The pathological prion protein forms ionic conductance in lipid bilayer

Paulis, Daniele; Maras, Bruno; Schininà, Maria Eugenia; Francesco, Laura Di; Principe, Serena; Galeno, Roberta; Abdel‐Haq, Hanin; Cardone, Franco; Florio, Tullio; Pocchiari, Maurizio; Mazzanti, Michele

doi:10.1016/j.neuint.2011.04.008

Cited by 17 publications

(15 citation statements)

References 32 publications

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“…Several reports suggest a direct interaction between A␤ and the plasma membrane as one possible mechanism of toxicity (21,(42)(43)(44)(45). Electrophysiological experiments employed the Tip-Dip technique, which accurately studies single ion permeability in artificial lipid bilayers (21).…”

Section: Discussionmentioning

confidence: 99%

“…Electrophysiological experiments employed the Tip-Dip technique, which accurately studies single ion permeability in artificial lipid bilayers (21). The results showed that A␤ 1-42 solutions preincubated for 5 h (i.e., those containing 4G8-binding oligomers) had a much greater effect than freshly prepared solutions (monomers) or solutions preincubated for 24 h (lacking 4G8-binding oligomers).…”

Section: Discussionmentioning

confidence: 99%

“…Electrophysiological Assay-Single-channel recordings from lipid bilayer were obtained using the Tip-Dip method, as previously described (21). Experiments carried out using only ionic solutions and pure lipid bilayer do not show any ionic flow for more than 1 h of continuous current recordings (n ϭ 5).…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Specific Recognition of Biologically Active Amyloid-β Oligomers by a New Surface Plasmon Resonance-based Immunoassay and an in Vivo Assay in Caenorhabditis elegans

Stravalaci

Bastone

Beeg

et al. 2012

Journal of Biological Chemistry

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Background: A␤ oligomers are major players in Alzheimer disease, but the tools for their detection are not satisfactory. Results:We developed a SPR-based immunoassay and a test in C. elegans, specifically identifying toxic oligomers. Conclusion: These methods allow study of the effects of mutations or drugs on A␤ oligomerization. Significance: The SPR-based immunoassay provides new opportunities for the detection of toxic oligomers in biological samples.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Specific Recognition of Biologically Active Amyloid-β Oligomers by a New Surface Plasmon Resonance-based Immunoassay and an in Vivo Assay in Caenorhabditis elegans

Stravalaci

Bastone

Beeg

et al. 2012

Journal of Biological Chemistry

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“…Demuro et al reported that AβP, human amylin, prion and polyglutamine increased the elevation of [Ca 2+ ] i in a conformation-dependent manner [67]. Furthermore, a recombinant PrP protein (PrP90-231) formed channels through artificial lipid bilayers [68]. PrP has microbial activity similar to AβP [69].…”

Section: Molecular Mechanism Of the Neurotoxicity Induced By Prp106-126mentioning

confidence: 99%

Disruption of Metal Homeostasis and the Pathogenesis of Prion Diseases

Kawahara¹,

Tanaka²,

Mizuno³

2017

Prion - An Overview

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Prion diseases are progressive neurodegenerative diseases that are associated with the conformational conversion of normal cellular prion protein (PrP C ) into abnormal pathogenic prion protein (PrP Sc ). PrP C is a metal-binding protein that is located in the synapse and possesses the ability to bind to various metals, including Cu, Zn, Mn and Fe. Moreover, increasing evidence suggests that PrP C plays essential roles in the maintenance of metal homeostasis in the synapse. Trace elements have a crucial influence on the conformational change of PrP C . Given that other disease-related proteins such as β-amyloid protein and its precursor protein (APP) in Alzheimer's disease also exist in the synapse and possess a metal-binding ability, an interaction between PrP and metals and between PrP and APP, may occur in the synapse; the resulting metal homeostasis may lead to the pathogenesis of prion diseases. Here, we review our studies and other new findings that inform the current understanding of the link between trace elements and physiological functions of PrP C and the neurotoxicity of PrP Sc .

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“…By limited thermal denaturation (1 hr at 53 °C), hPrP90-231 was converted into a β-sheet rich, insoluble, aggregation-prone, hydrophobic peptide (all of these representing features identified in PrP Sc ) [34]. Moreover, in this conformation, but not in its native α-helix structure, hPrP90-231 induces cell death through caspase-dependent apoptosis, mimicking the effects of PrP Sc purified from infected Hamster brain [34,82,83]. …”

Section: Determinants Of Structural Misfolding Of Recombinant Prp mentioning

confidence: 99%

Role of Prion Protein Aggregation in Neurotoxicity

Corsaro

Thellung

Villa

et al. 2012

IJMS

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In several neurodegenerative diseases, such as Parkinson, Alzheimer’s, Huntington, and prion diseases, the deposition of aggregated misfolded proteins is believed to be responsible for the neurotoxicity that characterizes these diseases. Prion protein (PrP), the protein responsible of prion diseases, has been deeply studied for the peculiar feature of its misfolded oligomers that are able to propagate within affected brains, inducing the conversion of the natively folded PrP into the pathological conformation. In this review, we summarize the available experimental evidence concerning the relationship between aggregation status of misfolded PrP and neuronal death in the course of prion diseases. In particular, we describe the main findings resulting from the use of different synthetic (mainly PrP106-126) and recombinant PrP-derived peptides, as far as mechanisms of aggregation and amyloid formation, and how these different spatial conformations can affect neuronal death. In particular, most data support the involvement of non-fibrillar oligomers rather than actual amyloid fibers as the determinant of neuronal death.

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The pathological prion protein forms ionic conductance in lipid bilayer

Cited by 17 publications

References 32 publications

Specific Recognition of Biologically Active Amyloid-β Oligomers by a New Surface Plasmon Resonance-based Immunoassay and an in Vivo Assay in Caenorhabditis elegans

Specific Recognition of Biologically Active Amyloid-β Oligomers by a New Surface Plasmon Resonance-based Immunoassay and an in Vivo Assay in Caenorhabditis elegans

Disruption of Metal Homeostasis and the Pathogenesis of Prion Diseases

Role of Prion Protein Aggregation in Neurotoxicity

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