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215 results on '"REINA, Simona"'

16. Specific Post-Translational Modifications of VDAC3 in ALS-SOD1 Model Cells Identified by High-Resolution Mass Spectrometry

Author

Pittalà, Maria Gaetana Giovanna, primary, Reina, Simona, additional, Nibali, Stefano Conti, additional, Cucina, Annamaria, additional, Cubisino, Salvatore Antonio Maria, additional, Cunsolo, Vincenzo, additional, Amodeo, Giuseppe Federico, additional, Foti, Salvatore, additional, De Pinto, Vito, additional, Saletti, Rosaria, additional, and Messina, Angela, additional

Published
2022
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23. A multicenter retrospective study on 4480 implanted PICC-ports: A GAVeCeLT project

Author

Bertoglio, Sergio, primary, Annetta, Maria Giuseppina, additional, Brescia, Fabrizio, additional, Emoli, Alessandro, additional, Fabiani, Fabio, additional, Fino, Maria, additional, Merlicco, Domenico, additional, Musaro, Andrea, additional, Orlandi, Marina, additional, Parisella, Laura, additional, Pinelli, Fulvio, additional, Reina, Simona, additional, Selmi, Valentina, additional, Solari, Nicola, additional, Tricarico, Fausto, additional, and Pittiruti, Mauro, additional

Published
2022
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25. Voltage-Dependent Anion Selective Channel 3: Unraveling Structural and Functional Features of the Least Known Porin Isoform

Author

Reina, Simona and Checchetto, Vanessa

Subjects
VDAC3, Physiology, Physiology (medical), Mini Review, QP1-981, electrophysiology, redox signaling, human pathologies, planar lipid bilayer
Abstract

Voltage-dependent anion-selective channels (VDAC) are pore-forming proteins located in the outer mitochondrial membrane. Three isoforms are encoded by separate genes in mammals (VDAC1-3). These proteins play a crucial role in the cell, forming the primary interface between mitochondrial and cellular metabolisms. Research on the role of VDACs in the cell is a rapidly growing field, but the function of VDAC3 remains elusive. The high-sequence similarity between isoforms suggests a similar pore-forming structure. Electrophysiological analyzes revealed that VDAC3 works as a channel; however, its gating and regulation remain debated. A comparison between VDAC3 and VDAC1-2 underlines the presence of a higher number of cysteines in both isoforms 2 and 3. Recent mass spectrometry data demonstrated that the redox state of VDAC3 cysteines is evolutionarily conserved. Accordingly, these residues were always detected as totally reduced or partially oxidized, thus susceptible to disulfide exchange. The deletion of selected cysteines significantly influences the function of the channel. Some cysteine mutants of VDAC3 exhibited distinct kinetic behavior, conductance values and voltage dependence, suggesting that channel activity can be modulated by cysteine reduction/oxidation. These properties point to VDAC3 as a possible marker of redox signaling in the mitochondrial intermembrane space. Here, we summarize our current knowledge about VDAC3 predicted structure, physiological role and regulation, and possible future directions in this research field.

Published
2021

35. A lower affinity to cytosolic proteins reveals VDAC3 isoform-specific role in mitochondrial biology

Author

Queralt-Martín, María, primary, Bergdoll, Lucie, additional, Teijido, Oscar, additional, Munshi, Nabill, additional, Jacobs, Daniel, additional, Kuszak, Adam J., additional, Protchenko, Olga, additional, Reina, Simona, additional, Magrì, Andrea, additional, De Pinto, Vito, additional, Bezrukov, Sergey M., additional, Abramson, Jeff, additional, and Rostovtseva, Tatiana K., additional

Published
2020
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37. Deletion of Voltage-Dependent Anion Channel 1 knocks mitochondria down triggering metabolic rewiring in yeast

Author

Magrì, Andrea, primary, Di Rosa, Maria Carmela, additional, Orlandi, Ivan, additional, Guarino, Francesca, additional, Reina, Simona, additional, Guarnaccia, Maria, additional, Morello, Giovanna, additional, Spampinato, Antonio, additional, Cavallaro, Sebastiano, additional, Messina, Angela, additional, Vai, Marina, additional, and De Pinto, Vito, additional

Published
2019
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40. Hypoxic-induced truncation of voltage-dependent anion channel 1 is mediated by both asparagine endopeptidase and calpain 1 activities

Author

Hadas, Pahima, Reina, Simona, Noa, Tadmor, Daniella, Dadon-Klein, Anna, Shteinfer-Kuzmine, Mazure, Nathalie M., DE PINTO, Vito Nicola, and Varda, Shoshan-Barmatz

Subjects
asparagine endopeptidase, VDAC1, hypoxia, calpain, Research Paper
Abstract

The voltage-dependent anion channel 1 (VDAC1), an outer mitochondria membrane (OMM) protein, serves as a mitochondrial gatekeeper, mediating the transport of nucleotides, Ca2+ and other metabolites across the OMM. VDAC1 also plays a central role in mitochondria-mediated apoptosis by facilitating the release of apoptotic proteins and by association with both pro- and anti-apoptotic proteins. Tumor cells, which are constantly exposed to hypoxic conditions, affect the cell via the transcription factor hypoxia-inducible factor (HIF) that induces transcriptional activity. In cultured cells and in lung cancer patients, hypoxia induces VDAC1 truncation at the C-terminus (VDAC1-ΔC). However, the molecular mechanisms involved in VDAC1-ΔC formation are unknown. Here, we show that hypoxia-induced VDAC1-ΔC formation is inhibited by the Ca2+ chelator BAPTA-AM, by calpain inhibitor-1, by inhibitor of the asparagine endopeptidase (AEP) and by si-RNA targeting HIF1-α or Ca2+-activated protease calpain-1 expression but not that of calpain-2. Finally, VDAC1-ΔC expressed in bacteria and reconstituted into a planar lipid bilayer exhibited decreased channel conductance relative to the full-length protein, yet retained voltage-dependent conductance. These findings suggest that hypoxia, acting via HIF-1α expression, leads to VDAC1 cleavage involving the activation of calpain 1 and AEP.

Published
2017

44. Anorectal Melanoma: Miles o Exeresi Locale?

Author

Cartesegna, Eleonora, Guzzetti, Sara, Valle, Valentina, Grossetti, Flavia, Reina, Simona, Caristo, Giuseppe, Razzore, Andrea, Soriero, Domenico, Costanzo, Federico, Casaccia, Marco, and Fornaro, Rosario

Published
2017

50. Recombinant yeast VDAC2: a comparison of electrophysiological features with the native form.

Author

Magrì, Andrea, Karachitos, Andonis, Di Rosa, Maria Carmela, Reina, Simona, Conti Nibali, Stefano, Messina, Angela, Kmita, Hanna, and De Pinto, Vito

Subjects
EUKARYOTIC cells, YEAST, POST-translational modification, RECOMBINANT proteins, SACCHAROMYCES cerevisiae, CANDIDA albicans
Abstract

Voltage‐dependent anion channel isoform 2 of the yeast Saccharomyces cerevisiae (yVDAC2) was believed for many years to be devoid of channel activity. Recently, we isolated yVDAC2 and showed that it exhibits channel‐forming activity in the planar lipid bilayer system when in its so‐called native form. Here, we describe an alternative strategy for yVDAC2 isolation, through heterologous expression in bacteria and refolding in vitro. Recombinant yVDAC2, like its native form, is able to form voltage‐dependent channels. However, some differences between native and recombinant yVDAC2 emerged in terms of voltage dependence and ion selectivity, suggesting that, in this specific case, the recombinant protein might be depleted of post‐translational modification(s) that occur in eukaryotic cells. [ABSTRACT FROM AUTHOR]

Published
2019
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