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Biomolecules
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Prion Diseases: A Natural Model for Neurodegenerative Disorders
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Prion Diseases: A Natural Model for Neurodegenerative Disorders

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

Deadline for manuscript submissions: closed (31 January 2021) | Viewed by 23327

Special Issue Editor

Dr. Marta Monzón

E-Mail Website
Guest Editor
Human Anatomy and Histology, Faculty of Medicine / Research Centre for Encephalopathies and Transmissible Emerging Diseases - University of Zaragoza, Zaragoza, Spain
Interests: prion and prion-like diseases; neurodegeneration; neuroinflammation; astroglia; microglia; morphological studies by optical, confocal and electron microscopy

Special Issue Information

Current evidence supports the idea that many neurodegenerative diseases such as Alzheimer’s, Parkinson’s Huntington’s or amyotrophic lateral sclerosis, are considered prion-like disorders because they are all proteinopathies in which aberrant proteins spread throughout the brain during disease progression. All of them share molecular mechanisms of specific protein aggregation and spreading similar to those demonstrated for aberrant prion proteins, turning studies elucidating the mechanisms of prion propagation into useful tools for the study of other neurodegenerative diseases.

It would be relevant to emphasize the importance of studying brain material from naturally affected individuals to provide reliable results. As you know, it has become a common practice in Neurobiology to extrapolate from experimental studies to natural disorders. However, large differences between both models have been demonstrated. They probably constitute the likely reason why many conclusions drawn from experimental studies performed fail to reflect actual mechanisms of disease.

It is my great pleasure to invite you, as experts from any background or working field about neurodegenerative diseases to contribute to this special issue by original research or review articles.

Dr. Marta Monzón
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.

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Keywords

  • Neurodegenerative diseases
  • Prion and prion-like disorders
  • Natural model
  • Neuroinflammation
  • Neurodegeneration

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Published Papers (5 papers)

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Research

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20 pages, 3559 KiB  
Article
Medial Temporal Lobe Involvement in Human Prion Diseases: Implications for the Study of Focal Non Prion Neurodegenerative Pathology
by Alberto Rábano, Carmen Guerrero Márquez, Ramón A. Juste, María V. Geijo and Miguel Calero
Biomolecules 2021, 11(3), 413; https://doi.org/10.3390/biom11030413 - 10 Mar 2021
Cited by 2 | Viewed by 2832
Abstract
Human prion and non-prion neurodegenerative diseases share pathogenic mechanisms and neuropathological features. The lesion profile of a particular entity results from specific involvement of vulnerable neuron populations and connectivity circuits by a pathogenic protein isoform with strain-like properties. The lesion profile of the [...] Read more.
Human prion and non-prion neurodegenerative diseases share pathogenic mechanisms and neuropathological features. The lesion profile of a particular entity results from specific involvement of vulnerable neuron populations and connectivity circuits by a pathogenic protein isoform with strain-like properties. The lesion profile of the medial temporal lobe (MTL) was studied in postmortem tissue of 143 patients with human prion disease (HPD) including sporadic, genetic, and acquired forms. Most cases (90%) were classified according to PrPres type and/or PRNP codon 129 status, in addition to a full neuropathological profile. Mixed histotypes represented 29.4% of total sporadic Creutzfeldt-Jakob disease (sCJD) cases. An intensity score of involvement including spongiosis and astrogliosis was determined for the amygdala, presubiculum, subiculum, entorhinal cortex, CA1 to CA4 sectors of the hippocampal cortex, and dentate gyrus. Connectivity hubs within the MTL presented the highest scores. Diverse lesion profiles were obtained for different types and subtypes of HPD. Impact of mixed PrPres types on the MTL lesion profile was higher for sCJDMV2K cases than in other histotypes. Differences between MTL profiles was globally consistent with current evidence on specific strains in HPD. These results may be relevant for the analysis of possible strain effects in focal non-prion neurodegenerative conditions limited to the MTL. Full article
(This article belongs to the Special Issue Prion Diseases: A Natural Model for Neurodegenerative Disorders)
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18 pages, 30287 KiB  
Article
Neuroimmune Response Mediated by Cytokines in Natural Scrapie after Chronic Dexamethasone Treatment
by Isabel M. Guijarro, Moisés Garcés, Pol Andrés-Benito, Belén Marín, Alicia Otero, Tomás Barrio, Margarita Carmona, Isidro Ferrer, Juan J. Badiola and Marta Monzón
Biomolecules 2021, 11(2), 204; https://doi.org/10.3390/biom11020204 - 2 Feb 2021
Cited by 5 | Viewed by 2292
Abstract
The actual role of prion protein-induced glial activation and subsequent cytokine secretion during prion diseases is still incompletely understood. The overall aim of this study is to assess the effect of an anti-inflammatory treatment with dexamethasone on different cytokines released by neuroglial cells [...] Read more.
The actual role of prion protein-induced glial activation and subsequent cytokine secretion during prion diseases is still incompletely understood. The overall aim of this study is to assess the effect of an anti-inflammatory treatment with dexamethasone on different cytokines released by neuroglial cells that are potentially related to neuroinflammation in natural scrapie. This study emphasizes the complex interactions existent among several pleiotropic neuromodulator peptides and provides a global approach to clarify neuroinflammatory processes in prion diseases. Additionally, an impairment of communication between microglial and astroglial populations mediated by cytokines, mainly IL-1, is suggested. The main novelty of this study is that it is the first one assessing in situ neuroinflammatory activity in relation to chronic anti-inflammatory therapy, gaining relevance because it is based on a natural model. The cytokine profile data would suggest the activation of some neurotoxicity-associated route. Consequently, targeting such a pathway might be a new approach to modify the damaging effects of neuroinflammation. Full article
(This article belongs to the Special Issue Prion Diseases: A Natural Model for Neurodegenerative Disorders)
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Review

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24 pages, 8902 KiB  
Review
Reflections on Cerebellar Neuropathology in Classical Scrapie
by Adolfo Toledano-Díaz, María Isabel Álvarez, Jose-Julio Rodríguez, Juan Jose Badiola, Marta Monzón and Adolfo Toledano
Biomolecules 2021, 11(5), 649; https://doi.org/10.3390/biom11050649 - 28 Apr 2021
Cited by 2 | Viewed by 3099
Abstract
In this review, the most important neuropathological changes found in the cerebella of sheep affected by classical natural scrapie are discussed. This disease is the oldest known of a group of unconventional “infections” caused by toxic prions of different origins. Scrapie is currently [...] Read more.
In this review, the most important neuropathological changes found in the cerebella of sheep affected by classical natural scrapie are discussed. This disease is the oldest known of a group of unconventional “infections” caused by toxic prions of different origins. Scrapie is currently considered a “transmissible spongiform encephalopathy” (due to its neuropathological characteristics and its transmission), which is the paradigm of prion pathologies as well as many encephalopathies (prion-like) that present aberrant deposits of insoluble protein with neurotoxic effects due to errors in their catabolization (“misfolding protein diseases”). The study of this disease is, therefore, of great relevance. Our work data from the authors’ previous publications as well as other research in the field. The four most important types of neuropathological changes are neuron abnormalities and loss, neurogliosis, tissue vacuolization (spongiosis) and pathological or abnormal prion protein (PrP) deposits/deposition. These findings were analyzed and compared to other neuropathologies. Various aspects related to the presentation and progression of the disease, the involution of different neuronal types, the neuroglial responses and the appearance of abnormal PrP deposits are discussed. The most important points of controversy in scrapie neuropathology are presented. Full article
(This article belongs to the Special Issue Prion Diseases: A Natural Model for Neurodegenerative Disorders)
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29 pages, 12461 KiB  
Review
Neuropathology of Animal Prion Diseases
by Leonor Orge, Carla Lima, Carla Machado, Paula Tavares, Paula Mendonça, Paulo Carvalho, João Silva, Maria de Lurdes Pinto, Estela Bastos, Jorge Cláudio Pereira, Nuno Gonçalves-Anjo, Adelina Gama, Alexandra Esteves, Anabela Alves, Ana Cristina Matos, Fernanda Seixas, Filipe Silva, Isabel Pires, Luis Figueira, Madalena Vieira-Pinto, Roberto Sargo and Maria dos Anjos Piresadd Show full author list remove Hide full author list
Biomolecules 2021, 11(3), 466; https://doi.org/10.3390/biom11030466 - 21 Mar 2021
Cited by 24 | Viewed by 7262
Abstract
Transmissible Spongiform Encephalopathies (TSEs) or prion diseases are a fatal group of infectious, inherited and spontaneous neurodegenerative diseases affecting human and animals. They are caused by the conversion of cellular prion protein (PrPC) into a misfolded pathological isoform (PrPSc or [...] Read more.
Transmissible Spongiform Encephalopathies (TSEs) or prion diseases are a fatal group of infectious, inherited and spontaneous neurodegenerative diseases affecting human and animals. They are caused by the conversion of cellular prion protein (PrPC) into a misfolded pathological isoform (PrPSc or prion- proteinaceous infectious particle) that self-propagates by conformational conversion of PrPC. Yet by an unknown mechanism, PrPC can fold into different PrPSc conformers that may result in different prion strains that display specific disease phenotype (incubation time, clinical signs and lesion profile). Although the pathways for neurodegeneration as well as the involvement of brain inflammation in these diseases are not well understood, the spongiform changes, neuronal loss, gliosis and accumulation of PrPSc are the characteristic neuropathological lesions. Scrapie affecting small ruminants was the first identified TSE and has been considered the archetype of prion diseases, though atypical and new animal prion diseases continue to emerge highlighting the importance to investigate the lesion profile in naturally affected animals. In this report, we review the neuropathology and the neuroinflammation of animal prion diseases in natural hosts from scrapie, going through the zoonotic bovine spongiform encephalopathy (BSE), the chronic wasting disease (CWD) to the newly identified camel prion disease (CPD). Full article
(This article belongs to the Special Issue Prion Diseases: A Natural Model for Neurodegenerative Disorders)
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23 pages, 1320 KiB  
Review
Prion Diseases: A Unique Transmissible Agent or a Model for Neurodegenerative Diseases?
by Diane L. Ritchie and Marcelo A. Barria
Biomolecules 2021, 11(2), 207; https://doi.org/10.3390/biom11020207 - 2 Feb 2021
Cited by 17 | Viewed by 6738
Abstract
The accumulation and propagation in the brain of misfolded proteins is a pathological hallmark shared by many neurodegenerative diseases such as Alzheimer’s disease (Aβ and tau), Parkinson’s disease (α-synuclein), and prion disease (prion protein). Currently, there is no epidemiological evidence to suggest that [...] Read more.
The accumulation and propagation in the brain of misfolded proteins is a pathological hallmark shared by many neurodegenerative diseases such as Alzheimer’s disease (Aβ and tau), Parkinson’s disease (α-synuclein), and prion disease (prion protein). Currently, there is no epidemiological evidence to suggest that neurodegenerative disorders are infectious, apart from prion diseases. However, there is an increasing body of evidence from experimental models to suggest that other pathogenic proteins such as Aβ and tau can propagate in vivo and in vitro in a prion-like mechanism, inducing the formation of misfolded protein aggregates such as amyloid plaques and neurofibrillary tangles. Such similarities have raised concerns that misfolded proteins, other than the prion protein, could potentially transmit from person-to-person as rare events after lengthy incubation periods. Such concerns have been heightened following a number of recent reports of the possible inadvertent transmission of Aβ pathology via medical and surgical procedures. This review will provide a historical perspective on the unique transmissible nature of prion diseases, examining their impact on public health and the ongoing concerns raised by this rare group of disorders. Additionally, this review will provide an insight into current evidence supporting the potential transmissibility of other pathogenic proteins associated with more common neurodegenerative disorders and the potential implications for public health. Full article
(This article belongs to the Special Issue Prion Diseases: A Natural Model for Neurodegenerative Disorders)
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