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Biomolecules
Special Issues
Molecular and Cellular Basis of Alzheimer's Disease
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Molecular and Cellular Basis of Alzheimer's Disease

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Medicine".

Deadline for manuscript submissions: closed (31 July 2022) | Viewed by 5184

Special Issue Editors

Dr. Xavier Gallart-Palau

E-Mail Website
Guest Editor
1. Institut d'Investigació Sanitària Pere Virgili (IISPV), Reus, Spain
2. Carlos III Health Institute (Instituto de Salud Carlos III), Madrid, Spain
Interests: neurochemistry; proteinopathy; Alzheimer’s disease; vascular dementia; neurovascular unit; extracellular vesicles; proteomics
Special Issues, Collections and Topics in MDPI journals
Dr. Aida Serra

E-Mail Website
Guest Editor
1. IMDEA Food & Health Sciences Research Institute, +Pec Proteomics, Campus of International Excellence UAM+CSIC, Old Cantoblanco Hospital, 8 Crta. Canto Blanco, 28049 Madrid, Spain
2. Proteored-Instituto de Salud Carlos III (ISCIII), Madrid, Spain
Interests: proteomics; neurodegeneration; extracellular vesicles; protein post-translational modifications; degenerative protein modifications; metabolism; human diseases
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Giulio Pasinetti

E-Mail Website
Guest Editor
Icahn School of Medicine at Mount Sinai, New York, NY, USA
Interests: inflammation; inflammasome; beta-amyloid; Tau; microglia; apoptosis; caspase; Alzheimer’s disease; Parkinson’s disease; amyotrophic lateral sclerosis; frontotemporal dementia; traumatic brain injury; polyphenols; bioavailability; drug discovery
Special Issues, Collections and Topics in MDPI journals
Dr. Joyce Harary

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Guest Editor
Icahn School of Medicine at Mount Sinai, New York, NY, USA
Interests: Alzheimer’s Disease
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Alzheimer’s disease (AD) is the main contributor to dementia worldwide, a cognitive syndrome that progressively and fatally impairs the ability of the affected individuals to perform essential everyday tasks. Dementia is also the major cause of disability among elderly people worldwide, and its derived social and economic costs are massive. Although the molecular and cellular basis of AD remains a matter of intense scientific investigation and has been partially uncovered, several crucial aspects related to the neuropathology of AD still require our attention and interest. These aspects, although not exhaustive, may involve the following actions: uncovering currently unknown idiopathic triggering factors, shedding light on the molecular mechanisms of neuropathology onset, understanding common neuropathological mechanisms that defy brain cell heterogeneity, identifying potential early-onset biological diagnostic and prognostic markers (neuropathology onset proposed as early as 20 years before clinical diagnosis). Thus, this Special Issue focuses on generating genuine and valuable scientific knowledge on the molecular and cellular basis of AD, with foresight on the apparition of novel diagnosis and therapeutic strategies for this fatal neurological disorder.

You may choose our Joint Special Issue in NeuroSci, or Joint Special Issue in Cells.

Dr. Xavier Gallart-Palau
Dr. Aida Serra
Prof. Dr. Giulio Pasinetti
Dr. Joyce Harary
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. Biomolecules 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 2700 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.

Published Papers (2 papers)

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Research

22 pages, 26643 KiB  
Article
Spreading of P301S Aggregated Tau Investigated in Organotypic Mouse Brain Slice Cultures
by Dhwani S. Korde and Christian Humpel
Biomolecules 2022, 12(9), 1164; https://0-doi-org.brum.beds.ac.uk/10.3390/biom12091164 - 23 Aug 2022
Cited by 3 | Viewed by 2380
Abstract
Tau pathology extends throughout the brain in a prion-like fashion through connected brain regions. However, the details of the underlying mechanisms are incompletely understood. The present study aims to examine the spreading of P301S aggregated tau, a mutation that is implicated in tauopathies, [...] Read more.
Tau pathology extends throughout the brain in a prion-like fashion through connected brain regions. However, the details of the underlying mechanisms are incompletely understood. The present study aims to examine the spreading of P301S aggregated tau, a mutation that is implicated in tauopathies, using organotypic slice cultures. Coronal hippocampal organotypic brain slices (170 µm) were prepared from postnatal (day 8–10) C57BL6 wild-type mice. Collagen hydrogels loaded with P301S aggregated tau were applied to slices and the spread of tau was assessed by immunohistochemistry after 8 weeks in culture. Collagen hydrogels prove to be an effective protein delivery system subject to natural degradation in 14 days and they release tau proteins up to 8 weeks. Slices with un- and hyperphosphorylated P301S aggregated tau demonstrate significant spreading to the ventral parts of the hippocampal slices compared to empty collagen hydrogels after 8 weeks. Moreover, the spread of P301S aggregated tau occurs in a time-dependent manner, which was interrupted when the neuroanatomical pathways are lesioned. We illustrate that the spreading of tau can be investigated in organotypic slice cultures using collagen hydrogels to achieve a localized application and slow release of tau proteins. P301S aggregated tau significantly spreads to the ventral areas of the slices, suggesting that the disease-relevant aggregated tau form possesses spreading potential. Thus, the results offer a novel experimental approach to investigate tau pathology. Full article
(This article belongs to the Special Issue Molecular and Cellular Basis of Alzheimer's Disease)
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20 pages, 19083 KiB  
Article
The Role of Cholesterol in Amyloidogenic Substrate Binding to the γ-Secretase Complex
by Urszula Orzeł, Jakub Jakowiecki, Krzysztof Młynarczyk and Sławomir Filipek
Biomolecules 2021, 11(7), 935; https://0-doi-org.brum.beds.ac.uk/10.3390/biom11070935 - 24 Jun 2021
Cited by 5 | Viewed by 2074
Abstract
Alzheimer’s disease is the most common progressive neurodegenerative disorder and is characterized by the presence of amyloid β (Aβ) plaques in the brain. The γ-secretase complex, which produces Aβ, is an intramembrane-cleaving protease consisting of four membrane proteins. In this paper we investigated [...] Read more.
Alzheimer’s disease is the most common progressive neurodegenerative disorder and is characterized by the presence of amyloid β (Aβ) plaques in the brain. The γ-secretase complex, which produces Aβ, is an intramembrane-cleaving protease consisting of four membrane proteins. In this paper we investigated the amyloidogenic fragments of amyloid precursor protein (substrates Aβ43 and Aβ45, leading to less amyloidogenic Aβ40 and more amyloidogenic Aβ42, respectively) docked to the binding site of presenilin, the catalytic subunit of γ-secretase. In total, we performed 9 μs of all-atom molecular dynamics simulations of the whole γ-secretase complex with both substrates in low (10%) and high (50%) concentrations of cholesterol in the membrane. We found that, at the high cholesterol level, the Aβ45 helix was statistically more flexible in the binding site of presenilin than Aβ43. An increase in the cholesterol concentration was also correlated with a higher flexibility of the Aβ45 helix, which suggests incompatibility between Aβ45 and the binding site of presenilin potentiated by a high cholesterol level. However, at the C-terminal part of Aβ45, the active site of presenilin was more compact in the case of a high cholesterol level, which could promote processing of this substrate. We also performed detailed mapping of the cholesterol binding sites at low and high cholesterol concentrations, which were independent of the typical cholesterol binding motifs. Full article
(This article belongs to the Special Issue Molecular and Cellular Basis of Alzheimer's Disease)
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