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Biomedicines
Special Issues
Amyloid Pathology: Cellular Mechanism and Therapy Targets
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Amyloid Pathology: Cellular Mechanism and Therapy Targets

A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Neurobiology and Clinical Neuroscience".

Deadline for manuscript submissions: closed (30 April 2024) | Viewed by 7628

Special Issue Editors

Dr. Tamas Letoha

E-Mail Website
Guest Editor
Pharmacoidea Ltd., Szeged, Hungary
Interests: peptides; cell signaling; proteins; signal transduction; inflammatory diseases; inflammation; drug delivery; neurodegeneration; protein aggregation; flow cytometry
Dr. Gábor Veres

E-Mail Website
Guest Editor
Pharmacoidea Ltd., Szeged, Hungary
Interests: neurodegeneration; neuroscience; neurology; neurochemistry; high-performance liquid chromatography; glutamate; neuroprotection; Huntington's disease; neurobiology and brain physiology

Special Issue Information

Dear Colleagues,

Amyloidosis is one of the misfolded protein diseases, caused by the intracellular or extracellular accumulation of amyloid fibrils. Many human proteins have been found to form amyloid in pathology and to be associated with well-defined diseases, such as beta amyloid peptide in Alzheimer’s disease and alpha-synuclein in Parkinson’s disease. This Special Issue will focus on the latest advances in amyloid research, including new insights into molecular biology, pharmacology, pathophysiology, and therapeutical approaches. Original research articles and review articles are invited.

Dr. Tamas Letoha
Dr. Gábor Veres
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomedicines is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • amyloid
  • amyloidosis
  • Alzheimer’s disease
  • Parkinson’s disease
  • neurodegeneration
  • alpha-synuclein
  • beta amyloid peptide

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Published Papers (3 papers)

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Research

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18 pages, 5232 KiB  
Article
Amyloid-Beta Peptides Trigger Premature Functional and Gene Expression Alterations in Human-Induced Neurons
by Ana Raquel Melo de Farias, Alexandre Pelletier, Lukas Cruz Carvalho Iohan, Orthis Saha, Amélie Bonnefond, Philippe Amouyel, Fabien Delahaye, Jean-Charles Lambert and Marcos R. Costa
Biomedicines 2023, 11(9), 2564; https://doi.org/10.3390/biomedicines11092564 - 18 Sep 2023
Cited by 3 | Viewed by 1880
Abstract
Alzheimer’s disease (AD) is the most prevalent cause of dementia in the elderly, characterized by the presence of amyloid-beta (Aβ) plaques, neurofibrillary tangles, neuroinflammation, synapse loss and neurodegeneration in the brain. The amyloid cascade hypothesis postulates that deposition of Aβ peptides is the [...] Read more.
Alzheimer’s disease (AD) is the most prevalent cause of dementia in the elderly, characterized by the presence of amyloid-beta (Aβ) plaques, neurofibrillary tangles, neuroinflammation, synapse loss and neurodegeneration in the brain. The amyloid cascade hypothesis postulates that deposition of Aβ peptides is the causative agent of AD pathology, but we still lack comprehensive understanding of the molecular mechanisms connecting Aβ peptides to neuronal dysfunctions in AD. In this work, we investigate the early effects of Aβ peptide accumulation on the functional properties and gene expression profiles of human-induced neurons (hiNs). We show that hiNs acutely exposed to low concentrations of both cell-secreted Aβ peptides or synthetic Aβ1–42 exhibit alterations in the frequency of calcium transients suggestive of increased neuronal excitability. Using single-cell RNA sequencing, we also show that cell-secreted Aβ up-regulates the expression of several synapse-related genes and down-regulates the expression of genes associated with metabolic stress mainly in glutamatergic neurons and, to a lesser degree, in GABAergic neurons and astrocytes. These neuronal alterations correlate with activation of the SEMA5, EPHA and NECTIN signaling pathways, which are important regulators of synaptic plasticity. Altogether, our findings indicate that slight elevations in Aβ concentrations are sufficient to elicit transcriptional changes in human neurons, which can contribute to early alterations in neural network activity. Full article
(This article belongs to the Special Issue Amyloid Pathology: Cellular Mechanism and Therapy Targets)
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27 pages, 9894 KiB  
Article
Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid
by Irena Roterman, Katarzyna Stapor and Leszek Konieczny
Biomedicines 2023, 11(5), 1324; https://doi.org/10.3390/biomedicines11051324 - 29 Apr 2023
Cited by 2 | Viewed by 1391
Abstract
The structural transformation producing amyloids is a phenomenon that sheds new light on the protein folding problem. The analysis of the polymorphic structures of the α-synuclein amyloid available in the PDB database allows analysis of the amyloid-oriented structural transformation itself, but also the [...] Read more.
The structural transformation producing amyloids is a phenomenon that sheds new light on the protein folding problem. The analysis of the polymorphic structures of the α-synuclein amyloid available in the PDB database allows analysis of the amyloid-oriented structural transformation itself, but also the protein folding process as such. The polymorphic amyloid structures of α-synuclein analyzed employing the hydrophobicity distribution (fuzzy oil drop model) reveal a differentiation with a dominant distribution consistent with the micelle-like system (hydrophobic core with polar shell). This type of ordering of the hydrophobicity distribution covers the entire spectrum from the example with all three structural units (single chain, proto-fibril, super-fibril) exhibiting micelle-like form, through gradually emerging examples of local disorder, to structures with an extremely different structuring pattern. The water environment directing protein structures towards the generation of ribbon micelle-like structures (concentration of hydrophobic residues in the center of the molecule forming a hydrophobic core with the exposure of polar residues on the surface) also plays a role in the amyloid forms of α-synuclein. The polymorphic forms of α-synuclein reveal local structural differentiation with a common tendency to accept the micelle-like structuralization in certain common fragments of the polypeptide chain of this protein. Full article
(This article belongs to the Special Issue Amyloid Pathology: Cellular Mechanism and Therapy Targets)
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Review

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15 pages, 615 KiB  
Review
The Roles of the Amyloid Beta Monomers in Physiological and Pathological Conditions
by Thomas Gabriel Schreiner, Oliver Daniel Schreiner, Maricel Adam and Bogdan Ovidiu Popescu
Biomedicines 2023, 11(5), 1411; https://doi.org/10.3390/biomedicines11051411 - 10 May 2023
Cited by 11 | Viewed by 3429
Abstract
Amyloid beta peptide is an important biomarker in Alzheimer’s disease, with the amyloidogenic hypothesis as one of the central hypotheses trying to explain this type of dementia. Despite numerous studies, the etiology of Alzheimer’s disease remains incompletely known, as the pathological accumulation of [...] Read more.
Amyloid beta peptide is an important biomarker in Alzheimer’s disease, with the amyloidogenic hypothesis as one of the central hypotheses trying to explain this type of dementia. Despite numerous studies, the etiology of Alzheimer’s disease remains incompletely known, as the pathological accumulation of amyloid beta aggregates cannot fully explain the complex clinical picture of the disease. Or, for the development of effective therapies, it is mandatory to understand the roles of amyloid beta at the brain level, from its initial monomeric stage prior to aggregation in the form of senile plaques. In this sense, this review aims to bring new, clinically relevant data on a subject intensely debated in the literature in the last years. In the first part, the amyloidogenic cascade is reviewed and the possible subtypes of amyloid beta are differentiated. In the second part, the roles played by the amyloid beta monomers in physiological and pathological (neurodegenerative) conditions are illustrated based on the most relevant and recent studies published on this topic. Finally, considering the importance of amyloid beta monomers in the pathophysiology of Alzheimer’s disease, new research directions with diagnostic and therapeutic impacts are suggested. Full article
(This article belongs to the Special Issue Amyloid Pathology: Cellular Mechanism and Therapy Targets)
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