Relevant bibliographies by topics / Β-synuclein

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Β-synuclein'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Β-synuclein"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Β-synuclein"

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Rivers, Robert Clay. "Biophysical analysis of the aggregation behaviour and structural properties of α- and β-synuclein." Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.612821.

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Psol, Maryna [Verfasser], Sebastian [Akademischer Betreuer] Kügler, Tiago Fleming [Gutachter] Outeiro, and Markus [Gutachter] Zweckstetter. "Neurotoxicity and aggregation of β-synuclein and its P123H and V70M mutants associated with dementia with Lewy bodies / Maryna Psol ; Gutachter: Tiago Fleming Outeiro, Markus Zweckstetter ; Betreuer: Sebastian Kügler." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2019. http://d-nb.info/1188886878/34.

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Toloe, Johan Verfasser], Sebastian [Akademischer Betreuer] Kügler, Sergej [Akademischer Betreuer] Mironov, and Tobias [Akademischer Betreuer] [Moser. "Effects of α/β/γ-Synuclein overexpression on the mitochondria and viability of neurons, examined using genetically encoded fluorescent sensors / Johan Tolö. Gutachter: Sergej Mironov ; Tobias Moser. Betreuer: Sebastian Kügler." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2014. http://d-nb.info/1058764403/34.

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Cheng, Yu-Shih, and 鄭毓仕. "Investigation of the Molecular Mechanisms on Amyloid β Mediating α-Synuclein-induced Neurotoxicity." Thesis, 2014. http://ndltd.ncl.edu.tw/handle/nmpt2j.

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碩士
中山醫學大學
醫學研究所
102
In all dementia patient, the percentage of Dementia with Lewy bodies (DLB) patients is very high, and just less than Alzheimer’s disease (AD) patients. In these two common dementia, α-Synuclein and Aβ are two major pathological features in the brain of patients, respectively. The mechanism of these features is that these abnormal folding protein accumulated in the neuron cells. Additionally, there are one type of DLB patients have been found not only α-Synuclein but also Aβ abnormal accumulated in the brain, and the progress of these DLB patients are more fast than AD patients. Accordingly, the aim of this study is to investigate whether Aβ affects the accumulation of α-Synuclein, and induced more neuron toxicity in pathological development process of DLB. We overexpressed α-Synuclein in SK-N-MC cell line by transfection, and treated with Aβ to mimic the brain environment of DLB patients. We studied some molecular mechanism which may cause DLB by this model. Besides, we had a cooperation with clinical doctors to collect the peripheral blood of patients, and purified the mRNA form leukocytes in blood, and compared it with AD patients and normal person. In this study, we first investigated that α-Synuclein increased Aβ induced cell apoptosis. Then we found this phenomenon may through inhibiting cell self-clearance system including autophagy and ubiquitin proteasome system (UPS), and increasing aging resulted in inhibition of Sirt1, Foxo3a and SOD1, the enzyme which can clean up ROS by western blot and fluorescence stain. Next the ROS increased may result in mitochondria dysfunction. Last, we observed the Sirt1, SOD1 and BDNF mRNA level of leukocyte from DLB patients are less than AD and human normal control. In conclusion, We suggested that Aβ may play an important role in the progression of DLB. The molecular mechanism of DLB was inhibiting cell self-clearance, and induced the phenomenon of aging, and finally led to more apoptosis. In the future, maybe we can use some drugs which can induce cell autophagy, or decrease the formation of Aβ to slow down the progression and the symptom of DLB, and to help the treatment of DLB effectively.
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Chang, Yen-Ting, and 張雁婷. "Investigating amyloid β mediated α-Synuclein-induced neurotoxicity in Dementia with Lewy Bodies." Thesis, 2016. http://ndltd.ncl.edu.tw/handle/p28y39.

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碩士
中山醫學大學
醫學研究所
104
Dementia with Lewy bodies (DLB) is the second most common cause of dementia, trailing Alzheimer’s disease (AD), which possessing a large proportion of demented population. In these two diseases, α-Synucleinand beta-Amyloid (Aβ) are the main pathologies in DLB and ADpatients brain respectively, and both proteins involved the mechanism of misfolded proteins in neurodegeneration. In the past, patients with DLB revealed similar pathology with AD in their brains; thus, the name LB variant of AD was used in previous documents. Comparing to AD patients,DLB patientsdevelop a much sooner process in disease progression; however, the mechanism of deposition and neurotoxicity of α-Synuclein by Aβis not yet clarified. In order to understand the effects of Aβ on α-Synucleinaccumulation, clearance, and production of neurotoxicity, we investigated the mechanisms of DLB pathology through established a conditionaloverexpressing α-Synuclein cell line. Furthermore, we treated the cells with Aβto mimic the pathological condition within DLB brains. In addition, tofurther understanding neurotoxicity of Aβin α-Synuclein accumulation and clearance, twelve weeks old male Wistar rats werei.c.v. injected by α-Synucleinvector (10 μg/10μL/rat) into brain ventricle, and/orAβ（10 μg/5 μL/side）into double sides of cortex by stereotactic surgery. After the brain lesion, animal behavioral tests were performed including short-term memory, learning, and object recognition test. Finally, rats were scarified in order to observe the level of α-Synuclein through Immunohistochemistry; moreover, blood and brain tissue were also collected and analyzed to understand neurotoxicity and autophagy through western blotting. Our data showed that overexpression of α-Synuclein increasesneurotoxicityby Aβ co-treatment. According to western blotting and fluorescent staining, the results displayed an increasing in apoptosisbut inhibition in autophagy. Furthermore, proteins which related to aging and ROS were also decreased. In addition,mitochondrial dysfunction was shown by fluorescent staining. More interestingly, DLB animal showed deficits both in memory and learning ability comparing to normal control through behavioral tests. In summary, our results suggest that Aβ maycontribute to the DLB pathogenesis by affecting the accumulation of α-Synuclein or interfering autophagic clearancemechanism.
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Psol, Maryna. "Neurotoxicity and aggregation of β-synuclein and its P123H and V70M mutants associated with dementia with Lewy bodies." Doctoral thesis, 2018. http://hdl.handle.net/21.11130/00-1735-0000-0003-C133-9.

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Toloe, Johan. "Effects of α/β/γ-Synuclein overexpression on the mitochondria and viability of neurons, examined using genetically encoded fluorescent sensors." Doctoral thesis, 2014. http://hdl.handle.net/11858/00-1735-0000-0023-98DB-7.

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Books on the topic "Β-synuclein"

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Attems, Johannes, and Kurt A. Jellinger. Neuropathology. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199644957.003.0006.

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This chapter describes the main neuropathological features of the most common age associated neurodegenerative diseases including Alzheimer's disease, Parkinson's disease and dementia with Lewy bodies as well as other less frequent ones such as multiple system atrophy, Pick's disease, corticobasal degeneration, progressive supranuclear palsy, argyrophilic grain disease, neurofibrillary tangle dominant dementia, frontotemporal lobar degeneration with TDP-43 pathology and Huntington's disease. Likewise cerebral amyloid angiopathy, hippocampal sclerosis, vascular dementia and prion diseases are described. A main aim of this chapter is to assist the reader in interpreting neuropathological reports, hence criteria for the neuropathological classifications of the major diseases are provided. One section covers general considerations on neurodegeneration and basic pathophysiological mechanisms of tau, amyloid-β, α-synuclein, TDP-43 and prions are briefly described in the sections on the respective diseases. Finally, one section is dedicated to cerebral multimorbidity and we give a view on currently emerging neuropathological methods.
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Book chapters on the topic "Β-synuclein"

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Walker, Lauren, and Johannes Attems. "Relationship Between Tau, β Amyloid and α-Synuclein Pathologies." In Advances in Experimental Medicine and Biology, 169–76. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-32-9358-8_14.

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"Synuclein β." In Encyclopedia of Cancer, 3597. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_5633.

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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." In Research Anthology on Diagnosing and Treating Neurocognitive Disorders, 366–85. IGI Global, 2021. http://dx.doi.org/10.4018/978-1-7998-3441-0.ch019.

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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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Calderón-Garcidueñas, Lilian, José Avila-Ramírez, Ana Calderón-Garcidueñas, Tonatiuh González-Heredia, Hilda Acuña-Ayala, Chih-kai Chao, Charles Thompson, et al. "Cerebrospinal Fluid Biomarkers in Highly Exposed PM2.5 Urbanites: The Risk of Alzheimer’s and Parkinson’s Diseases in Young Mexico City Residents." In Advances in Alzheimer’s Disease. IOS Press, 2021. http://dx.doi.org/10.3233/aiad210039.

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Exposure to fine particulate matter (PM2.5) and ozone (O3) above US EPA standards is associated with Alzheimer’s disease (AD) risk, while Mn toxicity induces parkinsonism. Mexico City Metropolitan Area (MCMA) children have pre- and postnatal sustained and high exposures to PM2.5, O3, polycyclic aromatic hydrocarbons, and metals. Young MCMA residents exhibit frontal tau hyperphosphorylation and amyloid-β (Aβ)1–42 diffuse plaques, and aggregated and hyperphosphorylated α-synuclein in olfactory nerves and key brainstem nuclei. We measured total prion protein (TPrP), total tau (T-tau), tau phosphorylated at threonine 181 (P-Tau), Aβ1–42, α-synuclein (t-α-syn and d-α-synuclein), BDNF, insulin, leptin, and/or inflammatory mediators, in 129 normal CSF samples from MCMA and clean air controls. Aβ1–42 and BDNF concentrations were significantly lower in MCMA children versus controls (p = 0.005 and 0.02, respectively). TPrP increased with cumulative PM2.5 up to 5 μg/m3 and then decreased, regardless of cumulative value or age (R2 = 0.56). TPrP strongly correlated with T-Tau and P-Tau, while d-α-synuclein showed a significant correlation with TNFα, IL10, and IL6 in MCMA children. Total synuclein showed an increment in childhood years related to cumulated PM2.5, followed by a decrease after age 12 years R2 = 0.47), while d-α-synuclein exhibited a tendency to increase with cumulated PM2.5 (R2 = 0.30). CSF Aβ1–42, BDNF, α-synuclein, and TPrP changes are evolving in young MCMA urbanites historically showing underperformance in cognitive processes, odor identification deficits, downregulation of frontal cellular PrP, and neuropathological AD and PD hallmarks. Neuroprotection of young MCMA residents ought to be a public health priority.
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Amin, Mohamed M. "Neurodegenerative Disorders." In Advances in Medical Diagnosis, Treatment, and Care, 195–216. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-5282-6.ch009.

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Neurodegenerative diseases (NDs) are characterized by specific dysfunction and damage of neurons related to pathologically changed proteins that deposit in the patient brain but also in peripheral organs. These proteins can be used for therapy or used as biomarkers. Except for a plethora of alterations revealed for dissimilar neurodegeneration-related proteins, amyloid-β, prion protein, TAR DNA-binding protein 43 (TDP-43, transactive response DNA binding protein 43 kDa), tau and α-synuclein, or fused in sarcoma protein (FUS), molecular classification of NDs depend on the full morphological assessment of protein deposits, their spreading in the brain, and their correspondence to clinical signs with specific genetic modifications. The current chapter represents the etiology of neurodegeneration, classification of NDs, concentrating on the maximum applicable biochemical and anatomical characteristics and most imperative NDs.
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Calderón-Garcidueñas, Lilian, Randy J. Kulesza, Yusra Mansour, Mario Aiello-Mora, Partha S. Mukherjee, and Luis Oscar González-González. "Increased Gain in the Auditory Pathway, Alzheimer’s Disease Continuum, and Air Pollution: Peripheral and Central Auditory System Dysfunction Evolves Across Pediatric and Adult Urbanites." In Advances in Alzheimer’s Disease. IOS Press, 2021. http://dx.doi.org/10.3233/aiad210038.

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A major impediment in early diagnosis of Alzheimer’s disease (AD) is the lack of robust non-invasive biomarkers of early brain dysfunction. Metropolitan Mexico City (MMC) children and young adults show hyperphosphorylated tau, amyloid-β, and α-synuclein within auditory and vestibular nuclei and marked dysmorphology in the ventral cochlear nucleus and superior olivary complex. Based on early involvement of auditory brainstem centers, we believe brainstem auditory evoked potentials can provide early AD biomarkers in MMC young residents. We measured brainstem auditory evoked potentials in MMC clinically healthy children (8.52 ± 3.3 years) and adults (21.08 ± 3.0 years, 42.48 ± 8.5 years, and 71.2 ± 6.4 years) compared to clean air controls (6.5 ± 0.7 years) and used multivariate analysis adjusting for age, gender, and residency. MMC children had decreased latency to wave I, delays in waves III and V, and longer latencies for interwave intervals, consistent with delayed central conduction time of brainstem neural transmission. In sharp contrast, young adults have significantly shortened interwave intervals I–III and I–V. By the 5th decade, wave V and interval I–V were significantly shorter, while the elderly cohort had significant delay in mean latencies and interwave intervals. Compensatory plasticity, increased auditory gain, cochlear synaptopathy, neuroinflammation, and AD continuum likely play a role in the evolving distinct auditory pathology in megacity urbanites. Understanding auditory central and peripheral dysfunction in the AD continuum evolving and progressing in pediatric and young adult populations may shed light on the complex mechanisms of AD development and help identify strong noninvasive biomarkers. AD evolving from childhood in air pollution environments ought to be preventable.
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Conference papers on the topic "Β-synuclein"

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Valensin, Daniela, Henryk Kozlowski, Isabella Tessari, Simone Dell'Acqua, Luigi Bubacco, Luigi Casella, Elena Gaggelli, and Gianni Valensin. "Interactions of metal ions with α synuclein and amyloid β peptides." In INTERNATIONAL CONFERENCE OF COMPUTATIONAL METHODS IN SCIENCES AND ENGINEERING 2014 (ICCMSE 2014). AIP Publishing LLC, 2014. http://dx.doi.org/10.1063/1.4897691.

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