scholarly journals Accumulation of Innate Amyloid Beta Peptide in Glioblastoma Tumors

2019 ◽  
Vol 20 (10) ◽  
pp. 2482 ◽  
Author(s):  
Lilia Y. Kucheryavykh ◽  
Jescelica Ortiz-Rivera ◽  
Yuriy V. Kucheryavykh ◽  
Astrid Zayas-Santiago ◽  
Amanda Diaz-Garcia ◽  
...  
Keyword(s):  
Blood Vessels ◽  
Amyloid Beta ◽  
Glioma Cells ◽  
Amyloid Beta Peptide ◽  
Enzyme Linked Immunosorbent Assay ◽  
Aβ Peptide ◽  
Brain Areas ◽  
Aβ Peptides ◽  
Beta Peptide ◽  
Glioma Tumors

Immunostaining with specific antibodies has shown that innate amyloid beta (Aβ) is accumulated naturally in glioma tumors and nearby blood vessels in a mouse model of glioma. In immunofluorescence images, Aβ peptide coincides with glioma cells, and enzyme-linked immunosorbent assay (ELISA) have shown that Aβ peptide is enriched in the membrane protein fraction of tumor cells. ELISAs have also confirmed that the Aβ(1–40) peptide is enriched in glioma tumor areas relative to healthy brain areas. Thioflavin staining revealed that at least some amyloid is present in glioma tumors in aggregated forms. We may suggest that the presence of aggregated amyloid in glioma tumors together with the presence of Aβ immunofluorescence coinciding with glioma cells and the nearby vasculature imply that the source of Aβ peptides in glioma can be systemic Aβ from blood vessels, but this question remains unresolved and needs additional studies.

scholarly journals Curcumin Inhibits the Primary Nucleation of Amyloid-Beta Peptide: A Molecular Dynamics Study

Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1323
Author(s):  
Irini Doytchinova ◽  
Mariyana Atanasova ◽  
Evdokiya Salamanova ◽  
Stefan Ivanov ◽  
Ivan Dimitrov
Keyword(s):  
Molecular Dynamics ◽  
Hydrogen Bonds ◽  
Amyloid Beta ◽  
Amyloid Plaques ◽  
Amyloid Beta Peptide ◽  
Aβ Peptides ◽  
Amyloid Peptides ◽  
Primary Nucleation ◽  
Beta Peptide ◽  
Good Agreement

The amyloid plaques are a key hallmark of neurodegenerative diseases such as Alzheimer’s disease and Parkinson’s disease. Amyloidogenesis is a complex long-lasting multiphase process starting with the formation of nuclei of amyloid peptides: a process assigned as a primary nucleation. Curcumin (CU) is a well-known inhibitor of the aggregation of amyloid-beta (Aβ) peptides. Even more, CU is able to disintegrate preformed Aβ firbils and amyloid plaques. Here, we simulate by molecular dynamics the primary nucleation process of 12 Aβ peptides and investigate the effects of CU on the process. We found that CU molecules intercalate among the Aβ chains and bind tightly to them by hydrogen bonds, hydrophobic, π–π, and cation–π interactions. In the presence of CU, the Aβ peptides form a primary nucleus of a bigger size. The peptide chains in the nucleus become less flexible and more disordered, and the number of non-native contacts and hydrogen bonds between them decreases. For comparison, the effects of the weaker Aβ inhibitor ferulic acid (FA) on the primary nucleation are also examined. Our study is in good agreement with the observation that taken regularly, CU is able to prevent or at least delay the onset of neurodegenerative disorders.

On the propagation of the OH radical produced by Cu-amyloid beta peptide model complexes. Insight from molecular modelling

Metallomics ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 1765-1780
Author(s):  
Federica Arrigoni ◽  
Fabio Rizza ◽  
Renata Tisi ◽  
Luca De Gioia ◽  
Giuseppe Zampella ◽  
...  
Keyword(s):  
Amyloid Beta ◽  
Molecular Modelling ◽  
Amyloid Beta Peptide ◽  
Side Chains ◽  
Oh Radical ◽  
Ros Production ◽  
Aβ Peptide ◽  
Model Complexes ◽  
Beta Peptide ◽  
Amyloid Aβ

Alzheimer's disease involves an anomalous interaction of copper with the amyloid Aβ peptide, inducing ROS production. The propagation of the OH radical toward Aβ side chains is investigated by molecular modelling.

Erythrocyte Amyloid Beta Peptide Isoform Distributions in Alzheimer and Mild Cognitive Impairment

2019 ◽  
Vol 16 (11) ◽  
pp. 1050-1054 ◽  
Author(s):  
Petter Järemo ◽  
Alenka Jejcic ◽  
Vesna Jelic ◽  
Tasmin Shahnaz ◽  
Magnus Oweling ◽  
...  
Keyword(s):  
Cognitive Impairment ◽  
Mild Cognitive Impairment ◽  
Amyloid Beta ◽  
Blood Cells ◽  
Cell Damage ◽  
Amyloid Beta Peptide ◽  
Low Density ◽  
Aβ Peptides ◽  
Cell Accumulation ◽  
Beta Peptide

Introduction: We recently showed that Amyloid Beta (Aβ)40 accumulates in erythrocytes and possibly causes cell damage as evidenced by an increased number of assumed injured low-density (kg/L) erythrocytes. Furthermore, we have suggested a separation technique to isolate and concentrate such damaged red blood cells for subsequent analysis. Objectives: We isolated high- and low-density erythrocytes and investigated the accumulation patterns of the Aβ peptides (Aβ40, Aβ42, and Aβ43) in Alzheimer (AD), mild cognitive impairment (MCI), and Subjective Cognitive Impairment (SCI). Methods: Whole blood was fractionated through a density gradient, resulting in two concentrated highand presumed injured low-density erythrocyte fractions. After cell lysis, intracellular Aβ40, Aβ42, and Aβ43 were quantified by ELISA. Results: In both high- and low-density erythrocytes, Aβ40 displayed the lowest concentration in MCI, while it was equal and higher in AD and SCI. Aβ40 was detected at a 10-fold higher level than Aβ42, and in injured low-density erythrocytes, the lowest quantity of Aβ42 was found in AD and MCI. Aβ40 exhibited a 100-fold greater amount than Aβ43, and lighter erythrocytes of MCI subjects displayed less intracellular Aβ43 than SCI. Conclusion: Red blood cell accumulation patterns of Aβ40, Aβ42, and Aβ43 differ significantly between AD, MCI, and SCI. The data must be verified through larger clinical trials. It is, however, tenable that Aβ peptide distributions in erythrocyte subpopulations have the potential to be used for diagnostic purposes.

G-lymphatic, vascular and immune pathways for Aβ clearance cascade and therapeutic targets for Alzheimer’s disease

2020 ◽  
Vol 23 ◽  
Author(s):  
Saurav Chakraborty ◽  
Jyothsna ThimmaReddygari ◽  
Divakar Selvaraj
Keyword(s):  
Alzheimer Disease ◽  
Amyloid Precursor Protein ◽  
Amyloid Beta ◽  
Complement System ◽  
Therapeutic Targets ◽  
Neuronal Cell ◽  
Precursor Protein ◽  
Amyloid Beta Peptide ◽  
Beta Peptide ◽  
Immune Pathways

The Alzheimer disease is a age related neurodegenerative disease. The factors causing alzheimer disease are numerous. Research on humans and rodent models predicted various causative factors involved in Alzheimer disease progression. Among them, neuroinflammation, oxidative stress and apoptosis play a major role because of accumulation of extracellular amyloid beta peptides. Here, the clearance of amyloid beta peptide plays a major role because of the imbalance in the production and clearance of the amyloid beta peptide. Additionally, neuroinflammation by microglia, astrocytes, cytokines, chemokines and the complement system also have a major role in Alzheimer disease. The physiological clearance pathways involved in amyloid beta peptide are glymphatic, vascular and immune pathways. Amyloid precursor protein, low density lipoprotein receptor-related protein 1, receptor for advanced glycation end product, apolipoprotein E, clusterin, aquaporin 4, auto-antibodies, complement system, cytokines and microglia are involved in amyloid beta peptide clearance pathways across the blood brain barrier. The plaque formation in the brain by alternative splicing of amyloid precursor protein and production of misfolded protein results in amyloid beta agglomeration. This insoluble amyloid beta leads to neurodegenerative cascade and neuronal cell death occurs. Studies had shown disturbed sleep may be a risk factor for dementia and cognitive decline. In this review, the therapeutic targets for alzheimer disease via focussing on pathways for amyloid beta clearance are discussed.

Conformations and Biological Activities of Amyloid Beta Peptide 25-35

2009 ◽  
Vol 999 (999) ◽  
pp. 1-6 ◽  
Author(s):  
L. Millucci ◽  
L. Ghezzi ◽  
G. Bernardini ◽  
A. Santucci
Keyword(s):  
Amyloid Beta ◽  
Biological Activities ◽  
Amyloid Beta Peptide ◽  
Beta Peptide
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