19 results on '"Biggi, Silvia"'
Search Results
2. Pharmacological inactivation of the prion protein by targeting a folding intermediate
- Author
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Spagnolli, Giovanni, Massignan, Tania, Astolfi, Andrea, Biggi, Silvia, Rigoli, Marta, Brunelli, Paolo, Libergoli, Michela, Ianeselli, Alan, Orioli, Simone, Boldrini, Alberto, Terruzzi, Luca, Bonaldo, Valerio, Maietta, Giulia, Lorenzo, Nuria L., Fernandez, Leticia C., Codeseira, Yaiza B., Tosatto, Laura, Linsenmeier, Luise, Vignoli, Beatrice, Petris, Gianluca, Gasparotto, Dino, Pennuto, Maria, Guella, Graziano, Canossa, Marco, Altmeppen, Hermann C., Lolli, Graziano, Biressi, Stefano, Pastor, Manuel M., Requena, Jesús R., Mancini, Ines, Barreca, Maria L., Faccioli, Pietro, and Biasini, Emiliano more...
- Published
- 2021
- Full Text
- View/download PDF
Catalog
3. Neuroprotection by MKK7 inhibition in excitotoxicity
- Author
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Vercelli, Alessandro, Borsello, Tiziana, Sclip, Alessandra, Biggi, Silvia, Repetto, Ivan Enrico, Cimini, Sara, Falleroni, Fabio, Tomasi, Simone, Monti, Riccardo, Tonna, Noemi, Morelli, Federica, Grande, Valentina, Marin, Oriano, Bianco, Fabio, and di Marino, Daniele more...
- Published
- 2015
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4. Pharmacological inactivation of the prion protein by targeting a folding intermediate
- Author
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Universidade de Santiago de Compostela. Centro de Investigación en Medicina Molecular e Enfermidades Crónicas, Universidade de Santiago de Compostela. Departamento de Psiquiatría, Radioloxía, Saúde Pública, Enfermaría e Medicina, Spagnolli, Giovanni, Massignan, Tania, Astolfi, Andrea, Biggi, Silvia, Rigoli, Marta, Brunelli, Paolo, Libergoli, Michela, Ianeselli, Alan, Orioli, Simone, Boldrini, Alberto, Terruzzi, Luca, Bonaldo, Valerio, Maietta, Giulia, López Lorenzo, Nuria, Fernández Flores, Leticia Camila, Bugallo Codeseira, Yaiza, Tosatto, Laura, Linsenmeier, Luise, Vignoli, Beatrice, Petris, Gianluca, Gasparotto, Dino, Pennuto, Maria, Guella, Graziano, Canossa, Marco, Altmeppen, Hermann C., Lolli, Graziano, Biressi, Stefano, Martín Pastor, Manuel, Rodríguez Requena, Jesús, Mancini, Ines, Barreca, Maria L., Faccioli, Pietro, Biasini, Emiliano, Universidade de Santiago de Compostela. Centro de Investigación en Medicina Molecular e Enfermidades Crónicas, Universidade de Santiago de Compostela. Departamento de Psiquiatría, Radioloxía, Saúde Pública, Enfermaría e Medicina, Spagnolli, Giovanni, Massignan, Tania, Astolfi, Andrea, Biggi, Silvia, Rigoli, Marta, Brunelli, Paolo, Libergoli, Michela, Ianeselli, Alan, Orioli, Simone, Boldrini, Alberto, Terruzzi, Luca, Bonaldo, Valerio, Maietta, Giulia, López Lorenzo, Nuria, Fernández Flores, Leticia Camila, Bugallo Codeseira, Yaiza, Tosatto, Laura, Linsenmeier, Luise, Vignoli, Beatrice, Petris, Gianluca, Gasparotto, Dino, Pennuto, Maria, Guella, Graziano, Canossa, Marco, Altmeppen, Hermann C., Lolli, Graziano, Biressi, Stefano, Martín Pastor, Manuel, Rodríguez Requena, Jesús, Mancini, Ines, Barreca, Maria L., Faccioli, Pietro, and Biasini, Emiliano more...
- Abstract
Recent computational advancements in the simulation of biochemical processes allow investigating the mechanisms involved in protein regulation with realistic physics-based models, at an atomistic level of resolution. These techniques allowed us to design a drug discovery approach, named Pharmacological Protein Inactivation by Folding Intermediate Targeting (PPI-FIT), based on the rationale of negatively regulating protein levels by targeting folding intermediates. Here, PPI-FIT was tested for the first time on the cellular prion protein (PrP), a cell surface glycoprotein playing a key role in fatal and transmissible neurodegenerative pathologies known as prion diseases. We predicted the all-atom structure of an intermediate appearing along the folding pathway of PrP and identified four different small molecule ligands for this conformer, all capable of selectively lowering the load of the protein by promoting its degradation. Our data support the notion that the level of target proteins could be modulated by acting on their folding pathways, implying a previously unappreciated role for folding intermediates in the biological regulation of protein expression more...
- Published
- 2021
5. Pharmacological inactivation of the prion protein by targeting a folding intermediate
- Author
-
Spagnolli, G, Massignan, T, Astolfi, A, Biggi, S, Rigoli, M, Brunelli, P, Libergoli, M, Ianeselli, A, Orioli, S, Boldrini, A, Terruzzi, L, Bonaldo, V, Maietta, G, Lorenzo, N, Fernandez, L, Codeseira, Y, Tosatto, L, Linsenmeier, L, Vignoli, B, Petris, G, Gasparotto, D, Pennuto, M, Guella, G, Canossa, M, Altmeppen, H, Lolli, G, Biressi, S, Pastor, M, Requena, J, Mancini, I, Barreca, M, Faccioli, P, Biasini, E, Spagnolli, Giovanni, Massignan, Tania, Astolfi, Andrea, Biggi, Silvia, Rigoli, Marta, Brunelli, Paolo, Libergoli, Michela, Ianeselli, Alan, Orioli, Simone, Boldrini, Alberto, Terruzzi, Luca, Bonaldo, Valerio, Maietta, Giulia, Lorenzo, Nuria L, Fernandez, Leticia C, Codeseira, Yaiza B, Tosatto, Laura, Linsenmeier, Luise, Vignoli, Beatrice, Petris, Gianluca, Gasparotto, Dino, Pennuto, Maria, Guella, Graziano, Canossa, Marco, Altmeppen, Hermann C, Lolli, Graziano, Biressi, Stefano, Pastor, Manuel M, Requena, Jesús R, Mancini, Ines, Barreca, Maria L, Faccioli, Pietro, Biasini, Emiliano, Spagnolli, G, Massignan, T, Astolfi, A, Biggi, S, Rigoli, M, Brunelli, P, Libergoli, M, Ianeselli, A, Orioli, S, Boldrini, A, Terruzzi, L, Bonaldo, V, Maietta, G, Lorenzo, N, Fernandez, L, Codeseira, Y, Tosatto, L, Linsenmeier, L, Vignoli, B, Petris, G, Gasparotto, D, Pennuto, M, Guella, G, Canossa, M, Altmeppen, H, Lolli, G, Biressi, S, Pastor, M, Requena, J, Mancini, I, Barreca, M, Faccioli, P, Biasini, E, Spagnolli, Giovanni, Massignan, Tania, Astolfi, Andrea, Biggi, Silvia, Rigoli, Marta, Brunelli, Paolo, Libergoli, Michela, Ianeselli, Alan, Orioli, Simone, Boldrini, Alberto, Terruzzi, Luca, Bonaldo, Valerio, Maietta, Giulia, Lorenzo, Nuria L, Fernandez, Leticia C, Codeseira, Yaiza B, Tosatto, Laura, Linsenmeier, Luise, Vignoli, Beatrice, Petris, Gianluca, Gasparotto, Dino, Pennuto, Maria, Guella, Graziano, Canossa, Marco, Altmeppen, Hermann C, Lolli, Graziano, Biressi, Stefano, Pastor, Manuel M, Requena, Jesús R, Mancini, Ines, Barreca, Maria L, Faccioli, Pietro, and Biasini, Emiliano more...
- Abstract
Recent computational advancements in the simulation of biochemical processes allow investigating the mechanisms involved in protein regulation with realistic physics-based models, at an atomistic level of resolution. These techniques allowed us to design a drug discovery approach, named Pharmacological Protein Inactivation by Folding Intermediate Targeting (PPI-FIT), based on the rationale of negatively regulating protein levels by targeting folding intermediates. Here, PPI-FIT was tested for the first time on the cellular prion protein (PrP), a cell surface glycoprotein playing a key role in fatal and transmissible neurodegenerative pathologies known as prion diseases. We predicted the all-atom structure of an intermediate appearing along the folding pathway of PrP and identified four different small molecule ligands for this conformer, all capable of selectively lowering the load of the protein by promoting its degradation. Our data support the notion that the level of target proteins could be modulated by acting on their folding pathways, implying a previously unappreciated role for folding intermediates in the biological regulation of protein expression. more...
- Published
- 2021
6. Characterization of Physical, Mechanical, and Biological Properties of SilkBridge Nerve Conduit after Enzymatic Hydrolysis
- Author
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Biggi, Silvia, primary, Bassani, Giulia A., additional, Vincoli, Valentina, additional, Peroni, Daniele, additional, Bonaldo, Valerio, additional, Biagiotti, Marco, additional, Belli, Romina, additional, Alessandrino, Antonio, additional, Biasini, Emiliano, additional, and Freddi, Giuliano, additional more...
- Published
- 2020
- Full Text
- View/download PDF
7. PHARMACOLOGICAL PROTEIN INACTIVATION BY TARGETING FOLDING INTERMEDIATES
- Author
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Spagnolli, Giovanni, primary, Massignan, Tania, additional, Astolfi, Andrea, additional, Biggi, Silvia, additional, Brunelli, Paolo, additional, Libergoli, Michela, additional, Ianeselli, Alan, additional, Orioli, Simone, additional, Boldrini, Alberto, additional, Terruzzi, Luca, additional, Maietta, Giulia, additional, Rigoli, Marta, additional, Lorenzo, Nuria Lopez, additional, Fernandez, Leticia C., additional, Tosatto, Laura, additional, Linsenmeier, Luise, additional, Vignoli, Beatrice, additional, Petris, Gianluca, additional, Gasparotto, Dino, additional, Pennuto, Maria, additional, Guella, Graziano, additional, Canossa, Marco, additional, Altmeppen, Hermann Clemens, additional, Lolli, Graziano, additional, Biressi, Stefano, additional, Pastor, Manuel Martin, additional, Requena, Jesús R., additional, Mancini, Ines, additional, Barreca, Maria Letizia, additional, Faccioli, Pietro, additional, and Biasini, Emiliano, additional more...
- Published
- 2020
- Full Text
- View/download PDF
8. Tackling Prion Replication and Toxicity by Targeting the Cellular Prion Protein with Different Pharmacological Strategies
- Author
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Biggi, Silvia
- Subjects
animal diseases ,nervous system diseases - Abstract
The great majority of therapeutic strategies tested so far for prion diseases, fatal transmissible neurodegenerative disorders, tackled PrPSc, the infectious isoform of the cellular prion protein (PrPC), with largely unsuccessful results. Conversely, targeting PrPC is a poorly explored strategy. In this thesis, I exploited the concepts of altering PrPC cell surface localization and tackling PrPC-mediated cytotoxicity to design two different screening paradigms and study the effect of novel anti-prion compounds. We recently shed light on the mode of action of chlorpromazine, an anti-psychotic drug known to inhibit prion replication and toxicity by inducing the re-localization of PrPC from the plasma membrane. Unfortunately, chlorpromazine possesses pharmacokinetic properties unsuitable for chronic use in vivo, namely low specificity and high toxicity. In the first part of my thesis, I employed cells expressing EGFP-PrP to carry out a semi-automated high content screening (HCS) of a chemical library directed at identifying non-cytotoxic molecules capable of specifically re-localizing PrPC from the plasma membrane as well as inhibiting prion replication and toxicity in cell cultures. I found four candidate hits inducing a significant reduction in cell surface PrPC, one of which also inhibited prion propagation and toxicity in cell cultures in a strain-independent fashion. In a previous publication, an artificial mutant of PrPC (?CR), sensitizing cells to several cationic antibiotics as Zeocin, was used to screen a library of compounds rescuing Zeocin-induced cytotoxicity. However, the main hit of the screening, named LD24, had low efficiency and high toxicity. In the second part of my thesis, I coupled cycles of chemical rearrangement and screening steps using ?CR cells, to test a small library of derivatives of LD24 and validated the selected compounds with a panel of cellular assays. I found that one molecule, SM231 and its derivative SM884, counteracted PrPC-mediated toxicity in cellular and ex vivo models of prion disease and Alzheimer's disease. Collectively, these studies define new screening methods and novel anti-prion compounds supporting the notion that removing PrPC from the cell surface and blocking its cytotoxicity could represent viable therapeutic strategies for prion diseases and other neurodegenerative conditions. more...
- Published
- 2019
9. Identification of compounds inhibiting prion replication and toxicity by removing PrPC from the cell surface
- Author
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Biggi, Silvia, primary, Pancher, Michael, additional, Stincardini, Claudia, additional, Luotti, Silvia, additional, Massignan, Tania, additional, Dalle Vedove, Andrea, additional, Astolfi, Andrea, additional, Gatto, Pamela, additional, Lolli, Graziano, additional, Barreca, Maria Letizia, additional, Bonetto, Valentina, additional, Adami, Valentina, additional, and Biasini, Emiliano, additional more...
- Published
- 2019
- Full Text
- View/download PDF
10. Identification of compounds inhibiting prion replication and toxicity by removing PrPC from the cell surface.
- Author
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Biggi, Silvia, Pancher, Michael, Stincardini, Claudia, Luotti, Silvia, Massignan, Tania, Dalle Vedove, Andrea, Astolfi, Andrea, Gatto, Pamela, Lolli, Graziano, Barreca, Maria Letizia, Bonetto, Valentina, Adami, Valentina, and Biasini, Emiliano more...
- Subjects
- *
CELL membranes , *PRIONS , *BOVINE spongiform encephalopathy , *PRION diseases , *SCRAPIE , *CHEMICAL libraries , *CELL culture - Abstract
The vast majority of therapeutic approaches tested so far for prion diseases, transmissible neurodegenerative disorders of human and animals, tackled PrPSc, the aggregated and infectious isoform of the cellular prion protein (PrPC), with largely unsuccessful results. Conversely, targeting PrPC expression, stability or cell surface localization are poorly explored strategies. We recently characterized the mode of action of chlorpromazine, an anti‐psychotic drug known to inhibit prion replication and toxicity by inducing the re‐localization of PrPC from the plasma membrane. Unfortunately, chlorpromazine possesses pharmacokinetic properties unsuitable for chronic use in vivo, namely low specificity and high toxicity. Here, we employed HEK293 cells stably expressing EGFP‐PrP to carry out a semi‐automated high content screening (HCS) of a chemical library directed at identifying non‐cytotoxic molecules capable of specifically relocalizing PrPC from the plasma membrane as well as inhibiting prion replication in N2a cell cultures. We identified four candidate hits inducing a significant reduction in cell surface PrPC, one of which also inhibited prion propagation and toxicity in cell cultures in a strain‐independent fashion. This study defines a new screening method and novel anti‐prion compounds supporting the notion that removing PrPC from the cell surface could represent a viable therapeutic strategy for prion diseases. [ABSTRACT FROM AUTHOR] more...
- Published
- 2020
- Full Text
- View/download PDF
11. Pharmacological Agents Targeting the Cellular Prion Protein
- Author
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Barreca, Maria, primary, Iraci, Nunzio, additional, Biggi, Silvia, additional, Cecchetti, Violetta, additional, and Biasini, Emiliano, additional
- Published
- 2018
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12. An antipsychotic drug exerts anti-prion effects by altering the localization of the cellular prion protein
- Author
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Stincardini, Claudia, primary, Massignan, Tania, additional, Biggi, Silvia, additional, Elezgarai, Saioa R., additional, Sangiovanni, Valeria, additional, Vanni, Ilaria, additional, Pancher, Michael, additional, Adami, Valentina, additional, Moreno, Jorge, additional, Stravalaci, Matteo, additional, Maietta, Giulia, additional, Gobbi, Marco, additional, Negro, Alessandro, additional, Requena, Jesús R., additional, Castilla, Joaquín, additional, Nonno, Romolo, additional, and Biasini, Emiliano, additional more...
- Published
- 2017
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13. A Small-Molecule Inhibitor of Prion Replication and Mutant Prion Protein Toxicity
- Author
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Massignan, Tania, primary, Sangiovanni, Valeria, additional, Biggi, Silvia, additional, Stincardini, Claudia, additional, Elezgarai, Saioa R., additional, Maietta, Giulia, additional, Andreev, Ivan A., additional, Ratmanova, Nina K., additional, Belov, Dmitry S., additional, Lukyanenko, Evgeny R., additional, Belov, Grigory M., additional, Barreca, Maria Letizia, additional, Altieri, Andrea, additional, Kurkin, Alexander V., additional, and Biasini, Emiliano, additional more...
- Published
- 2017
- Full Text
- View/download PDF
14. Evidence of Presynaptic Localization and Function of the c-Jun N-Terminal Kinase
- Author
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Biggi, Silvia, primary, Buccarello, Lucia, additional, Sclip, Alessandra, additional, Lippiello, Pellegrino, additional, Tonna, Noemi, additional, Rumio, Cristiano, additional, Di Marino, Daniele, additional, Miniaci, Maria Concetta, additional, and Borsello, Tiziana, additional more...
- Published
- 2017
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15. Epidermal RAF prevents allergic skin disease
- Author
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Raguz, Josipa, primary, Jeric, Ines, additional, Niault, Theodora, additional, Nowacka, Joanna Daniela, additional, Kuzet, Sanya Eduarda, additional, Rupp, Christian, additional, Fischer, Irmgard, additional, Biggi, Silvia, additional, Borsello, Tiziana, additional, and Baccarini, Manuela, additional more...
- Published
- 2016
- Full Text
- View/download PDF
16. Author response: Epidermal RAF prevents allergic skin disease
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Raguz, Josipa, primary, Jeric, Ines, additional, Niault, Theodora, additional, Nowacka, Joanna Daniela, additional, Kuzet, Sanya Eduarda, additional, Rupp, Christian, additional, Fischer, Irmgard, additional, Biggi, Silvia, additional, Borsello, Tiziana, additional, and Baccarini, Manuela, additional more...
- Published
- 2016
- Full Text
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17. The pharmacological inhibition of JNK-pathway reduces severity of Spinal Muscular Atrophy in mice.
- Author
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Boido, Marina, Schellino, Roberta, Biggi, SIlvia, Borsell, Tiziana, and Vercelli, Alessandro
- Subjects
SPINAL muscular atrophy ,PHARMACOLOGY ,JNK mitogen-activated protein kinases - Abstract
Spinal muscular atrophy (SMA) is a recessive autosomal neuromuscular disease, characterized by motor impairment, muscle atrophy and premature death following motor neuron (MN) degeneration, due to the lack of SMN (survival motor neuron) protein. Currently, the cellular and molecular mechanisms underlying MN death are only partly known [1], although recently it has been shown that the JNK-signalling pathway might be involved in the SMA pathogenesis. After confirming the activation of JNK in our SMA mouse model (SMN2+/+; SMNδ7+/+; Smn-/-), we tested on these mice a synthetic JNK-inhibitor peptide (D-JNKI), by chronic administration from postnatal day 1 (P1) to P10; then, at age P12, we analyzed their spinal cords and quadriceps muscles. We observed that D-JNKI administration delayed MN death and decreased neuroinflammation in the spinal cord. Moreover, by inhibiting JNK pathway, the muscular fibers and the neuromuscular junctions appeared respectively more trophic and mature. The histological/molecular results positively correlated with improved motor performances and hindlimb muscular tone. Finally, the treatment slightly, but significantly increased lifespan in SMA mice. Overall, our results identify JNK as a promising target to reduce MN cell death and progressive skeletal muscle atrophy, providing insight into the role of JNK-pathway for developing alternative pharmacological strategies for the treatment of SMA.This work was supported by grants from CRT Foundation, Girotondo/ONLUS and SMArathon-ONLUS foundations. [ABSTRACT FROM AUTHOR] more...
- Published
- 2018
18. Evidence of Presynaptic Localization and Function of the c-Jun N-Terminal Kinase
- Author
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Tiziana Borsello, Alessandra Sclip, Noemi Tonna, Maria Concetta Miniaci, Pellegrino Lippiello, Lucia Buccarello, Cristiano Rumio, Silvia Biggi, Daniele Di Marino, Biggi, Silvia, Buccarello, Lucia, Sclip, Alessandra, Lippiello, Pellegrino, Tonna, Noemi, Rumio, Cristiano, Di Marino, Daniele, Miniaci, Maria, and Borsello, Tiziana more...
- Subjects
0301 basic medicine ,Male ,N-Methylaspartate ,Article Subject ,Glycine ,Presynaptic Terminals ,Biology ,Receptors, N-Methyl-D-Aspartate ,lcsh:RC321-571 ,03 medical and health sciences ,Mice ,0302 clinical medicine ,Mitogen-Activated Protein Kinase 10 ,Excitatory Amino Acid Agonists ,Animals ,Mitogen-Activated Protein Kinase 9 ,Receptor ,lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry ,Cerebral Cortex ,Effector ,Kinase ,c-jun ,JNK Mitogen-Activated Protein Kinases ,Excitatory Postsynaptic Potentials ,Cell biology ,030104 developmental biology ,Neurology ,Synaptic plasticity ,Excitatory postsynaptic potential ,Phosphorylation ,NMDA receptor ,Female ,Neurology (clinical) ,SNARE Proteins ,030217 neurology & neurosurgery ,Research Article ,Synaptosomes - Abstract
The c-Jun N-terminal kinase (JNK) is part of a stress signalling pathway strongly activated by NMDA-stimulation and involved in synaptic plasticity. Many studies have been focused on the post-synaptic mechanism of JNK action, and less is known about JNK presynaptic localization and its physiological role at this site. Here we examined whether JNK is present at the presynaptic site and its activity after presynaptic NMDA receptors stimulation. By using N-SIM Structured Super Resolution Microscopy as well as biochemical approaches, we demonstrated that presynaptic fractions contained significant amount of JNK protein and its activated form. By means of modelling design, we found that JNK, via the JBD domain, acts as a physiological effector on T-SNARE proteins; then using biochemical approaches we demonstrated the interaction between Syntaxin-1-JNK, Syntaxin-2-JNK, and Snap25-JNK. In addition, taking advance of the specific JNK inhibitor peptide, D-JNKI1, we defined JNK action on the SNARE complex formation. Finally, electrophysiological recordings confirmed the role of JNK in the presynaptic modulation of vesicle release. These data suggest that JNK-dependent phosphorylation of T-SNARE proteins may have an important functional role in synaptic plasticity. more...
- Published
- 2017
19. Identification of compounds inhibiting prion replication and toxicity by removing PrP C from the cell surface.
- Author
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Biggi S, Pancher M, Stincardini C, Luotti S, Massignan T, Dalle Vedove A, Astolfi A, Gatto P, Lolli G, Barreca ML, Bonetto V, Adami V, and Biasini E
- Subjects
- Animals, Casein Kinase II antagonists & inhibitors, Cell Line, Tumor, Cell Survival drug effects, Drug Evaluation, Preclinical methods, Fluorescent Dyes, Gene Expression, Green Fluorescent Proteins analysis, Green Fluorescent Proteins genetics, HEK293 Cells, Harmaline analogs & derivatives, Harmaline pharmacology, Hematoxylin analogs & derivatives, Hematoxylin pharmacology, Humans, Mice, Neuroblastoma, PrPC Proteins genetics, Prions biosynthesis, Prions toxicity, Quinacrine pharmacology, Tacrolimus pharmacology, Cell Membrane chemistry, PrPC Proteins analysis, Prions antagonists & inhibitors
- Abstract
The vast majority of therapeutic approaches tested so far for prion diseases, transmissible neurodegenerative disorders of human and animals, tackled PrP
Sc , the aggregated and infectious isoform of the cellular prion protein (PrPC ), with largely unsuccessful results. Conversely, targeting PrPC expression, stability or cell surface localization are poorly explored strategies. We recently characterized the mode of action of chlorpromazine, an anti-psychotic drug known to inhibit prion replication and toxicity by inducing the re-localization of PrPC from the plasma membrane. Unfortunately, chlorpromazine possesses pharmacokinetic properties unsuitable for chronic use in vivo, namely low specificity and high toxicity. Here, we employed HEK293 cells stably expressing EGFP-PrP to carry out a semi-automated high content screening (HCS) of a chemical library directed at identifying non-cytotoxic molecules capable of specifically relocalizing PrPC from the plasma membrane as well as inhibiting prion replication in N2a cell cultures. We identified four candidate hits inducing a significant reduction in cell surface PrPC , one of which also inhibited prion propagation and toxicity in cell cultures in a strain-independent fashion. This study defines a new screening method and novel anti-prion compounds supporting the notion that removing PrPC from the cell surface could represent a viable therapeutic strategy for prion diseases., (© 2019 International Society for Neurochemistry.) more...- Published
- 2020
- Full Text
- View/download PDF
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