Protein Misfolding Diseases: From Experimental Approaches to Therapeutic Opportunities

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cellular Pathology".

Deadline for manuscript submissions: 31 July 2024 | Viewed by 2458

Special Issue Editors

Premedical Division, Weill Cornell Medicine-Qatar, Education City, Qatar
Interests: amyloid protein; neurodegenerative diseases; type 2 diabetes; biophysics

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Guest Editor
Department of Experimental Neurodegeneration, University Medical Center Göttingen, Göttingen, Germany
Interests: neurodegeneration; Parkinson’s disease; Alzheimer’s disease; protein aggregation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein misfolding and amyloid formation are the pathognomonic modalities behind the most globally prevalent neurodegenerative diseases, including Alzheimer’s disease and Parkinson’s disease. With the worldwide prevalence of dementia, a common pathological consequence of these neurodegenerative diseases that is expected to almost triple in less than thirty years, they pose significant challenges to healthcare systems worldwide. Strikingly, protein aggregation seems to also be an important hallmark in other highly prevalent diseases, such as cancer and diabetes, suggesting that shared mechanisms may be involved.

This Special Issue welcomes review articles and original reports that will improve our understanding of the mechanisms involved in protein misfolding diseases. A deeper understanding of these mechanisms, and the cross-fertilization between different fields will create opportunities for developing novel diagnostics and treatment modalities for many devastating diseases.

Dr. Ali Chaari
Prof. Dr. Tiago Fleming Outeiro
Guest Editors

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Keywords

  • protein aggregation
  • amyloid
  • neurodegenerative diseases
  • cancer
  • diabetes

Published Papers (1 paper)

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Research

14 pages, 1823 KiB  
Article
The Protein Network in Subcutaneous Fat Biopsies from Patients with AL Amyloidosis: More Than Diagnosis?
by Dario Di Silvestre, Francesca Brambilla, Francesca Lavatelli, Maila Chirivì, Diana Canetti, Claudia Bearzi, Roberto Rizzi, Johan Bijzet, Bouke P. C. Hazenberg, Vittorio Bellotti, Julian D. Gillmore and Pierluigi Mauri
Cells 2023, 12(5), 699; https://doi.org/10.3390/cells12050699 - 22 Feb 2023
Cited by 1 | Viewed by 1712
Abstract
AL amyloidosis is caused by the misfolding of immunoglobulin light chains leading to an impaired function of tissues and organs in which they accumulate. Due to the paucity of -omics profiles from undissected samples, few studies have addressed amyloid-related damage system wide. To [...] Read more.
AL amyloidosis is caused by the misfolding of immunoglobulin light chains leading to an impaired function of tissues and organs in which they accumulate. Due to the paucity of -omics profiles from undissected samples, few studies have addressed amyloid-related damage system wide. To fill this gap, we evaluated proteome changes in the abdominal subcutaneous adipose tissue of patients affected by the AL isotypes κ and λ. Through our retrospective analysis based on graph theory, we have herein deduced new insights representing a step forward from the pioneering proteomic investigations previously published by our group. ECM/cytoskeleton, oxidative stress and proteostasis were confirmed as leading processes. In this scenario, some proteins, including glutathione peroxidase 1 (GPX1), tubulins and the TRiC complex, were classified as biologically and topologically relevant. These and other results overlap with those already reported for other amyloidoses, supporting the hypothesis that amyloidogenic proteins could induce similar mechanisms independently of the main fibril precursor and of the target tissues/organs. Of course, further studies based on larger patient cohorts and different tissues/organs will be essential, which would be a key point that would allow for a more robust selection of the main molecular players and a more accurate correlation with clinical aspects. Full article
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