Serpin Signatures in Prion and Alzheimer's Diseases.

Acute-Phase Proteins Alzheimer Disease / pathology Animals Brain / metabolism Creutzfeldt-Jakob Syndrome / pathology Humans Mice Neurodegenerative Diseases / metabolism Prion Diseases / metabolism Prions / metabolism Serpins
Alzheimer’s disease Gene expression Prion diseases SERPINA3/SerpinA3n

Journal

Molecular neurobiology
ISSN: 1559-1182
Titre abrégé: Mol Neurobiol
Pays: United States
ID NLM: 8900963

Informations de publication

Date de publication:
Jun 2022
Historique:
received: 29 10 2021
accepted: 26 03 2022
pubmed: 14 4 2022
medline: 1 6 2022
entrez: 13 4 2022
Statut: ppublish

Résumé

Serpins represent the most broadly distributed superfamily of proteases inhibitors. They contribute to a variety of physiological functions and any alteration of the serpin-protease equilibrium can lead to severe consequences. SERPINA3 dysregulation has been associated with Alzheimer's disease (AD) and prion diseases. In this study, we investigated the differential expression of serpin superfamily members in neurodegenerative diseases. SERPIN expression was analyzed in human frontal cortex samples from cases of sporadic Creutzfeldt-Jakob disease (sCJD), patients at early stages of AD-related pathology, and age-matched controls not affected by neurodegenerative disorders. In addition, we studied whether Serpin expression was dysregulated in two animal models of prion disease and AD.Our analysis revealed that, besides the already observed upregulation of SERPINA3 in patients with prion disease and AD, SERPINB1, SERPINB6, SERPING1, SERPINH1, and SERPINI1 were dysregulated in sCJD individuals compared to controls, while only SERPINB1 was upregulated in AD patients. Furthermore, we analyzed whether other serpin members were differentially expressed in prion-infected mice compared to controls and, together with SerpinA3n, SerpinF2 increased levels were observed. Interestingly, SerpinA3n transcript and protein were upregulated in a mouse model of AD. The SERPINA3/SerpinA3nincreased anti-protease activity found in post-mortem brain tissue of AD and prion disease samples suggest its involvement in the neurodegenerative processes. A SERPINA3/SerpinA3n role in neurodegenerative disease-related protein aggregation was further corroborated by in vitro SerpinA3n-dependent prion accumulation changes. Our results indicate SERPINA3/SerpinA3n is a potential therapeutic target for the treatment of prion and prion-like neurodegenerative diseases.

Identifiants

DOI: 10.1007/s12035-022-02817-3 PMID: 35416570 PMC: PMC9148297
pubmed: 35416570
doi: 10.1007/s12035-022-02817-3
pii: 10.1007/s12035-022-02817-3
pmc: PMC9148297
doi:

Substances chimiques

Acute-Phase Proteins 0
Prions 0
SERPINA3 protein, human 0
Serpina3n protein, mouse 0
Serpins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

3778-3799

Informations de copyright

© 2022. The Author(s).

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Auteurs

Marco Zattoni (M)

Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore Di Studi Avanzati (SISSA), Trieste, Italy.

Marika Mearelli (M)

Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore Di Studi Avanzati (SISSA), Trieste, Italy.
German Center for Neurodegenerative Diseases (DZNE), 72076, Tübingen, Germany.

Silvia Vanni (S)

Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore Di Studi Avanzati (SISSA), Trieste, Italy.
Osteoncology Unit, Bioscience Laboratory, IRCCS Istituto Romagnolo Per Lo Studio Dei Tumori (IRST) "Dino Amadori", 47014, Meldola, Italy.

Arianna Colini Baldeschi (A)

Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore Di Studi Avanzati (SISSA), Trieste, Italy.
Institute of Biomedicine, Department of Pathology and Experimental Therapeutics, Bellvitge University Hospital-IDIBELL, Barcelona, Spain.

Thanh Hoa Tran (TH)

Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore Di Studi Avanzati (SISSA), Trieste, Italy.
VN-UK Institute for Research and Executive Education, The University of Danang, Da Nang, Vietnam.

Chiara Ferracin (C)

Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore Di Studi Avanzati (SISSA), Trieste, Italy.

Marcella Catania (M)

Division of Neurology 5 and Neuropathology, Fondazione IRCCS Istituto Neurologico Carlo Besta, Milan, Italy.

Fabio Moda (F)

Division of Neurology 5 and Neuropathology, Fondazione IRCCS Istituto Neurologico Carlo Besta, Milan, Italy.

Giuseppe Di Fede (G)

Division of Neurology 5 and Neuropathology, Fondazione IRCCS Istituto Neurologico Carlo Besta, Milan, Italy.

Giorgio Giaccone (G)

Division of Neurology 5 and Neuropathology, Fondazione IRCCS Istituto Neurologico Carlo Besta, Milan, Italy.

Fabrizio Tagliavini (F)

Scientific Directorate, Fondazione IRCCS Istituto Neurologico Carlo Besta, Milan, Italy.

Gianluigi Zanusso (G)

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

James W Ironside (JW)

National CJD Research & Surveillance Unit, Centre for Clinical Brain Sciences, University of Edinburgh, Edinburgh, UK.

Isidre Ferrer (I)

Department of Pathology and Experimental Therapeutics, University of Barcelona, Hospitalet de Llobregat, Spain.
Institute of Biomedical Research of Bellvitge (IDIBELL), Hospitalet de Llobregat, Spain.
Biomedical Research Network Center of Neurodegenerative Diseases (CIBERNED), Hospitalet de Llobregat, Spain.

Giuseppe Legname (G)

Laboratory of Prion Biology, Department of Neuroscience, Scuola Internazionale Superiore Di Studi Avanzati (SISSA), Trieste, Italy. legname@sissa.it.
ORCID: 0000-0003-0716-4393

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du sang › Protéine de la phase aigüe › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Troubles mentaux › Troubles neurocognitifs › Démence › Maladie d'Alzheimer › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Eucaryotes › Animaux › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Système nerveux › Système nerveux central › Encéphale › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Troubles mentaux › Troubles neurocognitifs › Démence › Maladie de Creutzfeldt-Jakob › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Maladies du système nerveux › Maladies neurodégénératives › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Maladies du système nerveux › Maladies neurodégénératives › Maladies à prions › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Prions › Serpin Signatures in Prion and Alzheimer's Diseases.
questionsmedicales.fr › Actions chimiques et utilisations › Actions pharmacologiques › Mécanismes moléculaires de l'action pharmacologique › Antienzymes › Inhibiteurs de protéases › Inhibiteurs de la sérine protéinase › Serpines › Serpin Signatures in Prion and Alzheimer's Diseases.