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Journal articles on the topic 'TEP amyloïde'

Author: Grafiati
Published: 14 February 2023

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1

Payoux, P., T. Voisin, M. Alonso, S. Peiffer, M. Tafani, J. Delrieu, A. Hitzel, S. Gillette, and B. Vellas. "Métabolisme cérébral et charge amyloïde chez les sujets fragiles : une étude en TEP." Médecine Nucléaire 36, no. 4 (April 2012): 161–62. http://dx.doi.org/10.1016/j.mednuc.2012.02.019.

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2

Santiago-Ribeiro, M. J., E. Beaufils, J. Vercouillie, D. Dufour, V. Camus, K. Mondon, D. Guilloteau, and C. Hommet. "Distribution cérébrale de la charge amyloïde par TEP au 18F-Florbétapir dans l’atrophie corticale postérieure." Médecine Nucléaire 39, no. 3 (May 2015): 210. http://dx.doi.org/10.1016/j.mednuc.2015.03.017.

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3

Bund, C., V. Noblet, F. Heitz, F. Blanc, and I. J. Namer. "Interprétation de l’imagerie de la plaque bêta-amyloïde en imagerie TEP/TDM : comment normaliser les intensités ?" Médecine Nucléaire 39, no. 3 (May 2015): 224–25. http://dx.doi.org/10.1016/j.mednuc.2015.03.069.

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4

Meyer, M., P. Zanotti Fregonara, F. Lamare, G. Catheline, C. Helmer, K. Peres, M. Allard, J. F. Dartigues, and P. Fernandez. "Charge amyloïde évaluée par TEP au 18F-flutemetamol et performances cognitives chez le sujet âgé non dément." Médecine Nucléaire 40, no. 3 (May 2016): 177. http://dx.doi.org/10.1016/j.mednuc.2016.03.022.

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5

Adel, D., J. Delrieu, A. S. Brun, A. Hitzel, D. De Verbizier, F. Lamarre, M. Razzouk, S. Gillette, B. Vellas, and P. Payoux. "Impact du choix des régions d’intérêt sur la quantification du SUVr en TEP des traceurs de la plaque amyloïde." Médecine Nucléaire 37, no. 5 (May 2013): 141. http://dx.doi.org/10.1016/j.mednuc.2013.03.024.

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6

Bottlaender, M., J. Lagarde, P. Olivieri, M. Tonietto, P. Gervais, C. Comtat, F. Caillé, and M. Sarazin. "Apport de l’imagerie TEP des dépôts tau et amyloïde dans le diagnostic étiologique chez des patients présentant un syndrome amnésique." Médecine Nucléaire 46, no. 2 (March 2022): 53. http://dx.doi.org/10.1016/j.mednuc.2022.01.012.

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7

Deberdt, W., G. Dell’agnello, A. Chevrette, M. Lu, and M. Pontecorvo. "Étude internationale multicentrique randomisée contrôlée de l’impact de l’imagerie TEP amyloïde au florbetapir (18F) sur la prise en charge des patients." Médecine Nucléaire 40, no. 3 (May 2016): 177–78. http://dx.doi.org/10.1016/j.mednuc.2016.03.023.

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8

Manca, C., V. Roch, C. Armand, T. Jonveaux, G. Karcher, P. Y. Marie, and A. Verger. "Analyse semi-quantitative de la TEP aux marqueurs de la plaque amyloïde après normalisation spatiale et correction d’atténuation vs analyse visuelle." Médecine Nucléaire 43, no. 2 (March 2019): 220. http://dx.doi.org/10.1016/j.mednuc.2019.01.132.

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9

Balamoutoff, N., and M. J. Santiago Ribeiro. "Imagerie moléculaire de la plaque amyloïde en TEP/TDM par 18F-Florbetapir et intégration des données de suivi neuropsychologique sur 2 ans." Médecine Nucléaire 41, no. 3 (May 2017): 166. http://dx.doi.org/10.1016/j.mednuc.2017.02.073.

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10

Simon, Maryline, Leslie M. Shaw, Kaj Blennow, Katharina Buck, Christina Rabe, Udo Eichenlaub, and Oskar Hansson. "Concordance du test immunologique Elecsys® B-amyloïde (1–42)’Abeta42 du liquide céphalorachidien (LCR), du Tau total (T-TAU) et du phospho-Tau (181P) LCR (PTAU) avec le TEP-amyloïde et leur association avec la progression clinique de la maladie d’Alzheimer." Revue Neurologique 175 (April 2019): S43—S44. http://dx.doi.org/10.1016/j.neurol.2019.01.053.

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11

Hanseeuw, B., and R. Lhommel. "Utilisation de la TEP-amyloïde pour prédire l’évolution à long terme des patients non déments consultant à la Clinique de la Mémoire : intérêt de la quantification Centiloïde, une échelle internationale standardisée." Médecine Nucléaire 44, no. 2 (March 2020): 138–39. http://dx.doi.org/10.1016/j.mednuc.2020.01.131.

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12

Partouche, David, Florian Turbant, Omar El Hamoui, Camille Campidelli, Marianne Bombled, Sylvain Trépout, Frank Wien, and Véronique Arluison. "Epigallocatechin Gallate Remodelling of Hfq Amyloid-Like Region Affects Escherichia coli Survival." Pathogens 7, no. 4 (December 1, 2018): 95. http://dx.doi.org/10.3390/pathogens7040095.

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Hfq is a pleiotropic regulator that has key roles in the control of genetic expression. The protein noticeably regulates translation efficiency and RNA decay in Gram-negative bacteria, due to the Hfq-mediated interaction between small regulatory noncoding RNA and mRNA. This property is of primary importance for bacterial adaptation and virulence. We have previously shown that the Hfq E. coli protein, and more precisely its C-terminal region (CTR), self-assembles into an amyloid-like structure. In the present work, we demonstrate that epigallocatechin gallate (EGCG), a major green tea polyphenol compound, targets the Hfq amyloid region and can be used as a potential antibacterial agent. We analysed the effect of this compound on Hfq amyloid fibril stability and show that EGCG both disrupts Hfq-CTR fibrils and inhibits their formation. We show that, even if EGCG affects other bacterial amyloids, it also specifically targets Hfq-CTR in vivo. Our results provide an alternative approach for the utilisation of EGCG that may be used synergistically with conventional antibiotics to block bacterial adaptation and treat infections.
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13

Wan, Juan, Meiyan Feng, Wenjing Pan, Xin Zheng, Xinya Xie, Baozhu Hu, Cuiqin Teng, et al. "Inhibitory Effects of Six Types of Tea on Aging and High-Fat Diet-Related Amyloid Formation Activities." Antioxidants 10, no. 10 (September 24, 2021): 1513. http://dx.doi.org/10.3390/antiox10101513.

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Aging and lipid metabolism disorders promote the formation and accumulation of amyloid with β-sheet structure, closely related to cardiovascular disease, senile dementia, type 2 diabetes, and other senile degenerative diseases. In this study, five representative teas were selected from each of the six types of tea, and a total of 30 teas were selected to evaluate the inhibitory activities on the formation of aging-related amyloid in vitro. The results showed that the 30 teas had a significant inhibitory effect on the formation activity on aging-related amyloid at the protein level in vitro. Although the content of catechins is relatively low, black tea and dark tea still have significant antioxidant activity and inhibit the formation of amyloid. A high-fat diet established the model of lipid metabolism disorder in premature aging SAMP8 mice, and these mice were gavaged different tea water extracts. The results showed that different tea types have a significant inhibitory effect on the formation of β-amyloid and Aβ42 mediated by age-related lipid metabolism disorders, and the in vivo activity of fully fermented teas was better than that of green tea. The action mechanism was related to antioxidation, anti-inflammatory, and improving lipid metabolism.
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14

Laudanski, Krzysztof, Da Liu, Tony Okeke, Mariana Restrepo, and Wilson Y. Szeto. "Persistent Depletion of Neuroprotective Factors Accompanies Neuroinflammatory, Neurodegenerative, and Vascular Remodeling Spectra in Serum Three Months after Non-Emergent Cardiac Surgery." Biomedicines 10, no. 10 (September 22, 2022): 2364. http://dx.doi.org/10.3390/biomedicines10102364.

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We hypothesized that the persistent depletion of neuroprotective markers accompanies neuroinflammation and neurodegeneration in patients after cardiac surgery. A total of 158 patients underwent elective heart surgery with their blood collected before surgery (tbaseline) and 24 h (t24hr), seven days (t7d), and three months (t3m) post-surgery. The patients’ serum was measured for markers of neurodegeneration (τau, τaup181–183, amyloid β1-40/β2-42, and S100), atypical neurodegeneration (KLK6 and NRGN), neuro-injury (neurofilament light/heavy, UC-HL, and GFAP), neuroinflammation (YKL-40 and TDP-43), peripheral nerve damage (NCAM-1), neuroprotection (apoE4, BDNF, fetuin, and clusterin), and vascular smoldering inflammation (C-reactive protein, CCL-28 IL-6, and IL-8). The mortality at 28 days, incidence of cerebrovascular accidents (CVA), and functional status were followed for three months. The levels of amyloid β1-40/β1-42 and NF-L were significantly elevated at all time points. The levels of τau, S100, KLK6, NRGN, and NCAM-1 were significantly elevated at 24 h. A cluster analysis demonstrated groupings around amyloids, KLK6, and NCAM-1. YKL-40, but not TDP-43, was significantly elevated across all time points. BDNF, apoE4, fetuin, and clusterin levels were significantly diminished long-term. IL-6 and IL-8 levles returned to baseline at t3m. The levels of CRP, CCL-28, and Hsp-70 remained elevated. At 3 months, 8.2% of the patients experienced a stroke, with transfusion volume being a significant variable. Cardiac-surgery patients exhibited persistent peripheral and neuronal inflammation, blood vessel remodeling, and the depletion of neuroprotective factors 3 months post-procedure.
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15

Hengge, Regine. "Targeting Bacterial Biofilms by the Green Tea Polyphenol EGCG." Molecules 24, no. 13 (June 29, 2019): 2403. http://dx.doi.org/10.3390/molecules24132403.

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Bacterial biofilms are multicellular aggregates in which cells are embedded in an extracellular matrix of self-produced biopolymers. Being refractory to antibiotic treatment and host immune systems, biofilms are involved in most chronic infections, and anti-biofilm agents are being searched for urgently. Epigallocatechin-3-gallate (EGCG) was recently shown to act against biofilms by strongly interfering with the assembly of amyloid fibres and the production of phosphoethanolamin-modified cellulose fibrils. Mechanistically, this includes a direct inhibition of the fibre assembly, but also triggers a cell envelope stress response that down-regulates the synthesis of these widely occurring biofilm matrix polymers. Based on its anti-amyloidogenic properties, EGCG seems useful against biofilms involved in cariogenesis or chronic wound infection. However, EGCG seems inefficient against or may even sometimes promote biofilms which rely on other types of matrix polymers, suggesting that searching for ‘magic bullet’ anti-biofilm agents is an unrealistic goal. Combining molecular and ecophysiological aspects in this review also illustrates why plants control the formation of biofilms on their surfaces by producing anti-amyloidogenic compounds such as EGCG. These agents are not only helpful in combating certain biofilms in chronic infections but even seem effective against the toxic amyloids associated with neuropathological diseases.
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16

Delrieu, J., and B. Vellas. "L’imagerie TEP-traceurs des plaques amyloïdes : le point de vue du clinicien." Médecine Nucléaire 35, no. 11 (November 2011): 608–12. http://dx.doi.org/10.1016/j.mednuc.2011.08.004.

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17

Pantoja-Uceda, David, Cristiana Stuani, Douglas V. Laurents, Ann E. McDermott, Emanuele Buratti, and Miguel Mompeán. "Phe-Gly motifs drive fibrillization of TDP-43’s prion-like domain condensates." PLOS Biology 19, no. 4 (April 28, 2021): e3001198. http://dx.doi.org/10.1371/journal.pbio.3001198.

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Transactive response DNA-binding Protein of 43 kDa (TDP-43) assembles various aggregate forms, including biomolecular condensates or functional and pathological amyloids, with roles in disparate scenarios (e.g., muscle regeneration versus neurodegeneration). The link between condensates and fibrils remains unclear, just as the factors controlling conformational transitions within these aggregate species: Salt- or RNA-induced droplets may evolve into fibrils or remain in the droplet form, suggesting distinct end point species of different aggregation pathways. Using microscopy and NMR methods, we unexpectedly observed in vitro droplet formation in the absence of salts or RNAs and provided visual evidence for fibrillization at the droplet surface/solvent interface but not the droplet interior. Our NMR analyses unambiguously uncovered a distinct amyloid conformation in which Phe-Gly motifs are key elements of the reconstituted fibril form, suggesting a pivotal role for these residues in creating the fibril core. This contrasts the minor participation of Phe-Gly motifs in initiation of the droplet form. Our results point to an intrinsic (i.e., non-induced) aggregation pathway that may exist over a broad range of conditions and illustrate structural features that distinguishes between aggregate forms.
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18

He, Ruei-Yu, Yi-Chen Huang, Chao-Wei Chiang, Yu-Ju Tsai, Ting-Juan Ye, Hua-De Gao, Chu-Ya Wu, Hsien-Ming Lee, and Joseph Jen-Tse Huang. "Characterization and real-time imaging of the FTLD-related protein aggregation induced by amyloidogenic peptides." Chemical Communications 51, no. 41 (2015): 8652–55. http://dx.doi.org/10.1039/c5cc00513b.

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19

Scialò, Carlo, Luigi Celauro, Marco Zattoni, Thanh Hoa Tran, Edoardo Bistaffa, Fabio Moda, Robert Kammerer, Emanuele Buratti, and Giuseppe Legname. "The Cellular Prion Protein Increases the Uptake and Toxicity of TDP-43 Fibrils." Viruses 13, no. 8 (August 17, 2021): 1625. http://dx.doi.org/10.3390/v13081625.

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Cytoplasmic aggregation of the primarily nuclear TAR DNA-binding protein 43 (TDP-43) affects neurons in most amyotrophic lateral sclerosis (ALS) and approximately half of frontotemporal lobar degeneration (FTLD) cases. The cellular prion protein, PrPC, has been recognized as a common receptor and downstream effector of circulating neurotoxic species of several proteins involved in neurodegeneration. Here, capitalizing on our recently adapted TDP-43 real time quaking induced reaction, we set reproducible protocols to obtain standardized preparations of recombinant TDP-43 fibrils. We then exploited two different cellular systems (human SH-SY5Y and mouse N2a neuroblastoma cells) engineered to express low or high PrPC levels to investigate the link between PrPC expression on the cell surface and the internalization of TDP-43 fibrils. Fibril uptake was increased in cells overexpressing either human or mouse prion protein. Increased internalization was associated with detrimental consequences in all PrP-overexpressing cell lines but was milder in cells expressing the human form of the prion protein. As described for other amyloids, treatment with TDP-43 fibrils induced a reduction in the accumulation of the misfolded form of PrPC, PrPSc, in cells chronically infected with prions. Our results expand the list of misfolded proteins whose uptake and detrimental effects are mediated by PrPC, which encompass almost all pathological amyloids involved in neurodegeneration.
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20

Khan, Adittya Sabhayasachi, Rezowana Mannan, Laila Anjuman Banu, Sohidul Islam, and Mahmud Hossain. "Green Tea Augments Cognitive Function: An In Silico Model." Bioresearch Communications 8, no. 2 (July 4, 2022): 1113–23. http://dx.doi.org/10.3329/brc.v8i2.60642.

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Recent scientific advancements have sparked an increasing trend of returning to nature. Scientists worldwide prefer natural medical derivatives over synthetic ones due to fewer side effects. Green tea is abundant in bioactive components and vitamins. Although most components of green tea were thought to be absorbed inadequately by oral administration, they are essential for better health. In the present study, an in silico approach was taken to evaluate the effect or correlation of bioactive components of tea on memory retention, cognitive performance, and prevention of neurodegenerative diseases that result in memory alterations, dementia, and cognitive dysfunction. Furthermore, binding of bioactive components with brain-specific proteins and possible alterations in those proteins due to tea components were illustrated. Four critical brain-specific proteins were evaluated in the present molecular analysis. Cyclooxygenase 1 (COX1), Acetylcholinesterase (AChE), Amyloid-β Precursor Protein (APP1), and Cytochrome P4502D6 (Cyp2D6) were the proteins involved. Their interaction with the bioactive components of green tea was evaluated using computational molecular docking analysis (CMDA). The bioactive molecules were Epigallocatechin gallate (EGCG), L-Theanine, Kaemferol, Coumarin, and Myricetin. The beneficial effect of green tea on memory was prioritized in this study. CMDA has shown possible inhibition of acetylcholinesterase, amyloid-β protein, cyclooxygenase 1, and Cytochrome P4502D6 (Cyp2D6). Bioactive components of green tea passed the blood-brain barrier and influenced short-term memory at low concentrations. Significant dosage or concentration in capsulated form might result in long-term effects since both bioavailability, and concentration of essential components of green tea are scarce. Bioresearch Commu. 8(2): 1113-1123, 2022 (July)
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21

Martinez Pomier, Karla, Rashik Ahmed, and Giuseppe Melacini. "Catechins as Tools to Understand the Molecular Basis of Neurodegeneration." Molecules 25, no. 16 (August 6, 2020): 3571. http://dx.doi.org/10.3390/molecules25163571.

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Protein misfolding as well as the subsequent self-association and deposition of amyloid aggregates is implicated in the progression of several neurodegenerative disorders including Alzheimer’s and Parkinson’s diseases. Modulators of amyloidogenic aggregation serve as essential tools to dissect the underlying molecular mechanisms and may offer insight on potential therapeutic solutions. These modulators include green tea catechins, which are potent inhibitors of amyloid aggregation. Although catechins often exhibit poor pharmacokinetic properties and bioavailability, they are still essential tools for identifying the drivers of amyloid aggregation and for developing other aggregation modulators through structural mimicry. As an illustration of such strategies, here we review how catechins have been used to map the toxic surfaces of oligomeric amyloid-like species and develop catechin-based phenolic compounds with enhanced anti-amyloid activity.
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22

Zeng, Yu-Teng, Lu-Lu Bi, Xiao-Feng Zhuo, Ling-Yun Yang, Bo Sun, and Jun-Xia Lu. "Different Intermolecular Interactions Drive Nonpathogenic Liquid–Liquid Phase Separation and Potentially Pathogenic Fibril Formation by TDP-43." International Journal of Molecular Sciences 23, no. 23 (December 3, 2022): 15227. http://dx.doi.org/10.3390/ijms232315227.

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The liquid–liquid phase separation (LLPS) of proteins has been found ubiquitously in eukaryotic cells, and is critical in the control of many biological processes by forming a temporary condensed phase with different bimolecular components. TDP-43 is recruited to stress granules in cells and is the main component of TDP-43 granules and proteinaceous amyloid inclusions in patients with amyotrophic lateral sclerosis (ALS). TDP-43 low complexity domain (LCD) is able to de-mix in solution, forming the protein condensed droplets, and amyloid aggregates would form from the droplets after incubation. The molecular interactions regulating TDP-43 LCD LLPS were investigated at the protein fusion equilibrium stage, when the droplets stopped growing after incubation. We found the molecules in the droplet were still liquid-like, but with enhanced intermolecular helix–helix interactions. The protein would only start to aggregate after a lag time and aggregate slower than at the condition when the protein does not phase separately into the droplets, or the molecules have a reduced intermolecular helix–helix interaction. In the protein condensed droplets, a structural transition intermediate toward protein aggregation was discovered involving a decrease in the intermolecular helix–helix interaction and a reduction in the helicity. Our results therefore indicate that different intermolecular interactions drive LLPS and fibril formation. The discovery that TDP-43 LCD aggregation was faster through the pathway without the first protein phase separation supports that LLPS and the intermolecular helical interaction could help maintain the stability of TDP-43 LCD.
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23

Jayachandran, Muthuvel, Virginia M. Miller, Brian D. Lahr, Kent R. Bailey, Val J. Lowe, Julie A. Fields, Michelle M. Mielke, and Kejal Kantarci. "Peripheral Markers of Neurovascular Unit Integrity and Amyloid-β in the Brains of Menopausal Women." Journal of Alzheimer's Disease 80, no. 1 (March 9, 2021): 397–405. http://dx.doi.org/10.3233/jad-201410.

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Background: The identification of blood-borne biomarkers for the diagnosis and prognosis of Alzheimer’s disease and related dementias is more feasible at the population level than obtaining cerebrospinal fluid or neuroimaging markers. Objective: This study determined the association of blood microvesicles, derived from cells of the neurovascular unit, with brain amyloid-β deposition in menopausal women. Methods: A subset of women from the Kronos Early Estrogen Prevention Study underwent brain amyloid-β positron emission tomography three years following cessation of study treatment with placebo (PL, n = 29), transdermal 17β-estradiol (tE2; n = 21), or oral conjugated equine estrogen (oCEE; n = 17). Isolated peripheral venous blood microvesicles were analyzed by digital flow cytometry using fluorophore conjugated antibodies directed toward total tau, amyloid-β 1–42 (Aβ1–42), neuron specific class III β-tubulin (Tuj1), microglia ionized calcium -binding adaptor molecule 1(Iba1), glial fibrillary acid protein (GFAP), and low density lipoprotein receptor-related protein1 (LRP1). Principal components analysis reduced the dimensionality of these selected six markers to two principal components (PCs). Proportional odds ordinal logistic regression analysis was used with amyloid-β deposition regressed on these PCs. Results: Only the number of microvesicles positive for Aβ1–42 differed statistically among prior treatment groups (median [IQR]: 6.06 [2.11, 12.55] in PL; 2.49 [0.73, 3.59] in tE2; and 4.96 [0.83, 10.31] in oCEE; p = 0.032). The joint association between the 2 PCs and brain amyloid-β deposition was significant (p = 0.045). Conclusion: Six selected markers expressing peripheral blood microvesicles derived from cells of the neurovascular unit, when summarized into two principal components, were associated with brain amyloid-β deposition.
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24

Guo, Li, Yu Zhu, and Xian feng Du. "Compatibility studies on tea polysaccharide/amylose/water and tea polysaccharide/amylopectin/water." Carbohydrate Polymers 92, no. 1 (January 2013): 441–47. http://dx.doi.org/10.1016/j.carbpol.2012.09.037.

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25

Laudanski, Krzysztof, Jihane Hajj, Mariana Restrepo, Kumal Siddiq, Tony Okeke, and Daniel J. Rader. "Dynamic Changes in Central and Peripheral Neuro-Injury vs. Neuroprotective Serum Markers in COVID-19 Are Modulated by Different Types of Anti-Viral Treatments but Do Not Affect the Incidence of Late and Early Strokes." Biomedicines 9, no. 12 (November 29, 2021): 1791. http://dx.doi.org/10.3390/biomedicines9121791.

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The balance between neurodegeneration, neuroinflammation, neuroprotection, and COVID-19-directed therapy may underly the heterogeneity of SARS-CoV-2′s neurological outcomes. A total of 105 patients hospitalized with a diagnosis of COVID-19 had serum collected over a 6 month period to assess neuroinflammatory (MIF, CCL23, MCP-1), neuro-injury (NFL, NCAM-1), neurodegenerative (KLK6, τ, phospho τ, amyloids, TDP43, YKL40), and neuroprotective (clusterin, fetuin, TREM-2) proteins. These were compared to markers of nonspecific inflammatory responses (IL-6, D-dimer, CRP) and of the overall viral burden (spike protein). Data regarding treatment (steroids, convalescent plasma, remdasavir), pre-existing conditions, and incidences of strokes were collected. Amyloid β42, TDP43, NF-L, and KLK6 serum levels declined 2–3 days post-admission, yet recovered to admission baseline levels by 7 days. YKL-40 and NCAM-1 levels remained elevated over time, with clusters of differential responses identified among TREM-2, TDP43, and YKL40. Fetuin was elevated after the onset of COVID-19 while TREM-2 initially declined before significantly increasing over time. MIF serum level was increased 3–7 days after admission. Ferritin correlated with TDP-43 and KLK6. No treatment with remdesivir coincided with elevations in Amyloid-β40. A lack of convalescent plasma resulted in increased NCAM-1 and total tau, and steroidal treatments did not significantly affect any markers. A total of 11 incidences of stroke were registered up to six months after initial admission for COVID-19. Elevated D-dimer, platelet counts, IL-6, and leukopenia were observed. Variable MIF serum levels differentiated patients with CVA from those who did not have a stroke during the acute phase of COVID-19. This study demonstrated concomitant and opposite changes in neurodegenerative and neuroprotective markers persisting well into recovery.
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26

Cutler, Alicia A., Theodore Eugene Ewachiw, Giulia A. Corbet, Roy Parker, and Brad B. Olwin. "Myo-granules Connect Physiology and Pathophysiology." Journal of Experimental Neuroscience 13 (January 2019): 117906951984215. http://dx.doi.org/10.1177/1179069519842157.

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A hallmark of many neuromuscular diseases including Alzheimer disease, inclusion body myositis, amyotrophic lateral sclerosis, frontotemporal lobar dementia, and ocular pharyngeal muscular dystrophy is large cytoplasmic aggregates containing the RNA-binding protein, TDP-43. Despite acceptance that cytoplasmic TDP-43 aggregation is pathological, cytoplasmic TDP-43 assemblies form in healthy regenerating muscle. These recently discovered ribonucleoprotein assemblies, termed myo-granules, form in healthy muscle following injury and are readily cleared as the myofibers mature. The formation and dissolution of myo-granules during normal muscle regeneration suggests that these amyloid-like oligomers may be functional and that perturbations in myo-granule kinetics or composition may promote pathological aggregation.
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27

Kapaki, Elisabeth, Foteini Boufidou, Mara Bourbouli, Efstratios-Stylianos Pyrgelis, Vasilios C. Constantinides, Cleo Anastassopoulou, and George P. Paraskevas. "Cerebrospinal Fluid Biomarker Profile in TDP-43-Related Genetic Frontotemporal Dementia." Journal of Personalized Medicine 12, no. 10 (October 21, 2022): 1747. http://dx.doi.org/10.3390/jpm12101747.

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Cerebrospinal fluid (CSF) biomarkers, namely total tau, phospho-tau and amyloid beta peptides, have received much attention specifically regarding Alzheimer’s disease (AD), since they can detect the biochemical fingerprint of AD and serve as a diagnostic tool for accurate and early diagnosis during life. In the same way, biomarkers for other neurodegenerative disease pathologies are also needed. We present a case series of six patients with genetic frontotemporal dementia (FTD), with TDP-43 underlying proteinopathy, in an attempt to assess TDP-43 as a novel biomarker alone and in combination with established AD biomarkers for this specific patient group, based on the principles of personalized and precision medicine. Our results indicate that genetic TDP-43-FTD is characterized by increased CSF TPD-43 and increased TDP-43 × τΤ/τP-181 combination. Hence, TDP-43 combined with tau proteins could be a useful tool for the diagnosis of genetic FTD with TDP-43 underling histopathology, supplementing clinical, neuropsychological and imaging data.
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28

Jo, Myungjin, Shinrye Lee, Yu-Mi Jeon, Seyeon Kim, Younghwi Kwon, and Hyung-Jun Kim. "The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies." Experimental & Molecular Medicine 52, no. 10 (October 2020): 1652–62. http://dx.doi.org/10.1038/s12276-020-00513-7.

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Abstract TAR DNA-binding protein 43 (TDP-43) is a highly conserved nuclear RNA/DNA-binding protein involved in the regulation of RNA processing. The accumulation of TDP-43 aggregates in the central nervous system is a common feature of many neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), Alzheimer’s disease (AD), and limbic predominant age-related TDP-43 encephalopathy (LATE). Accumulating evidence suggests that prion-like spreading of aberrant protein aggregates composed of tau, amyloid-β, and α-synuclein is involved in the progression of neurodegenerative diseases such as AD and PD. Similar to those of prion-like proteins, pathological aggregates of TDP-43 can be transferred from cell-to-cell in a seed-dependent and self-templating manner. Here, we review clinical and experimental studies supporting the prion-like spreading of misfolded TDP-43 and discuss the molecular mechanisms underlying the propagation of these pathological aggregated proteins. The idea that misfolded TDP-43 spreads in a prion-like manner between cells may guide novel therapeutic strategies for TDP-43-associated neurodegenerative diseases.
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Bourbouli, Mara, Michael Rentzos, Anastasia Bougea, Vasiliki Zouvelou, Vasilios C. Constantinides, Ioannis Zaganas, Ioannis Evdokimidis, Elisabeth Kapaki, and George P. Paraskevas. "Cerebrospinal Fluid TAR DNA-Binding Protein 43 Combined with Tau Proteins as a Candidate Biomarker for Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Spectrum Disorders." Dementia and Geriatric Cognitive Disorders 44, no. 3-4 (2017): 144–52. http://dx.doi.org/10.1159/000478979.

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Background: Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are nowadays recognized as spectrum disorders with a molecular link, the TAR DNA-binding protein 43 (TDP-43), rendering it a surrogate biomarker for these disorders. Methods: We measured cerebrospinal fluid (CSF) levels of TDP-43, beta-amyloid peptide with 42 amino acids (Aβ42), total tau protein (τT), and tau protein phosphorylated at threonine 181 (τP-181) in 32 patients with ALS, 51 patients with FTD, and 17 healthy controls. Double-sandwich commercial enzyme-linked immunosorbent assays were used for measurements. Results: Both ALS and FTD patients presented with higher TDP-43 and τT levels compared to the control group. The combination of biomarkers in the form of the TDP-43 × τT / τP-181 formula achieved the best discrimination between ALS or FTD and controls, with sensitivities and specificities >0.8. Conclusion: Combined analysis of TDP-43, τT, and τP-181 in CSF may be useful for the antemortem diagnosis of ALS and FTD.
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Sennik, S., M. Anton, M. Cusimano, and D. G. Munoz. "13. Idiopathic Normal Pressure Hydrocephalus: Pathological changes in cortical biopsies in relation to function and response to treatment." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 42, S2 (August 2015): S5. http://dx.doi.org/10.1017/cjn.2015.261.

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Cortical peri-operative biopsies obtained from 11 idiopathic normal pressure hydrocephalus (iNPH) consenting patients (aged 67-88 years, median 74) were immuno-stained for Beta-amyloid (AMYB), Amyloid Precursor Protein (APP), total Tau, phosphorylated tau (AT8), Alpha Synuclein (AS), TDP- 43, P62 & GFAP. 5/11 patients had AMYB deposits, 2 diffuse plaques only, 3 diffuse and cored plaques; 1 also with amyloid angiopathy (CAA). Plaque neurites were labeled for APP and AT8 in all 3 patients with cored plaques; in one were these and neurofibrillary tangles labeled for total tau. The surface area covered by AMYB ranged from 12.8% to 0.08%. The presence of AMYB correlated with age (t, p=.02). Neither AS nor TDP-43 pathologies were identified. The density of cortical GFAP+ astrocytes showed a trend towards inverse correlation with age (r=-0.58, p=.06) but not with AMYB or AT8 pathologies. There were no significant correlations between pre-shunt Evans Ratio and MoCA scores and presence or amount of pathology. Improvement in ventriculomegaly (5/11) did not differ between patients with and without AMYB pathologies. Improvements in MoCA (6/8) were more common in patients without AMYB deposits (X2,p=.028; t, p=.04), but also in younger patients (t, p=.019). The patient with CAA improved, but the one with total tau pathology did not improve cognitively, although her gait did. In this preliminary study only AD-related pathology was found in iNPH. Cognitive improvement was associated with younger age and absence of amyloid deposits; however, a larger number of patients will be required to dissect these variables.
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Makaretz, Sara J., Megan Quimby, Jessica Collins, Nikos Makris, Scott McGinnis, Aaron Schultz, Neil Vasdev, Keith A. Johnson, and Bradford C. Dickerson. "Flortaucipir tau PET imaging in semantic variant primary progressive aphasia." Journal of Neurology, Neurosurgery & Psychiatry 89, no. 10 (October 6, 2017): 1024–31. http://dx.doi.org/10.1136/jnnp-2017-316409.

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ObjectiveThe semantic variant of primary progressive aphasia (svPPA) is typically associated with frontotemporal lobar degeneration (FTLD) with longTAR DNA-binding protein (TDP)-43-positive neuropil threads and dystrophic neurites (type C), and is only rarely due to a primary tauopathy or Alzheimer’s disease. We undertook this study to investigate the localisation and magnitude of the presumed tau Positron Emission Tomography (PET) tracer [18F]Flortaucipir (FTP; also known as T807 or AV1451) in patients with svPPA, hypothesising that most patients would not show tracer uptake different from controls.MethodsFTP and [11C]Pittsburgh compound B PET imaging as well as MRI were performed in seven patients with svPPA and in 20 controls. FTP signal was analysed by visual inspection and by quantitative comparison to controls, with and without partial volume correction.ResultsAll seven patients showed elevated FTP uptake in the anterior temporal lobe with a leftward asymmetry that was not observed in healthy controls. This elevated FTP signal, largely co-localised with atrophy, was evident on both visual inspection and quantitative cortical surface-based analysis. Five patients were amyloid negative, one was amyloid positive and one has an unknown amyloid status.ConclusionsIn this series of patients with clinical profiles, structural MRI and amyloid PET imaging typical for svPPA, FTP signal was unexpectedly elevated with a spatial pattern localised to areas of atrophy. This raises questions about the possible off-target binding of this tracer to non-tau molecules associated with neurodegeneration. Further investigation with autopsy analysis will help illuminate the binding target(s) of FTP in cases of suspected FTLD-TDP neuropathology.
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Li, Xinlei, Scott D. Smid, Jun Lin, Zhihong Gong, Si Chen, Fangning You, Yan Zhang, et al. "Neuroprotective and Anti-Amyloid β Effect and Main Chemical Profiles of White Tea: Comparison Against Green, Oolong and Black Tea." Molecules 24, no. 10 (May 19, 2019): 1926. http://dx.doi.org/10.3390/molecules24101926.

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White tea (WT) is one of six tea types originally derived from Fujian Province, China. White tea is known for its health-promoting properties. However, the neuroprotective and anti-aggregatory properties of WT against the hallmark toxic Alzheimer’s protein, Aβ have not been investigated. In this study, WT, green tea (GT), oolong tea (OT) and black tea (BT) were manufactured using tea leaves from the cultivar Camellia sinensis (Jin Guanyin). The protective effects of these tea extracts were then studied under oxidative stress conditions via t-bhp and H2O2 exposure, in addition to Aβ treatment using a PC-12 cell model. Each tea type failed to rescue PC-12 cells from either t-bhp or H2O2-mediated toxicity, however each extract exerted significant protection against Aβ-evoked neurotoxicity. Results of the Thioflavin T Kinetic (ThT) and TEM assay showed that Aβ aggregate formation was inhibited by each tea type. Additionally, TEM also supported the different anti-aggregatory effect of WT by modifying Aβ into an amorphous and punctate aggregate morphology. Higher accumulated precedent or potential neuroprotective compounds in WT, including ECG’’3Me, 8-C-ascorbyl-EGCG, GABA and Gln, in addition to flavonol or flavone glycosides detected by using UPLC-QTOF-MS and UPLC-QqQ-MS, may contribute to a favourable anti-aggregative and neuroprotective effect of WT against Aβ.
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Turbant, Florian, David Partouche, Omar El Hamoui, Sylvain Trépout, Théa Legoubey, Frank Wien, and Véronique Arluison. "Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq." Antibiotics 10, no. 3 (March 4, 2021): 257. http://dx.doi.org/10.3390/antibiotics10030257.

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Hfq is a bacterial regulator with key roles in gene expression. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, thanks to its binding to small regulatory noncoding RNAs. This property is of primary importance for bacterial adaptation and survival in hosts. Small RNAs and Hfq are, for instance, involved in the response to antibiotics. Previous work has shown that the E. coli Hfq C-terminal region (Hfq-CTR) self-assembles into an amyloid structure. It was also demonstrated that the green tea compound EpiGallo Catechin Gallate (EGCG) binds to Hfq-CTR amyloid fibrils and remodels them into nonamyloid structures. Thus, compounds that target the amyloid region of Hfq may be used as antibacterial agents. Here, we show that another compound that inhibits amyloid formation, apomorphine, may also serve as a new antibacterial. Our results provide an alternative in order to repurpose apomorphine, commonly used in the treatment of Parkinson’s disease, as an antibiotic to block bacterial adaptation to treat infections.
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Josephs, Keith A., Peter R. Martin, Stephen D. Weigand, Nirubol Tosakulwong, Marina Buciuc, Melissa E. Murray, Leonard Petrucelli, et al. "Protein contributions to brain atrophy acceleration in Alzheimer’s disease and primary age-related tauopathy." Brain 143, no. 11 (November 2020): 3463–76. http://dx.doi.org/10.1093/brain/awaa299.

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Abstract Alzheimer’s disease is characterized by the presence of amyloid-β and tau deposition in the brain, hippocampal atrophy and increased rates of hippocampal atrophy over time. Another protein, TAR DNA binding protein 43 (TDP-43) has been identified in up to 75% of cases of Alzheimer’s disease. TDP-43, tau and amyloid-β have all been linked to hippocampal atrophy. TDP-43 and tau have also been linked to hippocampal atrophy in cases of primary age-related tauopathy, a pathological entity with features that strongly overlap with those of Alzheimer’s disease. At present, it is unclear whether and how TDP-43 and tau are associated with early or late hippocampal atrophy in Alzheimer’s disease and primary age-related tauopathy, whether either protein is also associated with faster rates of atrophy of other brain regions and whether there is evidence for protein-associated acceleration/deceleration of atrophy rates. We therefore aimed to model how these proteins, particularly TDP-43, influence non-linear trajectories of hippocampal and neocortical atrophy in Alzheimer’s disease and primary age-related tauopathy. In this longitudinal retrospective study, 557 autopsied cases with Alzheimer’s disease neuropathological changes with 1638 ante-mortem volumetric head MRI scans spanning 1.0–16.8 years of disease duration prior to death were analysed. TDP-43 and Braak neurofibrillary tangle pathological staging schemes were constructed, and hippocampal and neocortical (inferior temporal and middle frontal) brain volumes determined using longitudinal FreeSurfer. Bayesian bivariate-outcome hierarchical models were utilized to estimate associations between proteins and volume, early rate of atrophy and acceleration in atrophy rates across brain regions. High TDP-43 stage was associated with smaller cross-sectional brain volumes, faster rates of brain atrophy and acceleration of atrophy rates, more than a decade prior to death, with deceleration occurring closer to death. Stronger associations were observed with hippocampus compared to temporal and frontal neocortex. Conversely, low TDP-43 stage was associated with slower early rates but later acceleration. This later acceleration was associated with high Braak neurofibrillary tangle stage. Somewhat similar, but less striking, findings were observed between TDP-43 and neocortical rates. Braak stage appeared to have stronger associations with neocortex compared to TDP-43. The association between TDP-43 and brain atrophy occurred slightly later in time (∼3 years) in cases of primary age-related tauopathy compared to Alzheimer’s disease. The results suggest that TDP-43 and tau have different contributions to acceleration and deceleration of brain atrophy rates over time in both Alzheimer’s disease and primary age-related tauopathy.
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35

Ye, Yuanyuan, Jiangling He, Zhijun He, Na Zhang, Xiaoqing Liu, Jiaojiao Zhou, Shuiyuan Cheng, and Jie Cai. "Evaluation of the Brewing Characteristics, Digestion Profiles, and Neuroprotective Effects of Two Typical Se-Enriched Green Teas." Foods 11, no. 14 (July 21, 2022): 2159. http://dx.doi.org/10.3390/foods11142159.

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As a functional beverage, selenium (Se)-enriched green tea (Se-GT) has gained increasing popularity for its superior properties in promoting health. In this study, we compared the brewing characteristics, in vitro digestion profiles, and protective effects on neurotoxicity induced through the amyloid-beta (Aβ) peptide of two typical Se-GTs (Enshi Yulu (ESYL) and Ziyang Maojian (ZYMJ), representing the typical low-Se green tea and high-Se green tea, respectively). ESYL and ZYMJ showed similar chemical component leaching properties with the different brewing methods, and the optimized brewing conditions were 5 min, 90 °C, 50 mL/g, and first brewing. The antioxidant activities of the tea infusions had the strongest positive correlation with the tea polyphenols among all of the leaching substances. The tea infusions of ESYL and ZYMJ showed similar digestive behaviors, and the tea polyphenols in the tea infusions were almost totally degraded or transferred after 150 min of dynamic digestion. Studies conducted in a cell model of Alzheimer’s disease (AD) showed that the extract from the high-Se green tea was more effective for neuroprotection compared with the low-Se green tea. Overall, our results revealed the best brewing conditions and digestion behaviors of Se-GT and the great potential of Se-GT or Se-enriched green extract (Se-GTE) to be used as promising AD-preventive beverages or food ingredients.
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36

Jamerlan, Angelo M., and Seong Soo A. An. "A Microplate-Based Approach to Map Interactions between TDP-43 and α-Synuclein." Journal of Clinical Medicine 11, no. 3 (January 24, 2022): 573. http://dx.doi.org/10.3390/jcm11030573.

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Trans-active response DNA-binding protein (TDP-43) is a multifunctional regulatory protein, whose abnormal deposition in neurons was linked to debilitating neurodegenerative diseases, such as amyotrophic lateral sclerosis, frontotemporal lobar degeneration, Limbic-predominant age-related TDP-43 encephalopathy, and Alzheimer’s disease with a secondary pathology. Several reports showed that TDP-43 proteinopathy as a comorbidity can form aggregates with other pathological proteins. The co-deposition of alpha synuclein and TDP-43 inclusions was previously reported in glial cells and by observing TDP-43 proteinopathy in Lewy body disease. In this study, it was hypothesized that alpha synuclein and TDP-43 may co-aggregate, resulting in comorbid synucleinopathy and TDP-43 proteinopathy. A solid-phase microplate-based immunoassay was used to map out the epitopes of anti-TDP-43 antibodies and locate the interaction of TDP-43 with α-synuclein. A region of the low complexity domain of TDP-43 (aa 311–314) was shown to interact with full-length α-synuclein. Conversely, full-length TDP-43 was shown to bind to the non-amyloid beta component of α-synuclein. Using in silico sequence-based prediction, the affinity and dissociation constant of full-length TDP-43 and α-synuclein were calculated to be −10.83 kcal/mol and 1.13 × 10−8, respectively. Taken together, this microplate-based method is convenient, economical, and rapid in locating antibody epitopes as well as interaction sites of two proteins.
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37

Petrlova, Jitka, Finja C. Hansen, Mariena J. A. van der Plas, Roland G. Huber, Matthias Mörgelin, Martin Malmsten, Peter J. Bond, and Artur Schmidtchen. "Aggregation of thrombin-derived C-terminal fragments as a previously undisclosed host defense mechanism." Proceedings of the National Academy of Sciences 114, no. 21 (May 4, 2017): E4213—E4222. http://dx.doi.org/10.1073/pnas.1619609114.

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Effective control of endotoxins and bacteria is crucial for normal wound healing. During injury, the key enzyme thrombin is formed, leading to generation of fibrin. Here, we show that human neutrophil elastase cleaves thrombin, generating 11-kDa thrombin-derived C-terminal peptides (TCPs), which bind to and form amorphous amyloid-like aggregates with both bacterial lipopolysaccharide (LPS) and gram-negative bacteria. In silico molecular modeling using atomic resolution and coarse-grained simulations corroborates our experimental observations, altogether indicating increased aggregation through LPS-mediated intermolecular contacts between clusters of TCP molecules. Upon bacterial aggregation, recombinantly produced TCPs induce permeabilization of Escherichia coli and phagocytic uptake. TCPs of about 11 kDa are present in acute wound fluids as well as in fibrin sloughs from patients with infected wounds. We noted aggregation and colocalization of LPS with TCPs in such fibrin material, which indicates the presence of TCP-LPS aggregates under physiological conditions. Apart from identifying a function of proteolyzed thrombin and its fragments, our findings provide an interesting link between the coagulation system, innate immunity, LPS scavenging, and protein aggregation/amyloid formation.
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38

Du, Fangzhou, Lin Zhou, Yan Jiao, Shuju Bai, Lu Wang, Junfeng Ma, and Xueqi Fu. "Ingredients in Zijuan Pu’er Tea Extract Alleviate β-Amyloid Peptide Toxicity in a Caenorhabditis elegans Model of Alzheimer’s Disease Likely through DAF-16." Molecules 24, no. 4 (February 18, 2019): 729. http://dx.doi.org/10.3390/molecules24040729.

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Amyloid-β, one of the hallmarks of Alzheimer’s disease (AD), is toxic to neurons and can also cause brain cell death. Oxidative stress is known to play an important role in AD, and there is strong evidence that oxidative stress is associated with amyloid-β. In the present study we report the protective effect of Zijuan Pu’er tea water extract (ZTWE) and the mixture of main ingredients (+)-catechins, caffeine and procyanidin (MCCP) in ZTWE on β-amyloid-induced toxicity in transgenic Caenorhabditis elegans (C. elegans) CL4176 expressing the human Aβ1–42 gene. ZTWE, (+)-catechins, caffeine, procyanidin and MCCP delayed the β-amyloid-induced paralysis to different degrees. The MCCP treatment did not affect the transcript abundance of amyloid-β transgene (amy-1); however, Thioflavin T staining showed a significant decrease in Aβ accumulation compared to untreated worms. Further research using transgenic worms found that MCCP promoted the translocation of DAF-16 from cytoplasm to nucleus and increased the expression of superoxide dismutase 3 (SOD-3). In addition, MCCP decreased the reactive oxygen species (ROS) content and increased the SOD activity in CL4176 worms. In conclusion, the results suggested that MCCP had a significant protective effect on β-amyloid-induced toxicity in C. elegans by reducing β-amyloid aggregation and inducing DAF-16 nuclear translocation that could activate the downstream signal pathway and enhance resistance to oxidative stress.
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39

Shenoy, Jayakrishna, Nadia El Mammeri, Antoine Dutour, Mélanie Berbon, Ahmad Saad, Alons Lends, Estelle Morvan, et al. "Structural dissection of amyloid aggregates of TDP‐43 and its C‐terminal fragments TDP‐35 and TDP‐16." FEBS Journal 287, no. 12 (December 20, 2019): 2449–67. http://dx.doi.org/10.1111/febs.15159.

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40

De Giorgi, Francesca, Muhammed Bilal Abdul-Shukkoor, Marianna Kashyrina, Leslie-Ann Largitte, Francesco De Nuccio, Brice Kauffmann, Alons Lends, et al. "Neurons with Cat’s Eyes: A Synthetic Strain of α-Synuclein Fibrils Seeding Neuronal Intranuclear Inclusions." Biomolecules 12, no. 3 (March 11, 2022): 436. http://dx.doi.org/10.3390/biom12030436.

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The distinct neuropathological features of the different α-Synucleinopathies, as well as the diversity of the α-Synuclein (α-Syn) intracellular inclusion bodies observed in post mortem brain sections, are thought to reflect the strain diversity characterizing invasive α-Syn amyloids. However, this “one strain, one disease” view is still hypothetical, and to date, a possible disease-specific contribution of non-amyloid factors has not been ruled out. In Multiple System Atrophy (MSA), the buildup of α-Syn inclusions in oligodendrocytes seems to result from the terminal storage of α-Syn amyloid aggregates first pre-assembled in neurons. This assembly occurs at the level of neuronal cytoplasmic inclusions, and even earlier, within neuronal intranuclear inclusions (NIIs). Intriguingly, α-Syn NIIs are never observed in α-Synucleinopathies other than MSA, suggesting that these inclusions originate (i) from the unique molecular properties of the α-Syn fibril strains encountered in this disease, or alternatively, (ii) from other factors specifically dysregulated in MSA and driving the intranuclear fibrillization of α-Syn. We report the isolation and structural characterization of a synthetic human α-Syn fibril strain uniquely capable of seeding α-Syn fibrillization inside the nuclear compartment. In primary mouse cortical neurons, this strain provokes the buildup of NIIs with a remarkable morphology reminiscent of cat’s eye marbles (see video abstract). These α-Syn inclusions form giant patterns made of one, two, or three lentiform beams that span the whole intranuclear volume, pushing apart the chromatin. The input fibrils are no longer detectable inside the NIIs, where they become dominated by the aggregation of endogenous α-Syn. In addition to its phosphorylation at S129, α-Syn forming the NIIs acquires an epitope antibody reactivity profile that indicates its organization into fibrils, and is associated with the classical markers of α-Syn pathology p62 and ubiquitin. NIIs are also observed in vivo after intracerebral injection of the fibril strain in mice. Our data thus show that the ability to seed NIIs is a strain property that is integrally encoded in the fibril supramolecular architecture. Upstream alterations of cellular mechanisms are not required. In contrast to the lentiform TDP-43 NIIs, which are observed in certain frontotemporal dementias and which are conditional upon GRN or VCP mutations, our data support the hypothesis that the presence of α-Syn NIIs in MSA is instead purely amyloid-strain-dependent.
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41

Jang, Hyemin, Yu-hyun Park, Young Sim Choe, Sung Hoon Kang, Eun-Sook Kang, Seunghoon Lee, Sang Won Seo, Hee Jin Kim, and Duk L. Na. "Amyloid Positive Hydrocephalus: A Hydrocephalic Variant of Alzheimer’s Disease?" Journal of Alzheimer's Disease 85, no. 4 (February 15, 2022): 1467–79. http://dx.doi.org/10.3233/jad-215110.

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Background: Alzheimer’s disease (AD) and normal pressure hydrocephalus (NPH) commonly coexist. Objective: We aimed to characterize an overlapping syndrome of AD and NPH that presents with gait disturbance, ventriculomegaly on magnetic resonance imaging, and significant amyloid deposition on positron emission tomography (PET). Methods: Of 114 patients who underwent cerebrospinal fluid (CSF) drainage for a possible diagnosis of NPH between 2015 and 2020 in Samsung Medical Center, we identified 24 patients (21.1%) with the NPH patients with amyloid deposition on PET, which we referred to as hydrocephalic AD in this study. We compared their clinical and imaging findings with those of 123 typical AD without hydrocephalic signs/symptoms. We also investigated the frequency and potential predictors of the tap test response in hydrocephalic AD. Results: Evans’ index was 0.36±0.03, and a disproportionately enlarged subarachnoid space was present in 54.2% of the hydrocephalic AD patients. The mean age (75.2±7.3 years) and the APOE4 frequency (68.2%) did not differ from those of AD controls. However, the hydrocephalic AD patients showed better memory and language performance, and a thinner cingulate cortex. About 42% of the hydrocephalic AD patients responded to the tap test, of whom seven underwent shunt surgery. Cognition did not improve, whereas gait improved after shunt surgery in all. Conclusion: Hydrocephalic AD has different neuropsychological and imaging characteristics from typical AD. Future studies are warranted to further investigate the effect of CSF removal on their clinical course and to elucidate the pathophysiological interaction between amyloid and NPH.
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42

Kapasi, Alifiya, Lei Yu, Christopher Stewart, Julie A. Schneider, David A. Bennett, and Patricia A. Boyle. "Association of Amyloid-β Pathology with Decision Making and Scam Susceptibility." Journal of Alzheimer's Disease 83, no. 2 (September 14, 2021): 879–87. http://dx.doi.org/10.3233/jad-210356.

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Background: Recent findings suggest that poor decision making and increased scam susceptibility are harbingers of Alzheimer’s disease (AD) dementia and may be among the earliest behavioral manifestations of pathologic cognitive aging. However, the degree to which poor decision making and scam susceptibility reflect accumulating Alzheimer’s disease (AD) pathology remains unclear. Objective: To investigate the associations of AD pathology with decision making and scam susceptibility in older adults without dementia. Methods: Data came from 198 deceased participants without clinical dementia (mean age at death = 90 years; 69%women) from two ongoing studies of aging. All underwent annual clinical evaluations, completed assessments of healthcare and financial decision making and scam susceptibility, and brain donation. Neuropathologic evaluations quantified pathologic hallmarks of AD, amyloid-β and tau-tangles, Lewy body pathology, and TDP-43 proteinopathy. Results: In linear regression models adjusted for demographics, amyloid-β pathology was associated with lower decision making (estimate = –0.35; SE = 0.16, p = 0.03), particularly healthcare decision making (estimate = –0.20; SE = 0.09, p = 0.03), as well as greater scam susceptibility (estimate = 0.12; SE = 0.04, p = 0.003); tau-tangle pathology was not related. Further, TDP-43 pathology was associated with greater scam susceptibility (estimate = 0.10; SE = 0.04; p = 0.02). Conclusion: Accumulating AD pathology, particularly amyloid-β, is associated with poor decision making and increased scam susceptibility among older persons without overt cognitive impairment. These findings provide compelling evidence that decision making and scam susceptibility are sensitive to the earliest pathological changes of AD.
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Zheng, Qiuchen, Micheal T. Kebede, Merc M. Kemeh, Saadman Islam, Bethany Lee, Stuart D. Bleck, Liliana A. Wurfl, and Noel D. Lazo. "Inhibition of the Self-Assembly of Aβ and of Tau by Polyphenols: Mechanistic Studies." Molecules 24, no. 12 (June 22, 2019): 2316. http://dx.doi.org/10.3390/molecules24122316.

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The amyloid-β (Aβ) peptide and tau protein are thought to play key neuropathogenic roles in Alzheimer’s disease (AD). Both Aβ and tau self-assemble to form the two major pathological hallmarks of AD: amyloid plaques and neurofibrillary tangles, respectively. In this review, we show that naturally occurring polyphenols abundant in fruits, vegetables, red wine, and tea possess the ability to target pathways associated with the formation of assemblies of Aβ and tau. Polyphenols modulate the enzymatic processing of the amyloid-β precursor protein and inhibit toxic Aβ oligomerization by enhancing the clearance of Aβ42 monomer, modulating monomer–monomer interactions and remodeling oligomers to non-toxic forms. Additionally, polyphenols modulate tau hyperphosphorylation and inhibit tau β-sheet formation. The anti-Aβ-self-assembly and anti-tau-self-assembly effects of polyphenols increase their potential as preventive or therapeutic agents against AD, a complex disease that involves many pathological mechanisms.
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Davis, Stephani A., Kok Ann Gan, James A. Dowell, Nigel J. Cairns, and Michael A. Gitcho. "TDP-43 expression influences amyloidβ plaque deposition and tau aggregation." Neurobiology of Disease 103 (July 2017): 154–62. http://dx.doi.org/10.1016/j.nbd.2017.04.012.

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45

Buciuc, Marina, Nirubol Tosakulwong, Mary M. Machulda, Jennifer L. Whitwell, Stephen D. Weigand, Melissa E. Murray, R. Ross Reichard, et al. "TAR DNA-Binding Protein 43 Is Associated with Rate of Memory, Functional and Global Cognitive Decline in the Decade Prior to Death." Journal of Alzheimer's Disease 80, no. 2 (March 23, 2021): 683–93. http://dx.doi.org/10.3233/jad-201166.

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Background: Transactive response DNA-binding protein of 43 kDa (TDP-43) is associated with memory impairment and overall cognitive decline. It is unclear how TDP-43 contributes to the rate of clinical decline. Objective: To determine whether cross-sectional and longitudinal cognitive and functional decline are associated with anatomical distribution of TDP-43 in the brain. Methods: Longitudinal clinical-neuropathologic autopsy cohort study of 385 initially cognitively normal/mildly impaired older adults prospectively followed until death. We investigated how TDP-43, amyloid-β (Aβ), tau neurofibrillary tangles (NFT), Lewy body disease (LBD), age, sex, and genetics are associated with clinical scores and rates of their longitudinal decline. Results: Of 385 participants, 260 (68%) had no TDP-43, 32 (8%) had TDP-43 limited to amygdala, and 93 (24%) had TDP-43 in the hippocampus and beyond. Higher TDP-43 and Braak NFT stages independently were associated with faster decline in global cognition, functional performance measured by Clinical Dementia Rating scale, and naming and episodic memory, whereas older age was associated with slower rate of cognitive, psychiatric, and functional decline. Cross-sectionally the following associations were found: higher TDP-43 and Braak NFT - worse performance; higher Aβ burden - worse global cognition, more behavioral changes, the latter also with higher LBD; older age - worse naming, lower frequency of behavioral changes; female sex - more impaired naming and better preserved episodic memory. There were no genetic associations. Conclusion: The association of TDP-43 distribution with decline in cognitive and functional performance suggests that TDP-43 is playing a role in the clinical progression to dementia. Further characterization of clinical features associated with TDP-43 can facilitate establishment of antemortem diagnosis.
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Cuevas, Eva P., Alberto Rodríguez-Fernández, Valle Palomo, Ana Martínez, and Ángeles Martín-Requero. "TDP-43 Pathology and Prionic Behavior in Human Cellular Models of Alzheimer’s Disease Patients." Biomedicines 10, no. 2 (February 5, 2022): 385. http://dx.doi.org/10.3390/biomedicines10020385.

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Alzheimer’s disease (AD) is a neurodegenerative disorder for which there is currently no effective treatment. Despite advances in the molecular pathology of the characteristic histopathological markers of the disease (tau protein and β-amyloid), their translation to the clinic has not provided the expected results. Increasing evidences have demonstrated the presence of aggregates of TDP-43 (TAR DNA binding protein 43) in the postmortem brains of patients diagnosed with AD. The present research is focused on of the study of the pathological role of TDP-43 in AD. For this purpose, immortalized lymphocytes samples from patients diagnosed with different severity of sporadic AD were used and the TDP-43 pathology was analyzed against controls, looking for differences in their fragmentation, phosphorylation and cellular location using Western blot and immunocytochemical techniques. The results revealed an increase in TDP-43 fragmentation, as well as increased phosphorylation and aberrant localization of TDP-43 in the cytosolic compartment of lymphocytes of patients diagnosed with severe AD. Moreover, a fragment of approximately 25 KD was found in the extracellular medium of cells derived from severe AD individuals that seem to have prion-like characteristics. We conclude that TDP-43 plays a key role in AD pathogenesis and its cell to cell propagation.
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Ma, Ya-Hui, Jia-Huan Wu, Wei Xu, Xue-Ning Shen, Hui-Fu Wang, Xiao-He Hou, Xi-Peng Cao, et al. "Associations of Green Tea Consumption and Cerebrospinal Fluid Biomarkers of Alzheimer’s Disease Pathology in Cognitively Intact Older Adults: The CABLE Study." Journal of Alzheimer's Disease 77, no. 1 (September 1, 2020): 411–21. http://dx.doi.org/10.3233/jad-200410.

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Background: Green tea has been widely recognized in ameliorating cognitive impairment and Alzheimer’s disease (AD), especially the progression of cognitive dysfunction. But the underlying mechanism is still unclear. Objective: This study was designed to determine the role of green tea consumption in the association with cerebrospinal fluid (CSF) biomarkers of AD pathology and to ascertain whether specific population backgrounds showed the differences toward these relationships. Methods: Multivariate linear models analyzed the available data on CSF biomarkers and frequency of green tea consumption of 722 cognitively intact participants from the Chinese Alzheimer’s Biomarker and LifestylE (CABLE) database, and we additionally detected the interaction effects of tea consumption with APOE ɛ4 status and gender using a two-way analysis of covariance. Results: Frequent green tea consumption was associated with a decreased level of CSF total-tau protein (t-tau) (p = 0.041) but not with the levels of CSF amyloid-β 42 (Aβ42) and CSF phosphorylated tau. The more pronounced associations of green tea consumption with CSF t-tau (p = 0.007) and CSF t-tau/Aβ42 (p = 0.039) were observed in individuals aged 65 years or younger. Additionally, males with frequent green tea consumption had a significantly low level of CSF t-tau/Aβ42 and a modest trend toward decreased CSF t-tau. There were no interaction effects of green tea consumption with APOE ɛ4 and gender. Conclusion: Collectively, our findings consolidated the favorable effects of green tea on the mitigation of AD risk. The constituents of green tea may improve abnormal tau metabolism and are promising targets in interventions and drug therapies.
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Chien, Hung-Ming, Chi-Chang Lee, and Joseph Jen-Tse Huang. "The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils." International Journal of Molecular Sciences 22, no. 15 (July 30, 2021): 8213. http://dx.doi.org/10.3390/ijms22158213.

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Transactive response DNA-binding protein 43 (TDP-43) is a nucleic acid-binding protein that is involved in transcription and translation regulation, non-coding RNA processing, and stress granule assembly. Aside from its multiple functions, it is also known as the signature protein in the hallmark inclusions of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) patients. TDP-43 is built of four domains, but its low-complexity domain (LCD) has become an intense research focus that brings to light its possible role in TDP-43 functions and involvement in the pathogenesis of these neurodegenerative diseases. Recent endeavors have further uncovered the distinct biophysical properties of TDP-43 under various circumstances. In this review, we summarize the multiple structural and biochemical properties of LCD in either promoting the liquid droplets or inducing fibrillar aggregates. We also revisit the roles of the LCD in paraspeckles, stress granules, and cytoplasmic inclusions to date.
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Xiao Jiang, Yi, Qin Cao, Michael R. Sawaya, Romany Abskharon, Peng Ge, Michael DeTure, Dennis W. Dickson, and David S. Eisenberg. "Amyloid fibrils from frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) are composed of TMEM106B, rather than TDP-43." Biophysical Journal 121, no. 3 (February 2022): 349a. http://dx.doi.org/10.1016/j.bpj.2021.11.983.

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Kurz, Alexander, and Timo Grimmer. "Neue Therapieansätze." Therapeutische Umschau 72, no. 4 (April 1, 2015): 279–85. http://dx.doi.org/10.1024/0040-5930/a000676.

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Die häufigsten Ursachen der Demenz sind fortschreitende und irreversible neurodegenerative Krankheiten des Gehirns. An erster Stelle steht die Alzheimer-Krankheit, gefolgt von Parkinson- und Lewy-Körper-Krankheit und den Frontotemporalen lobären Degenerationen. Die neurodegenerativen Prozesse sind durch die Entstehung, Zusammenballung und Ablagerung von pathologischen Proteinen gekennzeichnet. Diese sind β-Amyloid und Tau bei der Alzheimer-Krankheit; α-Synuklein bei der Parkinson- und Lewy-Körper-Krankheit sowie Tau, TDP-43 und FUS bei den Frontotemporalen Degenerationen. Die Aggregation zu Oligomeren und Fibrillen sowie die nachfolgende Sedimentierung dieser Proteine führen zur Funktionsstörung von Nervenzellen, zum Versagen von synaptischen Verbindungen und schließlich zum Zelluntergang. Die Defizite und Imbalancen von Neurotransmittersystemen, die einen wichtigen Ansatzpunkt der derzeitigen pharmakologischen Therapie der Demenz darstellen, sind Folgen des Nervenzelluntergangs. Viele der neuen, in Entwicklung befindlichen Therapieansätze sind darauf gerichtet, die Entstehung, Zusammenballung und Ablagerung pathologischer Proteine zu verhindern, zu verlangsamen oder abzumildern. Wichtige Strategien sind Hemmung der Sekretasen, die β-Amyloid generieren, aktive und passive Immunisierung gegen β-Amyloid, Hemmung der Aggregation von β-Amyloid und Tau sowie Stimulierung des aktiven Transports von β-Amyloid aus dem Gehirn. In klinischer Prüfung befinden sich auch neue symptomatische Therapieformen einschließlich der simultanen Stimulation mehrerer Neurotransmittersysteme, des Ausgleichs der zerebralen Insulinresistenz und der Neuroprotektion mittels spezieller Nahrungsbestandteile. Neben den pharmakologischen Behandlungsformen werden auch nicht-medikamentöse Interventionen weiterentwickelt.
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