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Different tau fibril types reduce prion level in chronically and de novo infected cells.

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Title: Different tau fibril types reduce prion level in chronically and de novo infected cells.
Authors: Celauro, Luigi1, Burato, Anna1, Zattoni, Marco1,2, De Cecco, Elena1,3, Fantuz, Marco4,5, Cazzaniga, Federico Angelo6, Bistaffa, Edoardo6, Moda, Fabio6, Legname, Giuseppe1 legname@sissa.it
Source: Journal of Biological Chemistry. Aug2023, Vol. 299 Issue 8, p1-12. 12p.
Subjects: Prions, Tau proteins, Alzheimer's disease, Prion diseases, Tauopathies, Cell membranes, Alpha-synuclein
Abstract: Neurodegenerative diseases are often characterized by the codeposition of different amyloidogenic proteins, normally defining distinct proteinopathies. An example is represented by prion diseases, where the classical deposition of the aberrant conformational isoform of the prion protein (PrPSc) can be associated with tau insoluble species, which are usually involved in another class of diseases called tauopathies. How this copresence of amyloidogenic proteins can influence the progression of prion diseases is still a matter of debate. Recently, the cellular form of the prion protein, PrPC, has been investigated as a possible receptor of amyloidogenic proteins, since its binding activity with Aβ, tau, and α-synuclein has been reported, and it has been linked to several neurotoxic behaviors exerted by these proteins. We have previously shown that the treatment of chronically prion-infected cells with tau K18 fibrils reduced PrPSc levels. In this work, we further explored this mechanism by using another tau construct that includes the sequence that forms the core of Alzheimer’s disease tau filaments in vivo to obtain a distinct fibril type. Despite a difference of six amino acids, these two constructs form fibrils characterized by distinct biochemical and biological features. However, their effects on PrPSc reduction were comparable and probably based on the binding to PrPC at the plasma membrane, inhibiting the pathological conversion event. Our results suggest PrPC as receptor for different types of tau fibrils and point out a role of tau amyloid fibrils in preventing the pathological PrPC to PrPSc conformational change. [ABSTRACT FROM AUTHOR]
Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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DbLabel: Engineering Source
An: 170727009
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PubType: Academic Journal
PubTypeId: academicJournal
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  Data: Different tau fibril types reduce prion level in chronically and de novo infected cells.
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  Data: <searchLink fieldCode="AR" term="%22Celauro%2C+Luigi%22">Celauro, Luigi</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Burato%2C+Anna%22">Burato, Anna</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Zattoni%2C+Marco%22">Zattoni, Marco</searchLink><relatesTo>1,2</relatesTo><br /><searchLink fieldCode="AR" term="%22De+Cecco%2C+Elena%22">De Cecco, Elena</searchLink><relatesTo>1,3</relatesTo><br /><searchLink fieldCode="AR" term="%22Fantuz%2C+Marco%22">Fantuz, Marco</searchLink><relatesTo>4,5</relatesTo><br /><searchLink fieldCode="AR" term="%22Cazzaniga%2C+Federico+Angelo%22">Cazzaniga, Federico Angelo</searchLink><relatesTo>6</relatesTo><br /><searchLink fieldCode="AR" term="%22Bistaffa%2C+Edoardo%22">Bistaffa, Edoardo</searchLink><relatesTo>6</relatesTo><br /><searchLink fieldCode="AR" term="%22Moda%2C+Fabio%22">Moda, Fabio</searchLink><relatesTo>6</relatesTo><br /><searchLink fieldCode="AR" term="%22Legname%2C+Giuseppe%22">Legname, Giuseppe</searchLink><relatesTo>1</relatesTo><i> legname@sissa.it</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Biological+Chemistry%22">Journal of Biological Chemistry</searchLink>. Aug2023, Vol. 299 Issue 8, p1-12. 12p.
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  Data: <searchLink fieldCode="DE" term="%22Prions%22">Prions</searchLink><br /><searchLink fieldCode="DE" term="%22Tau+proteins%22">Tau proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Alzheimer's+disease%22">Alzheimer's disease</searchLink><br /><searchLink fieldCode="DE" term="%22Prion+diseases%22">Prion diseases</searchLink><br /><searchLink fieldCode="DE" term="%22Tauopathies%22">Tauopathies</searchLink><br /><searchLink fieldCode="DE" term="%22Cell+membranes%22">Cell membranes</searchLink><br /><searchLink fieldCode="DE" term="%22Alpha-synuclein%22">Alpha-synuclein</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: Neurodegenerative diseases are often characterized by the codeposition of different amyloidogenic proteins, normally defining distinct proteinopathies. An example is represented by prion diseases, where the classical deposition of the aberrant conformational isoform of the prion protein (PrPSc) can be associated with tau insoluble species, which are usually involved in another class of diseases called tauopathies. How this copresence of amyloidogenic proteins can influence the progression of prion diseases is still a matter of debate. Recently, the cellular form of the prion protein, PrPC, has been investigated as a possible receptor of amyloidogenic proteins, since its binding activity with Aβ, tau, and α-synuclein has been reported, and it has been linked to several neurotoxic behaviors exerted by these proteins. We have previously shown that the treatment of chronically prion-infected cells with tau K18 fibrils reduced PrPSc levels. In this work, we further explored this mechanism by using another tau construct that includes the sequence that forms the core of Alzheimer’s disease tau filaments in vivo to obtain a distinct fibril type. Despite a difference of six amino acids, these two constructs form fibrils characterized by distinct biochemical and biological features. However, their effects on PrPSc reduction were comparable and probably based on the binding to PrPC at the plasma membrane, inhibiting the pathological conversion event. Our results suggest PrPC as receptor for different types of tau fibrils and point out a role of tau amyloid fibrils in preventing the pathological PrPC to PrPSc conformational change. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Biological Chemistry is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1016/j.jbc.2023.105054
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 12
        StartPage: 1
    Subjects:
      – SubjectFull: Prions
        Type: general
      – SubjectFull: Tau proteins
        Type: general
      – SubjectFull: Alzheimer's disease
        Type: general
      – SubjectFull: Prion diseases
        Type: general
      – SubjectFull: Tauopathies
        Type: general
      – SubjectFull: Cell membranes
        Type: general
      – SubjectFull: Alpha-synuclein
        Type: general
    Titles:
      – TitleFull: Different tau fibril types reduce prion level in chronically and de novo infected cells.
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            – D: 01
              M: 08
              Text: Aug2023
              Type: published
              Y: 2023
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