Cellular Regulation of Pathological Proteins in Neurodegenerative Disease
A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cells of the Nervous System".
Deadline for manuscript submissions: 31 July 2024 | Viewed by 1964
Special Issue Editor
Special Issue Information
Dear Colleagues,
In some neurodegenerative diseases, the pathology is characterised by the presence of toxic proteins that accumulate in aggregates in the brain. The aggregates and/or oligomers appear to be toxic, causing injury or cell death. However, the role of these aggregates in disease is not fully understood. These pathological proteins are implicated in neurodegenerative diseases that trigger progressive degeneration through largely unknown pathogenic mechanisms, and lack valid therapeutic approaches. In this Special Issue, the focus will be on the cellular regulation of pathological proteins in neurodegenerative diseases such as Alzheimer's disease (AD), Huntington’s disease (HD), Parkinson's disease (PD), frontotemporal dementia (FTD), dementia with Lewy bodies (DLB), amyotrophic lateral sclerosis (ALS) and prion disease (PrD).
This Special Issue will highlight the current knowledge on the regulation of pathological aggregates that form in neurodegenerative diseases.
Dr. Sonia Sirisi
Guest Editor
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. Cells is an international peer-reviewed open access semimonthly 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.
Keywords
- protein aggregates
- neurodegeneration
- neurodegenerative diseases
- regulation pathways
- misfolded proteins
- toxic proteins
- homeostasis
- autophagy
Planned Papers
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Transcriptome wide correlations with neuropathological hallmarks in the frontal cortex of FTLD-TDP patients
Authors: Oriol Dols-Icardo, Sònia Sirisi Dolcet, Natalia Valle Tamayo, Victor Montal, Érika Sánchez-Aced, Laura Molina, Ignacio Illán-Gala, Jordi Pegueroles, Alba Cervantes-González, Olivia Belbin, Juan Fortea
Affiliation: Memory Unit. Neurology Department and Sant Pau Biomedical Research Institute, Hospital
de la Santa Creu i Sant Pau, Universitat Autonoma de Barcelona;
Network Center for Biomedical Research in Neurodegenerative Diseases (CIBERNED)
Title: Effect of ATP13A2-associated changes of extracellular vesicles on a-syn propagation in mouse brains
Authors: Taiji Tsunemi, Asako Yoroisaka, Dou Feng, Yuta Ishiguro, Nobutaka Hattori
Affiliation: Department of Neurology, Juntendo University School of Medicine
Abstract: Parkinson's disease (PD) is pathologically defined as the deposition of α-synuclein (α-syn) containing Lewy bodies (LBs) and Lewy neurites (LNs). Accumulating evidence suggests that α-syn may spread within the nervous system in a prion-like manner. Extracellular vesicles (EVs) may contribute to this pathway. We and others reported ATP13A2/PARK9-deficiency results in the reduction of EVs while its overexpression leads to increased EV generation. To analyze the effect of the EV-mediated a-syn secretion in neighboring neurons, we plan to examine the alternations of Atp13a2 levels on α-syn spreading in vivo. [Methods] At three months after inoculating mouse α-syn fibrils into the striatum of three Atp13a2 null and three wild-type mice, we stained the brain sections with anti-phosphorylated α-syn antibodies, and then quantified LBs/LNs in each brain regions. We also injected the lentivirus carrying human ATP13A2 two weeks before the inoculation to examine the effect of increased levels of ATP13A2. [Results] While LBs/LNs were formed in the entire brains, no significant difference was observed in LB/LN formation between Atp13a2-deficient and wild-type mice. Interestingly, overexpression of ATP13A2 leads to decreased LB/LN formation in entire brains. [Conclusion] These results combined with our previous studies suggest that enhanced secretory pathways by increased ATP13A2 levels attenuate the spreading of α-syn in brains, suggesting a protective role of ATP13A2 in α-synucleinopathies.
