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8 results on '"Brunetti, Antonio"'

4. A polymorphism of HMGA1 protects against proliferative diabetic retinopathy by impairing HMGA1-induced VEGFA expression

Author

Chiefari, Eusebio, primary, Ventura, Valeria, additional, Capula, Carmelo, additional, Randazzo, Giorgio, additional, Scorcia, Vincenzo, additional, Fedele, Monica, additional, Arcidiacono, Biagio, additional, Nevolo, Maria Teresa, additional, Bilotta, Francesco Luciano, additional, Vitiello, Michela, additional, Palmieri, Camillo, additional, Gulletta, Elio, additional, Fusco, Alfredo, additional, Foti, Daniela, additional, Vero, Raffaella, additional, and Brunetti, Antonio, additional

Published
2016
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6. A polymorphism of HMGA1 is associated with increased risk of metabolic syndrome and related components

Author

Chiefari, Eusebio, primary, Tanyolaç, Sinan, additional, Iiritano, Stefania, additional, Sciacqua, Angela, additional, Capula, Carmelo, additional, Arcidiacono, Biagio, additional, Nocera, Aurora, additional, Possidente, Katiuscia, additional, Baudi, Francesco, additional, Ventura, Valeria, additional, Brunetti, Giuseppe, additional, Brunetti, Francesco S., additional, Vero, Raffaella, additional, Maio, Raffaele, additional, Greco, Manfredi, additional, Pavia, Maria, additional, Hodoglugil, Ugur, additional, Durlach, Vincent, additional, Pullinger, Clive R., additional, Goldfine, Ira D., additional, Perticone, Francesco, additional, Foti, Daniela, additional, and Brunetti, Antonio, additional

Published
2013
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7. HMGA1 is a novel downstream nuclear target of the insulin receptor signaling pathway

Author

Chiefari, Eusebio, primary, Nevolo, Maria T., additional, Arcidiacono, Biagio, additional, Maurizio, Elisa, additional, Nocera, Aurora, additional, Iiritano, Stefania, additional, Sgarra, Riccardo, additional, Possidente, Katiuscia, additional, Palmieri, Camillo, additional, Paonessa, Francesco, additional, Brunetti, Giuseppe, additional, Manfioletti, Guidalberto, additional, Foti, Daniela, additional, and Brunetti, Antonio, additional

Published
2012
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8. A novel mechanism of post-translational modulation of HMGA functions by the histone chaperone nucleophosmin

Author

Antonio Brunetti, Laura Arnoldo, Stefania Iiritano, Riccardo Sgarra, Biagio Arcidiacono, Eusebio Chiefari, Ilenia Pellarin, Guidalberto Manfioletti, Silvia Pegoraro, Arnoldo, Laura, Sgarra, Riccardo, Chiefari, Eusebio, Iiritano, Stefania, Arcidiacono, Biagio, Pegoraro, Silvia, Pellarin, Ilenia, Brunetti, Antonio, and Manfioletti, Guidalberto

Subjects
Transcription, Genetic, Molecular Sequence Data, Regulatory Sequences, Nucleic Acid, Article, DNA-binding, Chaperones, Humans, Histone Chaperones, Amino Acid Sequence, HMGA, RNA, Small Interfering, HMGA Proteins, Promoter Regions, Genetic, Genetics, Nucleophosmin, Multidisciplinary, Binding Sites, biology, Nuclear Proteins, Promoter, DNA, Hep G2 Cells, Chromatin, Receptor, Insulin, Cell biology, Protein Structure, Tertiary, Insulin-Like Growth Factor Binding Protein 1, Histone, Regulatory sequence, Chaperone (protein), biology.protein, Multidisciplinary, HMGA, Chaperones, Chromatin, DNA-binding, RNA Interference, Protein Processing, Post-Translational, Protein Binding
Abstract

High Mobility Group A are non-histone nuclear proteins that regulate chromatin plasticity and accessibility, playing an important role both in physiology and pathology. Their activity is controlled by transcriptional, post-transcriptional and post-translational mechanisms. In this study we provide evidence for a novel modulatory mechanism for HMGA functions. We show that HMGAs are complexed in vivo with the histone chaperone nucleophosmin (NPM1), that this interaction requires the histone-binding domain of NPM1 and that NPM1 modulates both DNA-binding affinity and specificity of HMGAs. By focusing on two human genes whose expression is directly regulated by HMGA1, the Insulin receptor (INSR) and the Insulin-like growth factor-binding protein 1 (IGFBP1) genes, we demonstrated that occupancy of their promoters by HMGA1 was NPM1-dependent, reflecting a mechanism in which the activity of these cis-regulatory elements is directly modulated by NPM1 leading to changes in gene expression. HMGAs need short stretches of AT-rich nucleosome-free regions to bind to DNA. Therefore, many putative HMGA binding sites are present within the genome. Our findings indicate that NPM1, by exerting a chaperoning activity towards HMGAs, may act as a master regulator in the control of DNA occupancy by these proteins and hence in HMGA-mediated gene expression.

Published
2015

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