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

Celauro, Luigi; Burato, Anna; Zattoni, Marco; De Cecco, Elena; Fantuz, Marco; Cazzaniga, Federico Angelo; Bistaffa, Edoardo; Moda, Fabio; Legname, Giuseppe

doi:10.1016/j.jbc.2023.105054

Cited by 2 publications

(3 citation statements)

References 44 publications

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“…Immunoreacted sections demonstrated the presence of 3R and 4Rtau isoforms in pSer422-positive aggregates. These data demonstrate that, although PrP C can interact and transport intracellularly with different forms of tau [25] or [35], PrP C absence or presence in the extracellular space does not impair significantly the seeding properties of sAD. Lastly, the generated 3R or 4R pSer422tau deposits are of mouse origin and showed low spreading properties to contralateral neurons, being localized in ptau-positive neurons and a low number in oligodendrocytes in the cortical white matter.…”

Section: Resultsmentioning

confidence: 93%

“…Indeed, increasing PrP C levels by transfection in supraphysiological levels that normally do not occur in vivo , enhanced tau uptake in overexpressing cells (i.e. [25, 107]. In a previous study, we and others demonstrated that PrP C plays a relevant role in the propagation of sonicated α-synuclein fibrils.…”

Section: Discussionmentioning

confidence: 96%

“…In this respect, a recent study suggests the presence of shared putative neuronal receptors for tau, Ab, and a-synuclein [98]. In fact, among others, the low-density lipoprotein receptor-related protein 1 (LRP1) [1,104], the cellular prion protein (PrP C ) [26,35,79] or the lymphocyte-activation gene 3 (LAG3) [30] have been revealed as functional neuronal receptors of tau oligomers in some experimental models. PrP C is a cell surface GPI-anchored protein expressed in several tissues with especially high levels expressed by neurons and glial cells [2,21,83,93].…”

Section: Humanmentioning

confidence: 99%

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Involvement of the cellular prion protein in seeding and spreading of sarkosyl-derived fractions of Alzheimer’s disease inPrnpmutant mice and in the P301S transgenic tauopathy mice model

Sala-Jarque,

Gil,

Andrés-Benito

et al. 2024

Preprint

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The natural cellular prion protein is known to play several roles during development and adult brain. Far from its pathological roles in prionopathies, the non-pathogenic cellular prion protein has been described as a receptor for several amyloid in oligomeric and prefibrillar forms. For some amyloids, specific domains of the protein play a crucial role in modulating amyloid's cellular uptake and seeding properties. In most studies, the functions and the role of putative amyloid receptors have been analyzed by using brain extracts derived from human neurodegenerative patients. Another strategy has been to modify the genetic dosage of the natural prion protein in genetic models of different diseases. In this study, we take advantage of both approaches to examine whether this protein plays a role in the seeding and spreading of pathogenic tau. Our results point to a role of the natural prion protein in the emergence of pathogenic tau in a mouse model overexpressing the mutation P301S of the human tau gene. In contrast, its role is minor when sarkosyl-derived brain samples of Alzheimer's disease are used. In fact, our results indicate that the use of this type of sample is not adequate to determine the role of a putative receptor in tau seeding and spreading.

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Section: Resultsmentioning

confidence: 93%

Section: Discussionmentioning

confidence: 96%

Section: Humanmentioning

confidence: 99%

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Involvement of the cellular prion protein in seeding and spreading of sarkosyl-derived fractions of Alzheimer’s disease inPrnpmutant mice and in the P301S transgenic tauopathy mice model

Sala-Jarque,

Gil,

Andrés-Benito

et al. 2024

Preprint

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Comparing Prion Proteins Across Species: Is Zebrafish a Useful Model?

Burato,

Legname

2024

Mol Neurobiol

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Despite the considerable body of research dedicated to the field of neurodegeneration, the gap in knowledge on the prion protein and its intricate involvement in brain diseases remains substantial. However, in the past decades, many steps forward have been taken toward a better understanding of the molecular mechanisms underlying both the physiological role of the prion protein and the misfolding event converting it into its pathological counterpart, the prion. This review aims to provide an overview of the main findings regarding this protein, highlighting the advantages of many different animal models that share a conserved amino acid sequence and/or structure with the human prion protein. A particular focus will be given to the species Danio rerio, a compelling research organism for the investigation of prion biology, thanks to its conserved orthologs, ease of genetic manipulation, and cost-effectiveness of high-throughput experimentation. We will explore its potential in filling some of the gaps on physiological and pathological aspects of the prion protein, with the aim of directing the future development of therapeutic interventions.

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

Cited by 2 publications

References 44 publications

Involvement of the cellular prion protein in seeding and spreading of sarkosyl-derived fractions of Alzheimer’s disease inPrnpmutant mice and in the P301S transgenic tauopathy mice model

Involvement of the cellular prion protein in seeding and spreading of sarkosyl-derived fractions of Alzheimer’s disease inPrnpmutant mice and in the P301S transgenic tauopathy mice model

Comparing Prion Proteins Across Species: Is Zebrafish a Useful Model?

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