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38 results on '"Oneto, Michele"'

2. Nanoscale Distribution of Nuclear Sites by Super-Resolved Image Cross-Correlation Spectroscopy

Author

Oneto, Michele, Scipioni, Lorenzo, Sarmento, Maria J, Cainero, Isotta, Pelicci, Simone, Furia, Laura, Pelicci, Pier G, Dellino, Gaetano I, Bianchini, Paolo, Faretta, Mario, Gratton, Enrico, Diaspro, Alberto, and Lanzanò, Luca

Subjects
Bioengineering, Genetics, Nanotechnology, 1.1 Normal biological development and functioning, Underpinning research, Generic health relevance, Cell Nucleus, Color, Humans, MCF-7 Cells, Microscopy, Spectrum Analysis, Physical Sciences, Chemical Sciences, Biological Sciences, Biophysics
Abstract

Deciphering the spatiotemporal coordination between nuclear functions is important to understand its role in the maintenance of human genome. In this context, super-resolution microscopy has gained considerable interest because it can be used to probe the spatial organization of functional sites in intact single-cell nuclei in the 20-250 nm range. Among the methods that quantify colocalization from multicolor images, image cross-correlation spectroscopy (ICCS) offers several advantages, namely it does not require a presegmentation of the image into objects and can be used to detect dynamic interactions. However, the combination of ICCS with super-resolution microscopy has not been explored yet. Here, we combine dual-color stimulated emission depletion (STED) nanoscopy with ICCS (STED-ICCS) to quantify the nanoscale distribution of functional nuclear sites. We show that super-resolved ICCS provides not only a value of the colocalized fraction but also the characteristic distances associated to correlated nuclear sites. As a validation, we quantify the nanoscale spatial distribution of three different pairs of functional nuclear sites in MCF10A cells. As expected, transcription foci and a transcriptionally repressive histone marker (H3K9me3) are not correlated. Conversely, nascent DNA replication foci and the proliferating cell nuclear antigen(PCNA) protein have a high level of proximity and are correlated at a nanometer distance scale that is close to the limit of our experimental approach. Finally, transcription foci are found at a distance of 130 nm from replication foci, indicating a spatial segregation at the nanoscale. Overall, our data demonstrate that STED-ICCS can be a powerful tool for the analysis of the nanoscale distribution of functional sites in the nucleus.

Published
2019

3. Fluorescence Microscopy

Author

Diaspro, Alberto, Bianchini, Paolo, Cella Zanacchi, Francesca, Lanzanò, Luca, Vicidomini, Giuseppe, Oneto, Michele, Pesce, Luca, Cainero, Isotta, Hawkes, Peter W., editor, and Spence, John C. H., editor

Published
2019
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7. Optical nanoscopy challenges in the metaverse era. The case of multimodal imaging of chromatin in the nucleus

Author

Diaspro, Alberto, primary, Bianchini, Paolo, additional, Cuneo, Lisa, additional, Baldini, Francesca, additional, Cainero, Isotta, additional, Usai, Chantal, additional, Civita, Simone, additional, Oneto, Michele, additional, Scotto d'Abbusco, Marco, additional, Nepita, Irene, additional, Zeinab Zeaiter, Lama, additional, Mariangeli, Matteo, additional, Kerdegari, Sajedeh, additional, Castello, Marco, additional, and Piazza, Simonluca, additional

Published
2023
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9. Evaluating the effect of different Expansion Microscopy protocols on mammalian DNA-Chromatin architecture

Author

Usai, Chantal, Oneto, Michele, Cainero, Isotta, Baldini, Francesca, Pierzyńska-Mach, Agnieszka, Bianchini, Paolo, and Diaspro, Alberto

Abstract

Expansion microscopy (ExM) is a novel super-resolution microscopy method that enables nano-scale biophysical studies by increasing the distance among biomolecules. Such effect is achieved through the physical magnification of the specimen obtained by its embedding inside a swellable polymer network, eventually expanded in water. Several improvements to the original ExM technique were made to optimize the imaging of proteins and the isotropicity of their expansion. However, few works have been done to investigate what happens to the DNA-chromatin architecture once it’s subjected to the mechanical strain associated with the expansion process. To understand whether this technique could be suitable for investigating the crowded nuclear environment, we aim to study the induced changes in the DNA conformation by the application of different expansion microscopy protocols to fixed mammalian cells and single mononucleosomes. Optical imaging will be performed using a combination of confocal, two-photon excitation and super-resolution microscopy techniques, and the performances of different fluorophores for DNA staining will also be compared. Finally, we aim to develop a reproducible protocol for the precise quantification of the expansion factor of the specimens at the microscale.

Published
2022
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14. Nanoscale Distribution of Nuclear Sites Analyzed by Superresolution STED Image Cross-Correlation Spectroscopy

Author

Oneto, Michele, primary, Scipioni, Lorenzo, additional, Sarmento, Maria, additional, Cainero, Isotta, additional, Cerutti, Elena, additional, Pelicci, Simone, additional, Furia, Laura, additional, Giuseppe Pelicci, Pier, additional, Ivan Dellino, Gaetano, additional, Bianchini, Paolo, additional, Faretta, Mario, additional, Gratton, Enrico, additional, Diaspro, Alberto, additional, and Lanzano, Luca, additional

Published
2020
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16. Hypericin–Apomyoglobin: An Enhanced Photosensitizer Complex for the Treatment of Tumor Cells

Author

Bianchini, Paolo, primary, Cozzolino, Marco, additional, Oneto, Michele, additional, Pesce, Luca, additional, Pennacchietti, Francesca, additional, Tognolini, Massimiliano, additional, Giorgio, Carmine, additional, Nonell, Santi, additional, Cavanna, Luigi, additional, Delcanale, Pietro, additional, Abbruzzetti, Stefania, additional, Diaspro, Alberto, additional, and Viappiani, Cristiano, additional

Published
2019
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19. Chromatin Alterations in a Model of Oncogene Activation Studied by Advanced Fluorescence Microscopy

Author

Lanzano′, Luca, primary, Oneto, Michele, additional, Cainero, Isotta, additional, Pelicci, Simone, additional, Sarmento, Maria, additional, Scipioni, Lorenzo, additional, Faretta, Mario, additional, Furia, Laura, additional, Ivan Dellino, Gaetano, additional, Giuseppe Pelicci, Pier, additional, Bianchini, Paolo, additional, and Diaspro, Alberto, additional

Published
2019
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23. A Liquid Tunable Microscope as a New Paradigm in Optical Microscopy to Paint 4D Chromatin Organisation in the Cell Nucleus

Author

Diaspro, Alberto, primary, Cainero, Isotta, additional, Lanzanò, Luca, additional, Bianchini, Paolo, additional, Vicidomini, Giuseppe, additional, Cella Zanacchi, Francesca, additional, Pesce, Luca, additional, Pelicci, Simone, additional, Oneto, Michele, additional, Di Bona, Melody, additional, Faretta, Mario, additional, Barboro, Paola, additional, and Le Gratiet, Aymeric, additional

Published
2018
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26. SPLIT-STED Imaging of Nuclear Structures

Author

Lanzano', Luca, primary, Sarmento, Maria J., additional, Scipioni, Lorenzo, additional, Oneto, Michele, additional, Pelicci, Simone, additional, Di Bona, Melody, additional, Pesce, Luca, additional, Faretta, Mario, additional, Furia, Laura, additional, Dellino, Gaetano I., additional, Pelicci, Pier G., additional, Bianchini, Paolo, additional, and Diaspro, Alberto, additional

Published
2018
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29. Corrigendum: Labeling and Selective Inactivation of Gram-Positive Bacteria Employing Bimodal Photoprobes with Dual Readouts

Author

Galstyan, Anzhela, primary, Block, Desiree, additional, Niemann, Silke, additional, Grüner, Malte C., additional, Abbruzzetti, Stefania, additional, Oneto, Michele, additional, Daniliuc, Constantin G., additional, Hermann, Sven, additional, Viappiani, Cristiano, additional, Schäfers, Michael, additional, Löffler, Bettina, additional, Strassert, Cristian A., additional, and Faust, Andreas, additional

Published
2016
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30. Labeling and Selective Inactivation of Gram-Positive Bacteria Employing Bimodal Photoprobes with Dual Readouts

Author

Galstyan, Anzhela, primary, Block, Desiree, additional, Niemann, Silke, additional, Grüner, Malte C., additional, Abbruzzetti, Stefania, additional, Oneto, Michele, additional, Daniliuc, Constantin G., additional, Hermann, Sven, additional, Viappiani, Cristiano, additional, Schäfers, Michael, additional, Löffler, Bettina, additional, Strassert, Cristian A., additional, and Faust, Andreas, additional

Published
2016
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32. 3 Color - 3 Dimensional STED Nanoscopy

Author

Peres, Chiara, primary, Oneto, Michele, additional, D’Autilia, Francesca, additional, Galiani, Silvia, additional, Lanzano’, Luca, additional, Vicidomini, Giuseppe, additional, Diaspro, Alberto, additional, and Bianchini, Paolo, additional

Published
2015
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33. New findings in ATP supply in rod outer segments: Insights for retinopathies

Author

Calzia, Daniela, primary, Barabino, Stefano, additional, Bianchini, Paolo, additional, Garbarino, Greta, additional, Oneto, Michele, additional, Caicci, Federico, additional, Diaspro, Alberto, additional, Tacchetti, Carlo, additional, Manni, Lucia, additional, Candiani, Simona, additional, Ravera, Silvia, additional, Morelli, Alessandro, additional, Enrico Traverso, Carlo, additional, and Panfoli, Isabella, additional

Published
2013
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35. MRCKα is activated by caspase cleavage to assemble an apical actin ring for epithelial cell extrusion.

Author

Gagliardi, Paolo Armando, Somale, Desiana, Puliafito, Alberto, Chiaverina, Giulia, di Blasio, Laura, Oneto, Michele, Bianchini, Paolo, Bussolino, Federico, and Primo, Luca

Subjects
*KINASES, *CASPASES, *ACTOMYOSIN
Abstract

Extrusion of apoptotic cells from epithelial tissues requires orchestrated morphological rearrangements of the apoptotic cell and its neighbors. However, the connections between the apoptotic cascade and events leading to extrusion are not fully understood. Here, we characterize an apoptotic extrusion apical actin ring (EAAR) that is assembled within the apoptotic cell and drives epithelial extrusion. Caspase-mediated cleavage of myotonic dystrophy kinase-related CDC42-binding kinase-α (MRCKα) triggers a signaling pathway that leads to the assembly of EAAR that pulls actin bundles, resulting in the compaction and removal of the cell body. We provide a detailed portrait of the EAAR including F-actin flow, the contribution of myosin contraction, and actin polymerization at bundles' terminals when the product of MRCKα cleavage is expressed. These results add to our understanding of the mechanisms controlling the process of epithelial extrusion by establishing a causal relationship between the triggering events of apoptosis, the activation of MRCKα, and its subsequent effects on the dynamics of actomyosin cytoskeleton rearrangement. [ABSTRACT FROM AUTHOR]

Published
2018
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36. An interaction between PRRT2 and Na+/K+ ATPase contributes to the control of neuronal excitability

Author

Anna Corradi, Michele Oneto, Flavia Valtorta, Alessandra Romei, Pietro Baldelli, Chiara Parodi, Fabio Benfenati, Davide Aprile, Bruno Sterlini, Anna Fassio, Pierluigi Valente, Anita Aperia, Sterlini, Bruno, Romei, Alessandra, Parodi, Chiara, Aprile, Davide, Oneto, Michele, Aperia, Anita, Valente, Pierluigi, Valtorta, Flavia, Fassio, Anna, Baldelli, Pietro, Benfenati, Fabio, and Corradi, Anna

Subjects
Proteomics, Cellular neuroscience, Molecular neuroscience, Paediatric neurological disorders, Proteomics, Cancer Research, ATPase, Immunology, Nerve Tissue Proteins, Molecular neuroscience, Synaptic Transmission, Cellular and Molecular Neuroscience, chemistry.chemical_compound, Cellular neuroscience, Humans, Na+/K+-ATPase, lcsh:QH573-671, Neurotransmitter, Adenosine Triphosphatases, Neurons, biology, Chemistry, lcsh:Cytology, Colocalization, Membrane Proteins, Afterhyperpolarization, Cell Biology, respiratory system, Cell biology, Paediatric neurological disorders, biology.protein, PRRT2
Abstract

Mutations in PRoline Rich Transmembrane protein 2 (PRRT2) cause pleiotropic syndromes including benign infantile epilepsy, paroxysmal kinesigenic dyskinesia, episodic ataxia, that share the paroxysmal character of the clinical manifestations. PRRT2 is a neuronal protein that plays multiple roles in the regulation of neuronal development, excitability, and neurotransmitter release. To better understand the physiopathology of these clinical phenotypes, we investigated PRRT2 interactome in mouse brain by a pulldown-based proteomic approach and identified α1 and α3 Na+/K+ ATPase (NKA) pumps as major PRRT2-binding proteins. We confirmed PRRT2 and NKA interaction by biochemical approaches and showed their colocalization at neuronal plasma membrane. The acute or constitutive inactivation of PRRT2 had a functional impact on NKA. While PRRT2-deficiency did not modify NKA expression and surface exposure, it caused an increased clustering of α3-NKA on the plasma membrane. Electrophysiological recordings showed that PRRT2-deficiency in primary neurons impaired NKA function during neuronal stimulation without affecting pump activity under resting conditions. Both phenotypes were fully normalized by re-expression of PRRT2 in PRRT2-deficient neurons. In addition, the NKA-dependent afterhyperpolarization that follows high-frequency firing was also reduced in PRRT2-silenced neurons. Taken together, these results demonstrate that PRRT2 is a physiological modulator of NKA function and suggest that an impaired NKA activity contributes to the hyperexcitability phenotype caused by PRRT2 deficiency.

Published
2021

38. Labeling and Selective Inactivation of Gram-Positive Bacteria Employing Bimodal Photoprobes with Dual Readouts.

Author

Galstyan A, Block D, Niemann S, Grüner MC, Abbruzzetti S, Oneto M, Daniliuc CG, Hermann S, Viappiani C, Schäfers M, Löffler B, Strassert CA, and Faust A

Subjects
Gram-Positive Bacteria chemistry, Luminescence, Methicillin-Resistant Staphylococcus aureus chemistry, Photosensitizing Agents pharmacology, Staphylococcus aureus chemistry, Carbohydrates chemistry, Gram-Positive Bacteria drug effects, Indoles chemistry, Methicillin-Resistant Staphylococcus aureus drug effects, Photosensitizing Agents chemistry, Silanes chemistry, Staphylococcus aureus drug effects
Abstract

Carbohydrate-conjugated silicon(IV) phthalocyanines with bimodal photoactivity were developed as probes with both fluorescent labeling and photosensitizing capabilities, and the concomitant fluorescent labeling and photoinduced inactivation of Gram-positive and Gram-negative models was explored. The maltohexaose-conjugated photoprobe provides a dual readout to distinguish between both groups of pathogens, as only the Gram-positive species was inactivated, even though both appeared labeled with near-infrared luminescence. Antibiotic resistance did not hinder the phototoxic effect, as even the methicillin-resistant pathogen Staphylococcus aureus (MRSA) was completely photoinactivated. Time-resolved confocal fluorescence microscopy analysis suggests that the photoprobe sticks onto the outer rim of the microorganisms, explaining the resistance of Gram-negative species on the basis of their membrane constitution. The mannose-conjugated photoprobe yields a different readout because it is able to label and to inactivate only the Gram-positive strain., (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Published
2016
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