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3 results on '"Biressi S"'

1. Combinatorial activation of the WNT-dependent fibrogenic program by distinct complement subunits in dystrophic muscle

Author

Florio, F, Vencato, S, Papa, F, Libergoli, M, Kheir, E, Ghzaiel, I, Rando, T, Torrente, Y, Biressi, S, Florio F., Vencato S., Papa F. T., Libergoli M., Kheir E., Ghzaiel I., Rando T. A., Torrente Y., Biressi S., Florio, F, Vencato, S, Papa, F, Libergoli, M, Kheir, E, Ghzaiel, I, Rando, T, Torrente, Y, Biressi, S, Florio F., Vencato S., Papa F. T., Libergoli M., Kheir E., Ghzaiel I., Rando T. A., Torrente Y., and Biressi S.

Abstract

Fibrosis is associated with compromised muscle functionality in Duchenne muscular dystrophy (DMD). We report observations with tissues from dystrophic patients and mice supporting a model to explain fibrosis in DMD, which relies on the crosstalk between the complement and the WNT signaling pathways and the functional interactions of two cellular types. Fibro-adipogenic progenitors and macrophages, which populate the inflamed dystrophic muscles, act as a combinatorial source of WNT activity by secreting distinct subunits of the C1 complement complex. The resulting aberrant activation of the WNT signaling in responsive cells, such as fibro-adipogenic progenitors, contributes to fibrosis. Indeed, pharmacological inhibition of the C1r/s subunits in a murine model of DMD mitigated the activation of the WNT signaling pathway, reduced the fibrogenic characteristics of the fibro-adipogenic progenitors, and ameliorated the dystrophic phenotype. These studies shed new light on the molecular and cellular mechanisms responsible for fibrosis in muscular dystrophy and open to new therapeutic strategies.

Published
2023

2. Mesoangioblasts at 20: From the embryonic aorta to the patient bed

Author

Cossu, G, Tonlorenzi, R, Brunelli, S, Sampaolesi, M, Messina, G, Azzoni, E, Benedetti, S, Biressi, S, Bonfanti, C, Bragg, L, Camps, J, Cappellari, O, Cassano, M, Ciceri, F, Coletta, M, Covarello, D, Crippa, S, Cusella-De Angelis, M, De Angelis, L, Dellavalle, A, Diaz-Manera, J, Galli, D, Galli, F, Gargioli, C, Gerli, M, Giacomazzi, G, Galvez, B, Hoshiya, H, Guttinger, M, Innocenzi, A, Minasi, M, Perani, L, Previtali, S, Quattrocelli, M, Ragazzi, M, Roostalu, U, Rossi, G, Scardigli, R, Sirabella, D, Tedesco, F, Torrente, Y, Ugarte, G, Cossu, Giulio, Tonlorenzi, Rossana, Brunelli, Silvia, Sampaolesi, Maurilio, Messina, Graziella, Azzoni, Emanuele, Benedetti, Sara, Biressi, Stefano, Bonfanti, Chiara, Bragg, Laricia, Camps, Jordi, Cappellari, Ornella, Cassano, Marco, Ciceri, Fabio, Coletta, Marcello, Covarello, Diego, Crippa, Stefania, Cusella-De Angelis, M Gabriella, De Angelis, Luciana, Dellavalle, Arianna, Diaz-Manera, Jordi, Galli, Daniela, Galli, Francesco, Gargioli, Cesare, Gerli, Mattia F M, Giacomazzi, Giorgia, Galvez, Beatriz G, Hoshiya, Hidetoshi, Guttinger, Maria, Innocenzi, Anna, Minasi, M Giulia, Perani, Laura, Previtali, Stefano C, Quattrocelli, Mattia, Ragazzi, Martina, Roostalu, Urmas, Rossi, Giuliana, Scardigli, Raffaella, Sirabella, Dario, Tedesco, Francesco Saverio, Torrente, Yvan, Ugarte, Gonzalo, Cossu, G, Tonlorenzi, R, Brunelli, S, Sampaolesi, M, Messina, G, Azzoni, E, Benedetti, S, Biressi, S, Bonfanti, C, Bragg, L, Camps, J, Cappellari, O, Cassano, M, Ciceri, F, Coletta, M, Covarello, D, Crippa, S, Cusella-De Angelis, M, De Angelis, L, Dellavalle, A, Diaz-Manera, J, Galli, D, Galli, F, Gargioli, C, Gerli, M, Giacomazzi, G, Galvez, B, Hoshiya, H, Guttinger, M, Innocenzi, A, Minasi, M, Perani, L, Previtali, S, Quattrocelli, M, Ragazzi, M, Roostalu, U, Rossi, G, Scardigli, R, Sirabella, D, Tedesco, F, Torrente, Y, Ugarte, G, Cossu, Giulio, Tonlorenzi, Rossana, Brunelli, Silvia, Sampaolesi, Maurilio, Messina, Graziella, Azzoni, Emanuele, Benedetti, Sara, Biressi, Stefano, Bonfanti, Chiara, Bragg, Laricia, Camps, Jordi, Cappellari, Ornella, Cassano, Marco, Ciceri, Fabio, Coletta, Marcello, Covarello, Diego, Crippa, Stefania, Cusella-De Angelis, M Gabriella, De Angelis, Luciana, Dellavalle, Arianna, Diaz-Manera, Jordi, Galli, Daniela, Galli, Francesco, Gargioli, Cesare, Gerli, Mattia F M, Giacomazzi, Giorgia, Galvez, Beatriz G, Hoshiya, Hidetoshi, Guttinger, Maria, Innocenzi, Anna, Minasi, M Giulia, Perani, Laura, Previtali, Stefano C, Quattrocelli, Mattia, Ragazzi, Martina, Roostalu, Urmas, Rossi, Giuliana, Scardigli, Raffaella, Sirabella, Dario, Tedesco, Francesco Saverio, Torrente, Yvan, and Ugarte, Gonzalo

Abstract

In 2002 we published an article describing a population of vessel-associated progenitors that we termed mesoangioblasts (MABs). During the past decade evidence had accumulated that during muscle development and regeneration things may be more complex than a simple sequence of binary choices (e.g., dorsal vs. ventral somite). LacZ expressing fibroblasts could fuse with unlabelled myoblasts but not among themselves or with other cell types. Bone marrow derived, circulating progenitors were able to participate in muscle regeneration, though in very small percentage. Searching for the embryonic origin of these progenitors, we identified them as originating at least in part from the embryonic aorta and, at later stages, from the microvasculature of skeletal muscle. While continuing to investigate origin and fate of MABs, the fact that they could be expanded in vitro (also from human muscle) and cross the vessel wall, suggested a protocol for the cell therapy of muscular dystrophies. We tested this protocol in mice and dogs before proceeding to the first clinical trial on Duchenne Muscular Dystrophy patients that showed safety but minimal efficacy. In the last years, we have worked to overcome the problem of low engraftment and tried to understand their role as auxiliary myogenic progenitors during development and regeneration.

Published
2023

3. 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

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.

Published
2021

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