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Tracking Back Proteotoxicity in Neurodegenerative Diseases

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Toxicology".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 4503

Special Issue Editors


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Guest Editor
1. School of Medicine and Surgery, Milan Center for Neuroscience (NeuroMI), University of Milano-Bicocca, Monza (MB), Italy
2. Departmentof Neurology, San Gerardo Hospital, Monza (MB), Italy
Interests: neurodegenerative diseases; amyotrophic lateral sclerosis; dementia, oxidative stress; excitotoxicity; peripheral cells; biomarkers
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Guest Editor
Milan Center for Neuroscience (NeuroMI), University of Milano-Bicocca, Milan, Italy
Interests: study of pathogenic mechanisms (proteotoxicity, autophagy dysfunctions, oxidative stress, excitotoxicity) and discovery of biomarkers in neurodegenerative diseases using ex vivo peripheral cells from patients and in vitro disease models
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Many neurodegenerative diseases including Parkinson’s disease (PD), Alzheimer’s disease (AD), and amyotrophic lateral sclerosis (ALS) belong to the large category of proteinopathies, conditions characterized by the presence of proteinaceous inclusions within and/or outside the degenerating neurons. The identification of such aggregates supports the view that misfolded proteins represent a basic requirement for the neurodegenerative process and provides input to verify the existence of possible dysfunctions of the biological systems influencing protein homeostasis.

In neurodegenerative diseases, both environmental and genetic factors contribute to altering the physiological processes involved in the synthesis of disease-specific proteins, resulting in a protein overproduction or in the generation of post-translationally modified protein forms more prone to aggregation. Furthermore, the impairment of intracellular protein catabolic systems plays a crucial role in proteotoxicity, and the prion-like spreading of pathological proteins further amplifies neuronal damage.

A better comprehension of the molecular mechanisms responsible for proteotoxicity in neurodegenerative diseases can allow the identification of both new therapeutic targets and useful biomarkers for these devastating disorders.

Prof. Dr. Lucio Tremolizzo
Dr. Gessica Sala
Guest Editors

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Keywords

  • Parkinson’s disease
  • amyotrophic lateral sclerosis
  • Alzheimer’s disease
  • neurodegenerative diseases
  • alpha-synuclein
  • TDP-43
  • beta-amyloid
  • tau
  • genetics
  • catabolism
  • proteotoxicity

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Published Papers (1 paper)

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Review

17 pages, 986 KiB  
Review
FKBP52 in Neuronal Signaling and Neurodegenerative Diseases: A Microtubule Story
by Béatrice Chambraud, Cillian Byrne, Geri Meduri, Etienne Emile Baulieu and Julien Giustiniani
Int. J. Mol. Sci. 2022, 23(3), 1738; https://doi.org/10.3390/ijms23031738 - 3 Feb 2022
Cited by 8 | Viewed by 3478
Abstract
The FK506-binding protein 52 (FKBP52) belongs to a large family of ubiquitously expressed and highly conserved proteins (FKBPs) that share an FKBP domain and possess Peptidyl-Prolyl Isomerase (PPIase) activity. PPIase activity catalyzes the isomerization of Peptidyl-Prolyl bonds and therefore influences target protein folding [...] Read more.
The FK506-binding protein 52 (FKBP52) belongs to a large family of ubiquitously expressed and highly conserved proteins (FKBPs) that share an FKBP domain and possess Peptidyl-Prolyl Isomerase (PPIase) activity. PPIase activity catalyzes the isomerization of Peptidyl-Prolyl bonds and therefore influences target protein folding and function. FKBP52 is particularly abundant in the nervous system and is partially associated with the microtubule network in different cell types suggesting its implication in microtubule function. Various studies have focused on FKBP52, highlighting its importance in several neuronal microtubule-dependent signaling pathways and its possible implication in neurodegenerative diseases such as tauopathies (i.e., Alzheimer disease) and alpha-synucleinopathies (i.e., Parkinson disease). This review summarizes our current understanding of FKBP52 actions in the microtubule environment, its implication in neuronal signaling and function, its interactions with other members of the FKBPs family and its involvement in neurodegenerative disease. Full article
(This article belongs to the Special Issue Tracking Back Proteotoxicity in Neurodegenerative Diseases)
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