Neurodegeneration-Associated Proteins in Human Olfactory Neurons Collected by Nasal Brushing.

misfolded proteins neurodegenerative diseases olfactory brushing olfactory neuroepithelium olfactory neurons

Journal

Frontiers in neuroscience
ISSN: 1662-4548
Titre abrégé: Front Neurosci
Pays: Switzerland
ID NLM: 101478481

Informations de publication

Date de publication:
2020
Historique:
received: 15 11 2019
accepted: 05 02 2020
entrez: 21 3 2020
pubmed: 21 3 2020
medline: 21 3 2020
Statut: epublish

Résumé

The olfactory neuroepithelium is located in the upper vault of the nasal cavity, lying on the olfactory cleft and projecting into the dorsal portion of the superior and middle turbinates beyond the mid-portion of the nasal septum. It is composed of a variety of cell types including olfactory sensory neurons, supporting glial-like cells, microvillar cells, and basal stem cells. The cells of the neuroepithelium are often intermingled with respiratory and metaplastic epithelial cells. Olfactory neurons undergo a constant self-renewal in the timespan of 2-3 months; they are directly exposed to the external environment, and thus they are vulnerable to physical and chemical injuries. The latter might induce metabolic perturbations and ultimately be the cause of cell death. However, the lifespan of olfactory neurons is biologically programmed, and for this reason, these cells have an accelerated metabolic cycle leading to an irreversible apoptosis. These characteristics make these cells suitable for research related to nerve cell degeneration and aging. Recent studies have shown that a non-invasive and painless olfactory brushing procedure allows an efficient sampling from the olfactory neuroepithelium. This approach allows to detect the pathologic prion protein in patients with sporadic Creutzfeldt-Jakob disease, using the real-time quaking-induced conversion assay. Investigating the expression of all the proteins associated to neurodegeneration in the cells of the olfactory mucosa is a novel approach toward understanding the pathogenesis of human neurodegenerative diseases. Our aim was to investigate the expression of α-synuclein, β-amyloid, tau, and TDP-43 in the olfactory neurons of normal subjects. We showed that these proteins that are involved in neurodegenerative diseases are expressed in olfactory neurons. These findings raise the question on whether a relationship exists between the mechanisms of protein aggregation that occur in the olfactory bulb during the early stage of the neurodegenerative process and the protein misfolding occurring in the olfactory neuroepithelium.

Identifiants

pubmed: 32194369
doi: 10.3389/fnins.2020.00145
pmc: PMC7066258
doi:

Types de publication

Journal Article

Langues

eng

Pagination

145

Subventions

Organisme : NIA NIH HHS
ID : P30 AG010133
Pays : United States

Informations de copyright

Copyright © 2020 Brozzetti, Sacchetto, Cecchini, Avesani, Perra, Bongianni, Portioli, Scupoli, Ghetti, Monaco, Buffelli and Zanusso.

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Auteurs

Lorenzo Brozzetti (L)

Neuropathology Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Luca Sacchetto (L)

Otolaryngology Section, Department of Surgery, Dentistry, Paediatrics and Gynaecology, University of Verona, Verona, Italy.

Maria Paola Cecchini (MP)

Anatomy and Histology Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Anna Avesani (A)

Physiology Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Daniela Perra (D)

Neuropathology Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Matilde Bongianni (M)

Neuropathology Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Corinne Portioli (C)

Anatomy and Histology Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Maria Scupoli (M)

Biology and Genetics Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Bernardino Ghetti (B)

Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, United States.

Salvatore Monaco (S)

Neuropathology Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Mario Buffelli (M)

Physiology Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Gianluigi Zanusso (G)

Neuropathology Section, Department of Neurosciences, Biomedicine, and Movement Sciences, University of Verona, Verona, Italy.

Classifications MeSH