-out (KO) mice and wild type (WT) animals of the same genetic background (n=10). Flow cytometric analysis of bone marrow elements did not show differences in the percentages and absolute numbers of erythroid, megakryocytic and myeloid lineages (data not shown). However, differential complete blood cell count (CBC) showed statistically significant decrease in red blood cell (RBC) count, hemoglobin (Hb) and hematocrit (Hct) in KO mice compared to WT mice. No difference was noted in other RBC indices (Table 1). However, platelets were smaller in KO mice as measured by the mean platelet volume (MPV). There was no difference in the number of platelets and white blood cell (WBC) counts. There was a significant reduction in the percentage of circulating lymphocytes, and associated increase in the percentage of neutrophils and monocytes in KO mice compared to WT mice, although the difference in the number of lymphocytes did not reach statistical significance (Table 1). Flow cytometric analysis of T lymphocytes in thymus and peripheral lymphoid organs demonstrated marked defect in development of mature T cells. There was a significant increase in the number of double negative thymocytes in KO mice associated with significant decrease in the number of single positive T cells. Furthermore, splenic CD4+ and CD8+ T cells were markedly decreased in KO mice, indicating that α-synuclein is required for T cell development (Table 2). In summary, our findings indicate an absolute requirement for α-synuclein in development of mature T lymphocytes. The underlying mechanism for this function is subject of future studies. Moreover, while α-synuclein-deficiency does not affect the development of myeloid lineage and platelets, lack of this protein is associated with lower number of erythrocytes, suggesting its role in development and/or survival red blood cells. Disclosures: No relevant conflicts of interest to declare.

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22

Zhou, Wenbo, Chunmei Long, Anthony Fink, and Vladimir Uversky. "Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro." Open Life Sciences 5, no. 1 (February 1, 2010): 11–20. http://dx.doi.org/10.2478/s11535-009-0071-8.

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Abstractα-Synuclein, a natively unfolded protein aggregation which is implicated in the pathogenesis of Parkinson’s disease and several other neurodegenerative diseases, is known to interact with a great number of unrelated proteins. Some of these proteins, such as β-synuclein and DJ-1, were shown to inhibit α-synuclein aggregation in vitro and in vivo therefore acting as chaperones. Since calbindin-D28K is co-localized with Ca2+ neuronal membrane pumps, and since α-synuclein is also found in the membrane proximity, these two proteins can potentially interact in vivo. Here we show that calbindin-D28K interacts with α-synuclein and inhibits its fibrillation in a calcium-dependent manner, therefore potentially acting as a calcium-dependent chaperone.

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23

Leitao, Andre, Akshay Bhumkar, Dominic Hunter, Yann Gambin, and Emma Sierecki. "Unveiling a Selective Mechanism for the Inhibition of α-Synuclein Aggregation by β-Synuclein." International Journal of Molecular Sciences 19, no. 2 (January 24, 2018): 334. http://dx.doi.org/10.3390/ijms19020334.

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24

Israeli, Eitan, and Ronit Sharon. "β-Synuclein occursin vivoin lipid-associated oligomers and forms hetero-oligomers with α-synuclein." Journal of Neurochemistry 108, no. 2 (January 2009): 465–74. http://dx.doi.org/10.1111/j.1471-4159.2008.05776.x.

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25

Teng, Chao-Yi, Shou-Lin Chang, Meng-Feng Tsai, and Tzong-Yuan Wu. "α-Synuclein and β-synuclein enhance secretion protein production in baculovirus expression vector system." Applied Microbiology and Biotechnology 97, no. 9 (January 12, 2013): 3875–84. http://dx.doi.org/10.1007/s00253-012-4679-7.

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26

Yamin, Ghiam, Larissa A. Munishkina, Mikhail A. Karymov, Yuri L. Lyubchenko, Vladimir N. Uversky, and Anthony L. Fink. "Correction to Forcing Nonamyloidogenic β-Synuclein To Fibrillate." Biochemistry 49, no. 1 (January 12, 2010): 247. http://dx.doi.org/10.1021/bi8016685.

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27

Zibaee, Shahin, Graham Fraser, Ross Jakes, David Owen, Louise C. Serpell, R. Anthony Crowther, and Michel Goedert. "Human β-Synuclein Rendered Fibrillogenic by Designed Mutations." Journal of Biological Chemistry 285, no. 49 (September 10, 2010): 38555–67. http://dx.doi.org/10.1074/jbc.m110.160721.

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28

Tanji, Kunikazu, Fumiaki Mori, Shigeo Nakajo, Tadaatsu Imaizumi, Hidemi Yoshida, Takahiro Hirabayashi, Makoto Yoshimoto, Kei Satoh, Hitoshi Takahashi, and Koichi Wakabayashi. "Expression of β-synuclein in normal human astrocytes." Neuroreport 12, no. 13 (September 2001): 2845–48. http://dx.doi.org/10.1097/00001756-200109170-00018.

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29

Hashimoto, Makoto, Pazit Bar-on, Gilbert Ho, Takato Takenouchi, Edward Rockenstein, Leslie Crews, and Eliezer Masliah. "β-Synuclein Regulates Akt Activity in Neuronal Cells." Journal of Biological Chemistry 279, no. 22 (March 16, 2004): 23622–29. http://dx.doi.org/10.1074/jbc.m313784200.

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30

Zhang, Feng, Li-Na Ji, Lin Tang, Jun Hu, Hong-Yu Hu, Hong-Jie Xu, and Jian-Hua He. "Structural Evidence for α-Synuclein Fibrils Using in Situ Atomic Force Microscopy." Acta Biochimica et Biophysica Sinica 37, no. 2 (February 1, 2005): 113–18. http://dx.doi.org/10.1093/abbs/37.2.113.

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Abstract Human α-synuclein is a presynaptic terminal protein and can form insoluble fibrils that are believed to play an important role in the pathogenesis of several neurodegenerative diseases such as Parkinson's disease, dementia with Lewy bodies and Lewy body variant of Alzheimer's disease. In this paper, in situ atomic force microscopy has been used to study the structural properties of α-synuclein fibrils in solution using two different atomic force microscopy imaging modes: tapping mode and contact mode. In the in situ contact mode atomic force microscopy experiments α-synuclein fibrils quickly broke into fragments, and a similar phenomenon was found using tapping mode atomic force microscopy in which α-synuclein fibrils were incubated with guanidine hydrochloride (0.6 M). The α-synuclein fibrils kept their original filamentous topography for over 1 h in the in situ tapping mode atomic force microscopy experiments. The present results provide indirect evidence on how β-sheets assemble into α-synuclein fibrils on a nanometer scale.

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31

Ho, Ying-Jui, Jun-Cheng Weng, Chih-Li Lin, Mei-Shiuan Shen, Hsin-Hua Li, Wen-Chieh Liao, Nu-Man Tsai, Ching-Sui Hung, Te-Jen Lai, and I.-Yen Lee. "Ceftriaxone Treatment for Neuronal Deficits: A Histological and MEMRI Study in a Rat Model of Dementia with Lewy Bodies." Behavioural Neurology 2018 (August 1, 2018): 1–9. http://dx.doi.org/10.1155/2018/4618716.

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Dementia with Lewy bodies (DLB) is characterized by neuronal deficits and α-synuclein inclusions in the brain. Ceftriaxone (CEF), a β-lactam antibiotic, has been suggested as a therapeutic agent in several neurodegenerative disorders for its abilities to counteract glutamate-mediated toxicity and to block α-synuclein polymerization. By using manganese-enhanced magnetic resonance imaging (MEMRI) and immunohistochemistry, we measured the effects of CEF on neuronal activity and α-synuclein accumulation in the brain in a DLB rat model. The data showed that CEF corrected neuronal density and activity in the hippocampal CA1 area, suppressed hyperactivity in the subthalamic nucleus, and reduced α-synuclein accumulation, indicating that CEF is a potential agent in the treatment of DLB.

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32

Unal-Cevik, Isin, Yasemin Gursoy-Ozdemir, Muge Yemisci, Sevda Lule, Gunfer Gurer, Alp Can, Veronica Müller, Philip J. Kahle, and Turgay Dalkara. "Alpha-Synuclein Aggregation Induced by Brief Ischemia Negatively Impacts Neuronal Survival in vivo: A Study in [A30P]alpha-Synuclein Transgenic Mouse." Journal of Cerebral Blood Flow & Metabolism 31, no. 3 (September 29, 2010): 913–23. http://dx.doi.org/10.1038/jcbfm.2010.170.

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Alpha-synuclein oligomerization and aggregation are considered to have a role in the pathogenesis of neurodegenerative diseases. However, despite numerous in vitro studies, the impact of aggregates in the intact brain is unclear. In vitro, oxidative/nitrative stress and acidity induce α-synuclein oligomerization. These conditions favoring α-synuclein fibrillization are present in the ischemic brain, which may serve as an in vivo model to study α-synuclein aggregation. In this study, we show that 30-minute proximal middle cerebral artery (MCA) occlusion and 72 hours reperfusion induce oligomerization of wild-type α-synuclein in the ischemic mouse brain. The nonamyloidogenic isoform β-synuclein did not form oligomers. Alpha-synuclein aggregates were confined to neurons and colocalized with ubiquitin immunoreactivity. We also found that 30 minutes proximal MCA occlusion and 24 hours reperfusion induced larger infarcts in C57BL/6(Thy1)-h[A30P]alphaSYN transgenic mice, which have an increased tendency to form synuclein fibrils. Trangenics also developed more selective neuronal necrosis when subjected to 20 minutes distal MCA occlusion and 72 hours reperfusion. Enhanced 3-nitrotyrosine immunoreactivity in transgenic mice suggests that oxidative/nitrative stress may be one of the mechanisms mediating aggregate toxicity. Thus, the increased vulnerability of transgenic mice to ischemia suggests that α-synuclein aggregates not only form during ischemia but also negatively impact neuronal survival, supporting the idea that α-synuclein misfolding may be neurotoxic.

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El-Agnaf, Omar M. A., and G. Brent Irvine. "Aggregation and properties of α‒synuclein and related proteins." Spectroscopy 15, no. 3,4 (2001): 141–50. http://dx.doi.org/10.1155/2001/939274.

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α-Synuclein has been identified as a component of intracellular fibrillar protein deposits in several neurodegenerative diseases, and two mutant forms have been associated with early onset Parkinson's disease. A fragment of α-synuclein has also been identified as the non-Aβ component of Alzheimer's disease amyloid (NAC). Ageing solutions of α-synuclein and NAC leads to formation of β-sheet, detectable by circular dichroism spectroscopy, and aggregation to form amyloid-like fibrils, detectable by electron microscopy. Differences in the rates of aggregation of the fibrils formed by α-synuclein and the two mutant proteins are presented. The toxicity of α-synuclein and related peptides towards neurons is also discussing in relation to the aetiology of neurodegenerative diseases.Experiments on fragments of NAC have enabled the region of NAC responsible for its aggregation and toxicity to be identified.

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Abramov, Andrey Y., Alexey V. Berezhnov, Evgeniya I. Fedotova, Valery P. Zinchenko, and Ludmila P. Dolgacheva. "Interaction of misfolded proteins and mitochondria in neurodegenerative disorders." Biochemical Society Transactions 45, no. 4 (July 21, 2017): 1025–33. http://dx.doi.org/10.1042/bst20170024.

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The number of the people affected by neurodegenerative disorders is growing dramatically due to the ageing of population. The major neurodegenerative diseases share some common pathological features including the involvement of mitochondria in the mechanism of pathology and misfolding and the accumulation of abnormally aggregated proteins. Neurotoxicity of aggregated β-amyloid, tau, α-synuclein and huntingtin is linked to the effects of these proteins on mitochondria. All these misfolded aggregates affect mitochondrial energy metabolism by inhibiting diverse mitochondrial complexes and limit ATP availability in neurones. β-Amyloid, tau, α-synuclein and huntingtin are shown to be involved in increased production of reactive oxygen species, which can be generated in mitochondria or can target this organelle. Most of these aggregated proteins are capable of deregulating mitochondrial calcium handling that, in combination with oxidative stress, lead to opening of the mitochondrial permeability transition pore. Despite some of the common features, aggregated β-amyloid, tau, α-synuclein and huntingtin have diverse targets in mitochondria that can partially explain neurotoxic effect of these proteins in different brain regions.

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Shameli, Afshin, Yan Zheng, Clifford Harding, Howard Meyerson, and Robert Maitta. "Alpha-Synuclein Deficiency Is Associated with Defective Th2 Differentiation and Enhanced Regulatory T Cell Development." Blood 124, no. 21 (December 6, 2014): 1424. http://dx.doi.org/10.1182/blood.v124.21.1424.1424.

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Abstract Synucleins (including α-, β- and γ-synucleins) are a group of proteins that are highly expressed in the central nervous system. Alpha-synuclein, in particular, has been implicated in the pathogenesis of neurodegenerative disorders known as synucleinopathies. The function of these proteins in other organ systems is largely unknown. Some studies have demonstrated expression of α-synuclein on peripheral blood mononuclear cells (PBMC), including B and T lymphocytes, NK cells and monocytes; and its expression has been shown to be higher in PBMCs of individuals with Parkinson’s compared to healthy controls. We have recently shown that α-synuclein-deficiency is associated with marked defect in development of mature B and T lymphocytes. In particular, we showed enhanced negative selection of developing thymic T cells in the absence α-synuclein. Furthermore, we demonstrated that α-synuclein-deficiency is associated with an impaired IgG response to T cell-dependent antigens. Here we used age and sex-matched α-synuclein knock-out (KO) and wild type (WT) mice to further investigate the lineage differentiation and activation of T cells. We found that few splenic T cells that develop in KO mice contain a higher percentage of CD8+ T cell expressing early activation markers CD69 (7.6 ± 0.09 for KO vs. 5.3 ± 0.23 for WT, p=0.005, figure 1A) and CD49d (12.97 ± 0.3 for KO vs. 7.32 ± 0.6 for WT, p=0.006, figure 1A). A similar trend was noted for CD4+ CD49d+ T cells, although the difference did not reach statistical significance (23.90 ± 3.48 for KO vs.13.23 ± 0.73 for WT, p=0.086, figure 1A). No difference was noted in the expression of late activation marker CD44, and lymph node homing marker CD62L. This was associated with significantly increased IL-2 production from KO CD4+ T cells (OD 2.70 ± 0.12 for KO vs.1.05 ± 0.39 for WT, p=0.002, figure 1B) and a trend for increased IFN-γ production from KO CD4+ T cells (OD 2.89 ± 0.33 for KO vs.2.12 ± 0.59 for WT, p=0.12) after in vitro activation with anti-CD3/anti-CD28 beads. Interestingly, In vitro activation of splenic CD4+ T cells resulted in significantly reduced IL-4 production from KO T cells (OD 0.20 ± 0.14 for KO, vs. 0.74 ± 0.31 for WT, p=0.05, Figure 2) suggesting a defective Th2 differentiation in KO CD4+ T cells. Further flow cytometric analysis of T cells showed that while thymic Foxp3+ CD4+ regulatory T cells are significantly reduced in KO mice (3.07 ±0.35 for KO vs. 5.00 ± 0.87 for WT, p=0.02, Figure 3), the percentage of splenic Foxp3+ CD4+ T cells is higher in the KO mice compared to WT mice (18.33 ± 4.90 for KO vs.10.33 ± 1.39 for WT, p=0.05, Figure 3). No difference was noted among NK cells from KO and WT mice. In summary, we demonstrate a role for α-synuclein in lineage differentiation and function of T cells. While α-synuclein-deficiency leads to a significant defect in development of mature T cells, the small population of cells that do mature, express higher levels of early activation markers, and produce higher levels of IL-2 upon antigenic stimulation. Of interest, these cells are defective in IL-4 production. Additionally, we also show that α-synuclein-deficiency is associated with a higher percentage of peripheral CD4+ Foxp3+ T cells, a finding that might be explained by higher levels of IL-2 production by α-synuclein-deficient CD4+ T cells, although a direct effect of α-synuclein on the survival of regulatory T cells cannot be excluded. The underlying mechanism for the function α-synuclein in development and function of T cells is subject of future studies. Disclosures No relevant conflicts of interest to declare.

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De Ricco, Riccardo, Daniela Valensin, Simone Dell'Acqua, Luigi Casella, Christelle Hureau, and Peter Faller. "Copper(I/II), α/β-Synuclein and Amyloid-β: Menage à Trois?" ChemBioChem 16, no. 16 (September 25, 2015): 2319–28. http://dx.doi.org/10.1002/cbic.201500425.

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Angelova, Dafina M., Hannah B. L. Jones, and David R. Brown. "Levels of α‐ and β‐synuclein regulate cellular susceptibility to toxicity from α‐synuclein oligomers." FASEB Journal 32, no. 2 (January 4, 2018): 995–1006. http://dx.doi.org/10.1096/fj.201700675r.

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Tsigelny, Igor F., Pazit Bar-On, Yuriy Sharikov, Leslie Crews, Makoto Hashimoto, Mark A. Miller, Steve H. Keller, Oleksandr Platoshyn, Jason X. J. Yuan, and Eliezer Masliah. "Dynamics of α-synuclein aggregation and inhibition of pore-like oligomer development by β-synuclein." FEBS Journal 274, no. 7 (March 5, 2007): 1862–77. http://dx.doi.org/10.1111/j.1742-4658.2007.05733.x.

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Park, June-Young, and Peter T. Lansbury. "β-Synuclein Inhibits Formation of α-Synuclein Protofibrils: A Possible Therapeutic Strategy against Parkinson's Disease†." Biochemistry 42, no. 13 (April 2003): 3696–700. http://dx.doi.org/10.1021/bi020604a.

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Bhayye, Sagar S., and Achintya Saha. "QSAR and QAAR Studies on Mixtures of 3-(Benzylidene)Indolin-2-One Isomers as Leads to Develop PET Radiotracers for Detection of Parkinson's Disease." International Journal of Quantitative Structure-Property Relationships 3, no. 2 (July 2018): 95–114. http://dx.doi.org/10.4018/ijqspr.2018070107.

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Deposition of α–synuclein, tau and β–amyloid protein plaques in brain leads to neurodegeneration. A series of indolin derivatives, which can bind to α–synuclein and detect Parkinson's disease (PD), were used for development of QSAR and QAAR models. It is the first attempt of QSAR for any radiotracer agents used for detection of PD. The binding affinity against α–synuclein was used as dependent variable while independent variables, such as structural, topological, E-state keys, electronic, molecular shape analysis and spatial molecular descriptors were used for QSAR modeling. For QAAR modeling, the binding affinities of molecules for tau and β–amyloid along with different molecular descriptors were used as independent variables. All models were successfully developed using multiple linear regression method, and validated internally and externally, based on different standard criteria. This article describes how the derived models postulate that conformation of molecules and presence of unsaturated hydrocarbon chains, nitro, methoxy and amine functionalities play an important role in determining binding affinity.

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Alsufyani, Faisal, and Shiv Pillai. "Luring T cells into a gray area." Science Immunology 4, no. 34 (April 5, 2019): eaax3917. http://dx.doi.org/10.1126/sciimmunol.aax3917.

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EI-Agnaf, O. M. A., and G. B. Irvine. "Aggregation and neurotoxicity of α-synuclein and related peptides." Biochemical Society Transactions 30, no. 4 (August 1, 2002): 559–65. http://dx.doi.org/10.1042/bst0300559.

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Fibrillar deposits of α-synuclein occur in several neurodegenerative diseases. Two mutant forms of α-synuclein have been associated with early-onset Parkinson's disease, and a fragment has been identified as the non-amyloid-β peptide component of Alzheimer's disease amyloid (NAC). Upon aging, solutions of α-synuclein and NAC change conformation to β-sheet, detectable by CD spectroscopy, and form oligomers that deposit as amyloid-like fibrils, detectable by electron microscopy. These aged peptides are also neurotoxic. Experiments on fragments of NAC have enabled the region of NAC responsible for its aggregation and toxicity to be identified. NAC(8–18) is the smallest fragment that aggregates, as indicated by the concentration of peptide remaining in solution after 3 days, and forms fibrils, as determined by electron microscopy. Fragments NAC(8–18) and NAC(8–16) are toxic, whereas NAC(12–18), NAC(9–16) and NAC(8–15) are not. Hence residues 8–16 of NAC comprise the region crucial for toxicity. Toxicity induced by α-synuclein, NAC and NAC(1–18) oligomers occurs via an apoptotic mechanism, possibly initiated by oxidative damage, since these peptides liberate hydroxyl radicals in the presence of iron. Molecules with anti-aggregational and/or antioxidant properties may therefore be potential therapeutic agents.

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Zhao, Na, Olivia N. Attrebi, Yingxue Ren, Wenhui Qiao, Berkiye Sonustun, Yuka A. Martens, Axel D. Meneses, et al. "APOE4 exacerbates α-synuclein pathology and related toxicity independent of amyloid." Science Translational Medicine 12, no. 529 (February 5, 2020): eaay1809. http://dx.doi.org/10.1126/scitranslmed.aay1809.

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The apolipoprotein E (APOE) ε4 allele is the strongest genetic risk factor for late-onset Alzheimer’s disease mainly by driving amyloid-β pathology. Recently, APOE4 has also been found to be a genetic risk factor for Lewy body dementia (LBD), which includes dementia with Lewy bodies and Parkinson’s disease dementia. How APOE4 drives risk of LBD and whether it has a direct effect on α-synuclein pathology are not clear. Here, we generated a mouse model of synucleinopathy using an adeno-associated virus gene delivery of α-synuclein in human APOE-targeted replacement mice expressing APOE2, APOE3, or APOE4. We found that APOE4, but not APOE2 or APOE3, increased α-synuclein pathology, impaired behavioral performances, worsened neuronal and synaptic loss, and increased astrogliosis at 9 months of age. Transcriptomic profiling in APOE4-expressing α-synuclein mice highlighted altered lipid and energy metabolism and synapse-related pathways. We also observed an effect of APOE4 on α-synuclein pathology in human postmortem brains with LBD and minimal amyloid pathology. Our data demonstrate a pathogenic role of APOE4 in exacerbating α-synuclein pathology independent of amyloid, providing mechanistic insights into how APOE4 increases the risk of LBD.

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Bachhuber, Teresa, Natalie Katzmarski, Joanna F. McCarter, Desiree Loreth, Sabina Tahirovic, Frits Kamp, Claudia Abou-Ajram, et al. "Inhibition of amyloid-β plaque formation by α-synuclein." Nature Medicine 21, no. 7 (June 22, 2015): 802–7. http://dx.doi.org/10.1038/nm.3885.

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Taschenberger, Grit, Johan Toloe, Julia Tereshchenko, Jasper Akerboom, Pauline Wales, Roland Benz, Stefan Becker, et al. "β-synuclein aggregates and induces neurodegeneration in dopaminergic neurons." Annals of Neurology 74, no. 1 (July 2013): 109–18. http://dx.doi.org/10.1002/ana.23905.

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Spillantini, Maria Grazia, Aspasia Divane, and Michel Goedert. "Assignment of Human α-Synuclein (SNCA) and β-Synuclein (SNCB) Genes to Chromosomes 4q21 and 5q35." Genomics 27, no. 2 (May 1995): 379–81. http://dx.doi.org/10.1006/geno.1995.1063.

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Park, Sang Myun, Han Young Jung, Hyun Ok Kim, Hyangshuk Rhim, Seung R. Paik, Kwang Chul Chung, Jeon Han Park, and Jongsun Kim. "Evidence that α-synuclein functions as a negative regulator of Ca++-dependent α-granule release from human platelets." Blood 100, no. 7 (October 1, 2002): 2506–14. http://dx.doi.org/10.1182/blood.v100.7.2506.

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α-Synuclein has been implicated in the pathogenesis of Parkinson disease (PD) and related neurodegenerative disorders. More recently, it has been suggested to be an important regulatory component of vesicle transport in neuronal cells. α-Synuclein is also highly expressed in platelets and is loosely associated with the membrane of the secretory α-granules. However, the functional significance of these observations is unknown. In this study, the possible function of α-synuclein in vesicle transport, with particular regard to α-granule release from the platelets, was investigated. The results showed that ionomycin- or thrombin-induced α-granule secretion was inhibited by exogenous α-synuclein addition in a dose-dependent manner. However, [3H]5-HT release from the dense granules and hexosaminidase release from the lysosomal granules were not affected. Two point mutants (A30P and A53T) found in some familial types of PD, in addition to β-synuclein and α-synuclein112, effectively inhibited PF4 release from the α-granules. However, the deletion mutants, which completely lacked either the N-terminal region or the C-terminal tail, did not affect α-granule release. Interestingly, exogenously added α-synuclein appeared to enter the platelets but did not change the Ca++ level in the platelets at the resting state and the increase in the Ca++level on stimulation. Electron microscopy also supported that α-synuclein inhibits α-granule release. These results suggest that α-synuclein may function as a specific negative regulator of α-granule release in platelets.

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Scheibe, Christian, Christiaan Karreman, Stefan Schildknecht, Marcel Leist, and Karin Hauser. "Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation." Biomolecules 11, no. 8 (July 21, 2021): 1067. http://dx.doi.org/10.3390/biom11081067.

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The 140 amino acid protein α-synuclein (αS) is an intrinsically disordered protein (IDP) with various roles and locations in healthy neurons that plays a key role in Parkinson’s disease (PD). Contact with biomembranes can lead to α-helical conformations, but can also act as s seeding event for aggregation and a predominant β-sheet conformation. In PD patients, αS is found to aggregate in various fibrillary structures, and the shift in aggregation and localization is associated with disease progression. Besides full-length αS, several related polypeptides are present in neurons. The role of many αS-related proteins in the aggregation of αS itself is not fully understood Two of these potential aggregation modifiers are the αS splicing variant αS Δexon3 (Δ3) and the paralog β-synuclein (βS). Here, polarized ATR-FTIR spectroscopy was used to study the membrane interaction of these proteins individually and in various combinations. The method allowed a continuous monitoring of both the lipid structure of biomimetic membranes and the aggregation state of αS and related proteins. The use of polarized light also revealed the orientation of secondary structure elements. While αS led to a destruction of the lipid membrane upon membrane-catalyzed aggregation, βS and Δ3 aggregated significantly less, and they did not harm the membrane. Moreover, the latter proteins reduced the membrane damage triggered by αS. There were no major differences in the membrane interaction for the different synuclein variants. In combination, these observations suggest that the formation of particular protein aggregates is the major driving force for αS-driven membrane damage. The misbalance of αS, βS, and Δ3 might therefore play a crucial role in neurodegenerative disease.

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Flores-Fernández, José, Vineet Rathod, and Holger Wille. "Comparing the Folds of Prions and Other Pathogenic Amyloids." Pathogens 7, no. 2 (May 4, 2018): 50. http://dx.doi.org/10.3390/pathogens7020050.

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Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt–Jakob disease, Alzheimer’s disease, and Parkinson’s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-β(1-42) (Aβ(1-42)) fibrils, and α-synuclein fibrils were recently reported using cryo-electron microscopy. A high-resolution structure for the infectious prion protein, PrPSc, is not yet available due to its insolubility and its propensity to aggregate, but cryo-electron microscopy, X-ray fiber diffraction, and other approaches have defined the overall architecture of PrPSc as a 4-rung β-solenoid. Thus, the structure of PrPSc must have a high similarity to that of the fungal prion HET-s, which is part of the fungal heterokaryon incompatibility system and contains a 2-rung β-solenoid. This review compares the structures of tau PHFs, Aβ(1-42), and α-synuclein fibrils, where the β-strands of each molecule stack on top of each other in a parallel in-register arrangement, with the β-solenoid folds of HET-s and PrPSc.

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Sivanesam, K., A. Byrne, M. Bisaglia, L. Bubacco, and N. Andersen. "Binding interactions of agents that alter α-synuclein aggregation." RSC Advances 5, no. 15 (2015): 11577–90. http://dx.doi.org/10.1039/c5ra00325c.

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NMR studies of the amyloidogenesis of α-synuclein, including studies of the binding sites of potent peptide inhibitors of the process, have produced a more detailed model of the earliest stages of β-oligomer formation.

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