116 results on '"Francesco Papa"'
Search Results
2. Dio e il mondo che verrà: Una conversazione con Domenico Agasso
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Francesco Papa and Francesco Papa
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- 2021
3. Io credo, noi crediamo: Una riflessione inedita sulle radici della nostra fede
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Francesco Papa and Francesco Papa
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- 2020
4. Amici del Signore: I grandi personaggi della Bibbia
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Francesco Papa and Francesco Papa
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- 2020
5. Il Vangelo della domenica: Commentato dal Santo Padre
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Francesco Papa and Francesco Papa
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- 2019
6. L'umiltà e lo stupore
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Francesco Papa and Francesco Papa
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- 2018
7. Nel cuore di ogni padre: Alle radici della mia spiritualità
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Francesco Papa and Francesco Papa
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- 2016
8. La verità è un incontro: Omelie da Santa Marta
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Francesco Papa, Antonio Spadaro and Francesco Papa, Antonio Spadaro
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- 2016
9. Nei tuoi occhi è la mia parola: Omelie e discorsi di Buenos Aires 1999-2013
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Francesco Papa and Francesco Papa
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- 2016
10. Aprite la mente al vostro cuore (VINTAGE)
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Francesco Papa and Francesco Papa
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- 2015
11. La logica dell'amore
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Francesco Papa and Francesco Papa
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- 2015
12. La misericordia è una carezza: Vivere il giubileo nella realtà di ogni giorno
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Francesco Papa and Francesco Papa
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- 2015
13. La felicità si impara ogni giorno: Omelie da Santa Marta - marzo 2014 _ giugno 2015
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Francesco Papa, Antonio Spadaro and Francesco Papa, Antonio Spadaro
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- 2015
14. Siate forti nella tenerezza: Parole di coraggio e speranza per un anno da vivere insieme
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Francesco Papa and Francesco Papa
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- 2014
15. È l'amore che apre gli occhi (VINTAGE)
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Francesco Papa and Francesco Papa
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- 2014
16. La mia porta è sempre aperta (VINTAGE): Una conversazione con Antonio Spadaro
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Francesco Papa, Antonio Spadaro and Francesco Papa, Antonio Spadaro
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- 2014
17. Lo sguardo semplice e profondo dell'amore: 365 pensieri sull'amore, la famiglia, la fede
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Francesco Papa and Francesco Papa
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- 2014
18. Induction of mitochondrial dysfunction and oxidative stress in human fibroblast cultures exposed to serum from septic patients
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Raffaella, Trentadue, Fiore, Flavio, Fabrizia, Massaro, Francesco, Papa, Arcangela, Iuso, Salvatore, Scacco, Luigi, Santacroce, and Nicola, Brienza
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- 2012
- Full Text
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19. Allosteric Cooperativity in Proton Energy Conversion in A1-Type Cytochrome c Oxidase
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Giuseppe Capitanio, Sergio Papa, Luigi Leonardo Palese, and Francesco Papa
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Conformational change ,Stereochemistry ,Respiratory chain ,Cooperativity ,Heme ,Crystallography, X-Ray ,010402 general chemistry ,7. Clean energy ,01 natural sciences ,Electron Transport ,Electron Transport Complex IV ,03 medical and health sciences ,chemistry.chemical_compound ,Allosteric Regulation ,Structural Biology ,Cytochrome c oxidase ,Electrochemical gradient ,Molecular Biology ,030304 developmental biology ,0303 health sciences ,Binding Sites ,biology ,Cytochrome c ,Proton Pumps ,0104 chemical sciences ,Oxygen ,Heme A ,chemistry ,biology.protein ,Protons ,Protein Binding - Abstract
Cytochrome c oxidase (CcO), the CuA, heme a, heme a3, CuB enzyme of respiratory chain, converts the free energy released by aerobic cytochrome c oxidation into a membrane electrochemical proton gradient (ΔμH+). ΔμH+ derives from the membrane anisotropic arrangement of dioxygen reduction to two water molecules and transmembrane proton pumping from a negative (N) space to a positive (P) space separated by the membrane. Spectroscopic, potentiometric, and X-ray crystallographic analyses characterize allosteric cooperativity of dioxygen binding and reduction with protonmotive conformational states of CcO. These studies show that allosteric cooperativity stabilizes the favorable conformational state for conversion of redox energy into a transmembrane ΔμH+. (i) Dioxygen binding to Fea3 at BNC selects a CcO state in which the conformation of the subunit I-helix X, next in sequence to the hemes a and a3 histidine axial ligands, opens access of pumped protons from the N space to a Mg2+-storage site at the opposite (P) membrane side. (ii) Sequential electron transfer at CuA and heme a is associated with additional CcO conformational change in which protons are translocated from the Mg2+-site to the propionate(s) of heme a. From there, protons are expelled in the P space on heme a oxidation by electrostatic repulsion along a hydrogen bond network of amino acid residues and/or structured water molecules.
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- 2020
20. GBA1 inactivation in oligodendrocytes affects myelination and induces neurodegenerative hallmarks and lipid dyshomeostasis in mice
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Ilaria Gregorio, Loris Russo, Enrica Torretta, Pietro Barbacini, Gabriella Contarini, Giada Pacinelli, Dario Bizzotto, Manuela Moriggi, Paola Braghetta, Francesco Papaleo, Cecilia Gelfi, Enrico Moro, and Matilde Cescon
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Parkinson’s disease ,Gaucher disease ,Oligodendrocyte ,White matter ,β-glucocerebrosidase ,Myelination ,Neurology. Diseases of the nervous system ,RC346-429 ,Geriatrics ,RC952-954.6 - Abstract
Abstract Background Mutations in the β-glucocerebrosidase (GBA1) gene do cause the lysosomal storage Gaucher disease (GD) and are among the most frequent genetic risk factors for Parkinson’s disease (PD). So far, studies on both neuronopathic GD and PD primarily focused on neuronal manifestations, besides the evaluation of microglial and astrocyte implication. White matter alterations were described in the central nervous system of paediatric type 1 GD patients and were suggested to sustain or even play a role in the PD process, although the contribution of oligodendrocytes has been so far scarcely investigated. Methods We exploited a system to study the induction of central myelination in vitro, consisting of Oli-neu cells treated with dibutyryl-cAMP, in order to evaluate the expression levels and function of β-glucocerebrosidase during oligodendrocyte differentiation. Conduritol-B-epoxide, a β-glucocerebrosidase irreversible inhibitor was used to dissect the impact of β-glucocerebrosidase inactivation in the process of myelination, lysosomal degradation and α-synuclein accumulation in vitro. Moreover, to study the role of β-glucocerebrosidase in the white matter in vivo, we developed a novel mouse transgenic line in which β-glucocerebrosidase function is abolished in myelinating glia, by crossing the Cnp1-cre mouse line with a line bearing loxP sequences flanking Gba1 exons 9–11, encoding for β-glucocerebrosidase catalytic domain. Immunofluorescence, western blot and lipidomic analyses were performed in brain samples from wild-type and knockout animals in order to assess the impact of genetic inactivation of β-glucocerebrosidase on myelination and on the onset of early neurodegenerative hallmarks, together with differentiation analysis in primary oligodendrocyte cultures. Results Here we show that β-glucocerebrosidase inactivation in oligodendrocytes induces lysosomal dysfunction and inhibits myelination in vitro. Moreover, oligodendrocyte-specific β-glucocerebrosidase loss-of-function was sufficient to induce in vivo demyelination and early neurodegenerative hallmarks, including axonal degeneration, α-synuclein accumulation and astrogliosis, together with brain lipid dyshomeostasis and functional impairment. Conclusions Our study sheds light on the contribution of oligodendrocytes in GBA1-related diseases and supports the need for better characterizing oligodendrocytes as actors playing a role in neurodegenerative diseases, also pointing at them as potential novel targets to set a brake to disease progression.
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- 2024
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21. The allosteric protein interactions in the proton-motive function of mammalian redox enzymes of the respiratory chain
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Sergio Papa, Francesco Papa, and Giuseppe Capitanio
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0301 basic medicine ,Conformational change ,Stereochemistry ,Protein subunit ,Allosteric regulation ,Respiratory chain ,Cytochromes c1 ,Biochemistry ,Electron Transport Complex IV ,03 medical and health sciences ,chemistry.chemical_compound ,Allosteric Regulation ,Oxidoreductase ,Animals ,Humans ,Heme ,Ubiquinone binding ,chemistry.chemical_classification ,Electron Transport Complex I ,030102 biochemistry & molecular biology ,Proton-Motive Force ,General Medicine ,Cytochromes b ,030104 developmental biology ,Heme A ,chemistry - Abstract
Insight into mammalian respiratory complexes defines the role of allosteric protein interactions in their proton-motive activity. In cytochrome c oxidase (CxIV) conformational change of subunit I, caused by O2 binding to heme a32+-CuB+ and reduction, and stereochemical transitions coupled to oxidation/reduction of heme a and CuA, combined with electrostatic effects, determine the proton pumping activity. In ubiquinone-cytochrome c oxidoreductase (CxIII) conformational movement of Fe-S protein between cytochromes b and c1 is the key element of the proton-motive activity. In NADH-ubiquinone oxidoreductase (CxI) ubiquinone binding and reduction result in conformational changes of subunits in the quinone reaction structure which initiate proton pumping.
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- 2021
22. An Extreme-Edge TCN-Based Low-Latency Collision-Avoidance Safety System for Industrial Machinery
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Marcello Zanghieri, Fabrizio Indirli, Antonio Latella, Giacomo Michele Puglia, Felice Tecce, Francesco Papariello, Giulio Urlini, Luca Benini, and Francesco Conti
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Collision avoidance ,embedded systems ,incremental learning ,microcontroller ,public dataset ,real-time ,Electrical engineering. Electronics. Nuclear engineering ,TK1-9971 - Abstract
Modern manufacturing industry relies on complex machinery that requires skills, attention, and precise safety certifications. Protecting operators in the machine’s surroundings while at the same time reducing the impact on the normal workflow is a major challenge. In particular, safety systems based on proximity sensing of humans or obstacles require that the detection is accurate, low-latency, and robust against variations in environmental conditions. This work proposes a functional safety solution for collision avoidance relying on Ultrasounds (US) and a Temporal Convolutional Network (TCN) suitable for deployment directly at the edge on a low-power Microcontroller Unit (MCU). The setup allowed to acquire a sensor-fusion dataset with 9 US sensors mounted on a real industrial woodworking machine. Applying incremental training, the proposed TCN achieved sensitivity 90.5%, specificity 95.2%, and AUROC 0.972 on data affected by the typical acoustic noise of an industrial facility, an accuracy comparable with the State-of-the-Art (SoA). Deployment on an STM32H7 MCU yielded a memory footprint of 560 B (3× less than SoA), with an extremely low latency of 5.0 ms and an energy consumption of 8.2 mJ per inference (both >2.3× less than SoA). The proposed solution increases its robustness against acoustic noise by leveraging new data, and it fits the resource budget of real-time operation execution on resource-constrained embedded devices. It is thus promising for generalization to different industrial settings and for scale-up to wider monitored spaces.
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- 2024
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23. The mechanism of coupling between oxido-reduction and proton translocation in respiratory chain enzymes
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Giuseppe Capitanio, Sergio Papa, and Francesco Papa
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0301 basic medicine ,chemistry.chemical_classification ,biology ,Allosteric regulation ,Respiratory chain ,Redox ,General Biochemistry, Genetics and Molecular Biology ,Transmembrane protein ,03 medical and health sciences ,Electron transfer ,030104 developmental biology ,Membrane ,Biochemistry ,chemistry ,Oxidoreductase ,Biophysics ,biology.protein ,Cytochrome c oxidase ,General Agricultural and Biological Sciences - Abstract
The respiratory chain of mitochondria and bacteria is made up of a set of membrane-associated enzyme complexes which catalyse sequential, stepwise transfer of reducing equivalents from substrates to oxygen and convert redox energy into a transmembrane protonmotive force (PMF) by proton translocation from a negative (N) to a positive (P) aqueous phase separated by the coupling membrane. There are three basic mechanisms by which a membrane-associated redox enzyme can generate a PMF. These are membrane anisotropic arrangement of the primary redox catalysis with: (i) vectorial electron transfer by redox metal centres from the P to the N side of the membrane; (ii) hydrogen transfer by movement of quinones across the membrane, from a reduction site at the N side to an oxidation site at the P side; (iii) a different type of mechanism based on co-operative allosteric linkage between electron transfer at the metal redox centres and transmembrane electrogenic proton translocation by apoproteins. The results of advanced experimental and theoretical analyses and in particular X-ray crystallography show that these three mechanisms contribute differently to the protonmotive activity of cytochrome c oxidase, ubiquinone-cytochrome c oxidoreductase and NADH-ubiquinone oxidoreductase of the respiratory chain. This review considers the main features, recent experimental advances and still unresolved problems in the molecular/atomic mechanism of coupling between the transfer of reducing equivalents and proton translocation in these three protonmotive redox complexes.
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- 2017
24. All trans retinoic acid depresses the content and activity of the mitochondrial ATP synthase in human keratinocytes
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Antonio Gnoni, Francesco Papa, Rosa Lippolis, Nicola Sardaro, and Salvatore Scacco
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Keratinocytes ,Proteomics ,0301 basic medicine ,Protein subunit ,Biophysics ,Retinoic acid ,Down-Regulation ,Tretinoin ,Oxidative phosphorylation ,Inhibitory postsynaptic potential ,Biochemistry ,03 medical and health sciences ,chemistry.chemical_compound ,0302 clinical medicine ,Humans ,Molecular Biology ,Cells, Cultured ,Cell Proliferation ,chemistry.chemical_classification ,Dose-Response Relationship, Drug ,Mass spectrometry ,ATP synthase ,biology ,All-trans retinoic acid ,Cell growth ,Human keratinocytes ,Cell Biology ,Mitochondrial Proton-Translocating ATPases ,Molecular biology ,Enzyme Activation ,030104 developmental biology ,Enzyme ,chemistry ,030220 oncology & carcinogenesis ,biology.protein - Abstract
Proteomic analysis shows that treatment of keratinocytes cultures with all trans retinoic acid (ATRA), under condition in which it inhibits cell growth, results in marked decrease of the level of the F1-beta subunit of the catalytic sector of the mitochondrial FoF1 ATP synthase complex. Enzymatic analysis shows in ATRA-treated keratinocytes a consistent depression of the ATPase activity, with decreased olygomycin sensitivity, indicating an overall alteration of the ATP synthase complex. These findings, together with the previously reported inhibition of respiratory complex I, show that depression of the activity of oxidative phosphorylation enzymes is involved in the cell growth inhibitory action of ATRA. (C) 2016 Elsevier Inc. All rights reserved.
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- 2017
25. Decreased amount of vimentin N-terminal truncated proteolytic products in parkin-mutant skin fibroblasts
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Francesco Papa, Sergio Papa, Tiziana Cocco, Maria Fiorella Mazzeo, Rosa Lippolis, Antonio Rosato, Anna Ferretta, Consiglia Pacelli, Salvatore Scacco, and Rosa Anna Siciliano
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0301 basic medicine ,Parkinson's disease Human skin fibroblasts Two-dimensional gel electrophoresis Mass spectrometry Proteomics ,Adult ,Proteomics ,Ubiquitin-Protein Ligases ,Mutant ,Biophysics ,Vimentin ,macromolecular substances ,Biochemistry ,Parkin ,Pathogenesis ,03 medical and health sciences ,0302 clinical medicine ,Humans ,Protein Isoforms ,Cytoskeleton ,Intermediate filament ,Molecular Biology ,Cells, Cultured ,Skin ,Two-dimensional gel electrophoresis ,biology ,Chemistry ,Parkinson Disease ,Cell Biology ,Fibroblasts ,Middle Aged ,Cell biology ,030104 developmental biology ,030220 oncology & carcinogenesis ,Mutation ,Proteolysis ,biology.protein ,Female ,Function (biology) - Abstract
Vimentin, a member of cytoskeleton intermediate filaments proteins, plays a critical role in cell structure and dynamics. The present proteomic study reveals reduced amount of six different lengths, N-terminal truncated proteolytic products of vimentin, in the primary skin fibroblasts from two unrelated PD patients, as compared to control fibroblasts. The decreased amount of N-terminal truncated forms of vimentin in parkin-mutant fibroblasts, could contribute to impairment of cellular function, potentially contributing to the pathogenesis of Parkinson disease.
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- 2019
26. Costruire un nuovo futuro del lavoro: Videomessaggio in occasione della 109a Conferenza internazionale del lavoro.
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Francesco, Papa
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- 2021
27. "Ricordo, passione conforto".
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Francesco, Papa
- Abstract
Copyright of Medicina e Morale is the property of PAGEPress and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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- 2021
28. Proteomics pattern associated with gingival oral squamous cell carcinoma and epulis: A case analysis
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Francesco Inchingolo, Maria Fiorella Mazzeo, Rosa Anna Siciliano, Francesco Papa, Rosa Lippolis, and Salvatore Scacco
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0301 basic medicine ,Gel electrophoresis ,Pathology ,medicine.medical_specialty ,business.industry ,Epulis ,Significant difference ,Early detection ,Proteomic analysis ,Oral cavity ,Proteomics ,medicine.disease ,03 medical and health sciences ,stomatognathic diseases ,030104 developmental biology ,0302 clinical medicine ,Otorhinolaryngology ,Oral squamous cell carcinoma ,030220 oncology & carcinogenesis ,Medicine ,Basal cell ,business ,Biomarkers ,Case analysis - Abstract
Objectives Oral squamous cell carcinoma (OSCC) is the most common epithelial malignant neoplasm affecting the oral cavity. OSCC can mimic oral lesions of inflammatory origin with benign features, often leading to delay in diagnosis and treatment. Early detection is important to greatly increase the chances of a successful treatment. The present study reports a proteomic analysis of a gingival oral squamous cell carcinoma (G-OSCC) and an epulis. Materials and methods Normal mucosae tissue, G-OSCC tissue, and epulis tissue as a comparative sample of benign nature were collected and immediately frozen in liquid nitrogen. Tissue-extracted proteins were separated by two-dimensional gel electrophoresis and subjected to image analysis. Proteins that showed a significant difference in the expression level in the G-OSCC tissue were identified by the nano-ESI-HPLC-MS/MS experiment and database searchi. Results and conclusion The proteomic analysis of G-OSCC tissue enabled the identification of proteins that are potentially related to the disease; these proteins can be considered as signature molecules for diagnostic and prognostic tumor markers.
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- 2018
29. Altered protein expression pattern in skin fibroblasts from parkin -mutant early-onset Parkinson's disease patients
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Rosa Lippolis, Anna Ferretta, Francesco Papa, Consiglia Pacelli, Antonio Gaballo, Salvatore Scacco, Claudia Dell'Aquila, Maria Fiorella Mazzeo, Michele De Mari, Tiziana Cocco, Sergio Papa, and Rosa Anna Siciliano
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Proteomics ,Calcium metabolism ,Parkinson's disease ,Mass spectrometry ,Dopaminergic ,Mutant ,Human skin fibroblasts ,Substantia nigra ,Biology ,medicine.disease ,medicine.disease_cause ,Molecular biology ,Parkin ,Two-dimensional gel electrophoresis ,Cancer research ,medicine ,Molecular Medicine ,Cytoskeleton ,Molecular Biology ,Oxidative stress - Abstract
Parkinson's disease (PD) is the most common neurodegenerative movement disorder caused primarily by selective degeneration of the dopaminergic neurons in substantia nigra. In this work the proteomes extracted from primary fibroblasts of two unrelated, hereditary cases of PD patients, with different parkin mutations, were compared with the proteomes extracted from commercial adult normal human dermal fibroblasts (NHDF) and primary fibroblasts from the healthy mother of one of the two patients. The results show that the fibroblasts from the two different cases of parkin -mutant patients display analogous alterations in the expression level of proteins involved in different cellular functions, like cytoskeleton structure–dynamics, calcium homeostasis, oxidative stress response, protein and RNA processing.
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- 2015
30. Precision Agriculture Applied to Harvesting Operations through the Exploitation of Numerical Simulation
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Federico Cheli, Ahmed Khaled Mohamed Abdelaziz, Stefano Arrigoni, Francesco Paparazzo, and Marco Pezzola
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precision agriculture ,harvesting ,path planning ,path tracking ,CarMaker ,agricultural simulator ,Chemical technology ,TP1-1185 - Abstract
When it comes to harvesting operations, precision agriculture needs to consider both combine harvester technology and the precise execution of the process to eliminate harvest losses and minimize out-of-work time. This work aims to propose a complete control framework defined by a two-layer-based algorithm and a simulation environment suitable for quantitative harvest loss, time, and consumption analyses. In detail, the path-planning layer shows suitable harvesting techniques considering field boundaries and irregularities, while the path-tracking layer presents a vision-guided Stanley Lateral Controller. In order to validate the developed control framework, challenging driving scenarios were created using IPG-CarMaker software to emulate wheat harvesting operations. Results showed the effectiveness of the designed controller to follow the reference trajectory under regular field conditions with zero harvest waste and minimum out-of-work time. Whereas, in presence of harsh road irregularities, the reference trajectory should be re-planned by either selecting an alternative harvesting method or overlapping the harvester header by some distance to avoid missing crops. Quantitative and qualitative comparisons between the two harvesting techniques as well as a relationship between the level of irregularities and the required overlap will be presented. Eventually, a Driver-in-the-loop (DIL) framework is proposed as a methodology to compare human and autonomous driving.
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- 2024
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31. Modeling and Measurements of Heat/Mass Transfer in a Linear Turbine Cascade
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Francesco Papa, Richard J Goldstein, and U. Madanan
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Materials science ,Turbine blade ,Turbulence ,020209 energy ,Mechanical Engineering ,Thermodynamics ,02 engineering and technology ,Heat transfer coefficient ,Mechanics ,01 natural sciences ,Transition modeling ,010305 fluids & plasmas ,law.invention ,law ,Mass transfer ,0103 physical sciences ,Heat transfer ,0202 electrical engineering, electronic engineering, information engineering ,Turbocharger ,Wind tunnel - Abstract
Measurements of the mass/heat transfer coefficients on the blade and end wall surfaces of a linear turbine cascade are compared to numerical predictions using the standard shear stress transport (SST) closure and the SST model in combination with the Reθ–γ transition model (SST-TRANS). Experiments were carried out in a wind tunnel test section composed of five large-scale turbine blades, using the naphthalene sublimation technique. Two cases were tested, with exit Reynolds number of 600,000 and inlet turbulence values of 0.2% and 4%, respectively. The main secondary flow features, consisting of the horseshoe vortex system, the passage vortex, and the corner vortices, are identified and their influence on heat/mass transfer is analyzed. Numerical simulations were carried out to match the conditions of the experiments. Results show that large improvements are obtained with the introduction of the Reθ–γ transition model. In particular, excellent agreement with the experiments is found, for the whole spanwise extension of the blade, on the pressure surface. On the suction surface, performance is very good in the highly three-dimensional region close to the end wall, but some weaknesses appear in predicting the location of transition in the two-dimensional region. On the end wall surface, the SST model in combination with the transition model produces satisfactory results, greatly improved compared to the standard SST model.
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- 2017
32. Regulation of the biogenesis of OXPHOS complexes in cell transition from replicating to quiescent state
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Loris Micelli, Sergio Papa, Giuliano Gattoni, Francesco Papa, Salvatore Scacco, Romina Ficarella, Anna Signorile, Arcangela Santeramo, and Domenico De Rasmo
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Cell Biology ,Biology ,TFAM ,CREB ,Cell biology ,chemistry.chemical_compound ,Biochemistry ,chemistry ,Transcription Coactivator ,Coactivator ,biology.protein ,Phosphorylation ,NRF1 ,Protein kinase A ,Adenosine triphosphate ,Molecular Biology - Abstract
A study is presented on the expression of mitochondrial oxidative phosphorylation complexes in exponentially growing and serum-starved, quiescent human fibroblast cultures. The functional levels of respiratory complexes I and III and complex V (adenosine triphosphate (ATP) synthase) were found to be severely depressed in serum-starved fibroblasts. The depression of oxidative phosphorylation system (OXPHOS) complexes was associated with reduced levels of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α) and the down-stream nuclear respiratory factor 1 (NRF1) and mitochondrial transcription factors (TFAM). In serum-starved fibroblasts decrease of the catalytic activity of AMP cyclic dependent protein kinase (PKA) and phosphorylation of cAMP response element-binding protein (CREB), the transcription coactivator of the PGC-1α gene, was found. Hydroxytyrosol prevented the decline in the expression of the PGC-1α transcription cascade of OXPHOS complexes in serum-starved fibroblast cultures. The positive effect of HT was associated with activation of PKA and CREB phosphorylation. These results show involvement of PKA, CREB and PGC-1α in the regulation of OXPHOS in cell transition from the replicating to the quiescent state.
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- 2014
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33. Cytokine Gene Polymorphisms Associate with Microbiogical Agents in Periodontal Disease: Our Experience
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Francesco Inchingolo, Andrea Ballini, Gianna Dipalma, Salvatore Scacco, Maria Franca Coscia, Danila De Vito, Francesco Papa, Stefania Cantore, and Rosanna Mirgaldi
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Adult ,Male ,Genetic factors ,Genotype ,medicine.medical_treatment ,Interleukin-1beta ,Single-nucleotide polymorphism ,Biology ,Polymorphism, Single Nucleotide ,Severe periodontitis ,Risk Factors ,Interleukin-1alpha ,medicine ,Humans ,Genetic Predisposition to Disease ,Allele ,Alleles ,Genetic Association Studies ,Periodontal Diseases ,Periodontitis ,Single nucleotide polymorphisms ,General Medicine ,medicine.disease ,Oral Microbiology ,Cytokine ,Case-Control Studies ,Oral microbiology ,Immunology ,Population study ,Female ,Periodontal disease ,Research Paper ,Interleukin-1 - Abstract
Periodontics has evolved from a simplistic model to a more complex interplay between infection and host response. Genetic factors have been a new addition to the list of risk factors for periodontal diseases. The processes leading to destruction and regeneration of the destroyed tissues are of great interest to both researchers and clinicians. The selective susceptibility of subjects for periodontitis has remained an enigma and wide varieties of risk factors have been implicated for the manifestation and progression of periodontitis. Emerging pathway models suggest that gene-environment interactions are etiologically important in disease pathogenesis. The current practical utility of genetic knowledge in periodontitis is limited. Allelic variants at multiple gene loci probably influence periodontitis susceptibility. The pro-inflammatory cytokine interleukin-1 (IL-1) is a key modulator of host responses to microbial infection and a major modulator of extracellular matrix catabolism and bone resorption, and polymorphisms in the IL-1 gene cluster have been associated with an increased risk of developing severe adult periodontitis. The aim of this study was to test if polymorphisms of genes of IL-1α+4845 and IL-1β +3954 were linked with periodontitis, in a case-control study population, delimited to a specific geographic area, in association with microbiological findings. The polymorphisms observed in IL-1α+4845 and IL-1β+3954 single nucleotide polymorphisms (SNPs), was significantly different among the study groups (healthy controls, mild, moderate and severe periodontitis with p
- Published
- 2014
34. Long-term, basin-scale salinity impacts from desalination in the Arabian/Persian Gulf
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Francesco Paparella, Daniele D’Agostino, and John A. Burt
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Medicine ,Science - Abstract
Abstract The nations on the shoreline of the Arabian/Persian Gulf are the world’s largest users of desalination technologies, which are essential to meet their freshwater needs. Desalinated freshwater production is projected to rapidly increase in future decades. Thus, concerns have been raised that desalination activities may result in non-negligible long-term, basin-wide increases of salinity, which would have widespread detrimental effects on the Gulf marine ecosystems, with ripple effects on fisheries, as well as impacting the desalination activities themselves. We find that current yearly desalinated freshwater production amounts to about 2% of the net yearly evaporation from the Gulf. Projections to 2050 bring this value to 8%, leading to the possibility that, later in the second half of the century, desalinated freshwater production may exceed 10% of net evaporation, an amount which is comparable to interannual fluctuations in net evaporation. With the help of a model we examine several climatological scenarios, and we find that, under IPCC’s SSP5-8.5 worst-case scenarios, end-of-century increases in air temperature may result in salinity increases comparable or larger to those produced by desalination activities. The same scenario suggests a reduced evaporation and an increased precipitation, which would have a mitigating effect. Finally we find that, owing to a strong overturning circulation, high-salinity waters are quickly flushed through the Strait of Hormuz. Thus, even in the worst-case scenarios, basin-scale salinity increases are unlikely to exceed 1 psu, and, under less extreme hypothesis, will likely remain well below 0.5 psu, levels that have negligible environmental implications at the basin-wide scale.
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- 2022
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35. In dialogo con la realtà senza pregiudizi: Il discorso di papa Francesco ad Aggiornamenti Sociali.
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Francesco, Papa
- Published
- 2020
36. The mechanism of alternative splicing of the X-linked NDUFB11 gene of the respiratory chain complex I, impact of rotenone treatment in neuroblastoma cells
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Francesco Papa, Francesca Paola Lorusso, Anna Maria Sardanelli, Patrizio Panelli, Alessandro Stella, Damiano Panelli, Sergio Papa, and Massimo Caputi
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Gene isoform ,NDUFB11 ,Protein subunit ,Biophysics ,Exonic splicing enhancer ,Apoptosis ,Biology ,Biochemistry ,Neuroblastoma ,Exon ,Genes, X-Linked ,Structural Biology ,Cell Line, Tumor ,Rotenone ,Genetics ,Humans ,Protein Isoforms ,Molecular Biology ,Gene ,Electron Transport Complex I ,Alternative splicing ,Exons ,Molecular biology ,Alternative Splicing ,HEK293 Cells ,Mitochondrial respiratory chain ,Gene Expression Regulation ,HeLa Cells - Abstract
A study is presented on the regulation of alternative splicing (AS) of the Ndufb11 gene of complex I of the mitochondrial respiratory chain and the impact on this process of rotenone treatment in neuroblastoma cells. In physiological conditions the Ndufb11 gene produces at high level a short transcript isoform encoding for a 153 aa protein. This subunit is essential for the assembly of a functional and stable mammalian complex I. The gene produces also, at low level, a longer transcript isoform encoding for a 163 aa protein whose role is unknown. Evidence is presented here showing that the level of the two isoforms is regulated by three DGGGD ESS elements located in exon 2 which can bind the hnRNPH1 protein. In neuronal cells rotenone treatment affects the Ndufb11 alternative splicing pathway, with the increase of the 163/153 mRNAs ratio. This effect appears to be due to the down-regulation of the hnRNPH1 protein. Since rotenone induces apoptosis in neuronal cells, the post-transcriptional regulation of the Ndufb11 gene can be involved in the programmed cell death process.
- Published
- 2013
37. Rhythmic oscillations in the midbrain dopaminergic nuclei in mice
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Virginie J. Oberto, Jumpei Matsumoto, Marco N. Pompili, Ralitsa Todorova, Francesco Papaleo, Hisao Nishijo, Laurent Venance, Marie Vandecasteele, and Sidney I. Wiener
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awake delta rhythm ,substantia nigra pars compacta ,ventral tegmental area ,slow rhythm ,4 Hz ,Neurosciences. Biological psychiatry. Neuropsychiatry ,RC321-571 - Abstract
IntroductionDopamine release in the forebrain by midbrain ventral tegmental nucleus (VTA) and substantia nigra pars compacta (SNc) neurons is implicated in reward processing, goal-directed learning, and decision-making. Rhythmic oscillations of neural excitability underlie coordination of network processing, and have been reported in these dopaminergic nuclei at several frequency bands. This paper provides a comparative characterization of several frequencies of oscillations of local field potential and single unit activity, highlighting some behavioral correlates.MethodsWe recorded from optogenetically identified dopaminergic sites in four mice training in operant olfactory and visual discrimination tasks.ResultsRayleigh and Pairwise Phase Consistency (PPC) analyses revealed some VTA/SNc neurons phase-locked to each frequency range, with fast spiking interneurons (FSIs) prevalent at 1–2.5 Hz (slow) and 4 Hz bands, and dopaminergic neurons predominant in the theta band. More FSIs than dopaminergic neurons were phase-locked in the slow and 4 Hz bands during many task events. The highest incidence of phase-locking in neurons was in the slow and 4 Hz bands, and occurred during the delay between the operant choice and trial outcome (reward or punishment) signals.DiscussionThese data provide a basis for further examination of rhythmic coordination of activity of dopaminergic nuclei with other brain structures, and its impact for adaptive behavior.
- Published
- 2023
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38. The mechanism of coupling between oxido-reduction and proton translocation in respiratory chain enzymes
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Sergio, Papa, Giuseppe, Capitanio, and Francesco, Papa
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Electron Transport ,Bacteria ,Animals ,Protons ,Oxidation-Reduction ,Enzymes ,Mitochondria - Abstract
The respiratory chain of mitochondria and bacteria is made up of a set of membrane-associated enzyme complexes which catalyse sequential, stepwise transfer of reducing equivalents from substrates to oxygen and convert redox energy into a transmembrane protonmotive force (PMF) by proton translocation from a negative (N) to a positive (P) aqueous phase separated by the coupling membrane. There are three basic mechanisms by which a membrane-associated redox enzyme can generate a PMF. These are membrane anisotropic arrangement of the primary redox catalysis with: (i) vectorial electron transfer by redox metal centres from the P to the N side of the membrane; (ii) hydrogen transfer by movement of quinones across the membrane, from a reduction site at the N side to an oxidation site at the P side; (iii) a different type of mechanism based on co-operative allosteric linkage between electron transfer at the metal redox centres and transmembrane electrogenic proton translocation by apoproteins. The results of advanced experimental and theoretical analyses and in particular X-ray crystallography show that these three mechanisms contribute differently to the protonmotive activity of cytochrome c oxidase, ubiquinone-cytochrome c oxidoreductase and NADH-ubiquinone oxidoreductase of the respiratory chain. This review considers the main features, recent experimental advances and still unresolved problems in the molecular/atomic mechanism of coupling between the transfer of reducing equivalents and proton translocation in these three protonmotive redox complexes.
- Published
- 2016
39. Effect of all-trans retinoic acid on post translational regulation and subcellular distribution of the oncosuppressor GRIM 19
- Author
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Francesco Papa, Nicola Sardaro, Rosa Lippolis, and Sergio Papa.
- Subjects
body regions ,animal structures ,fungi ,Atra ,Grim 19 - Abstract
GRIM-19 is an oncosuppressor which antagonizes the oncogene Stat 3. GRIM19 is partitioned between the nucleus and mitochondria where it appears as a subunit of respiratory complex I. Our group has studied the impact of the chemiotherapic agent all-trans- retinoic acid (ATRA) on the subcellular distribution of GRIM-19. The results show that ATRA treatment of keratinocytes results in increased level of GRIM-19 and other subunits of complex I, in particular of their carbonylated forms, associated with inhibition of its enzymatic activity. In keratinocytes ATRA-promoted phosphatase activity appears to control the proteostasis and activity of complex I. Furthermore, the oncogene STAT-3, besides being localized in the nucleus, has also been found in mitochondria where it interacts with GRIM 19. Thus, perturbation of the interplay of GRIM 19 with factors, associated with complex I, can be involved in the ATRA suppression of keratinocyte growth.
- Published
- 2016
40. Respiratory chain complex I, a main regulatory target of the cAMP/PKA pathway is defective in different human diseases
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Zuzana Technikova-Dobrova, Sergio Papa, Domenico De Rasmo, Vittoria Petruzzella, Damiano Panelli, Francesco Papa, Giuseppe Palmisano, Anna Maria Sardanelli, Anna Signorile, Antonio Gnoni, Salvatore Scacco, and Loris Micelli
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cAMP/PKA pathway ,NDUFS4 ,Biophysics ,Mitochondrial diseases ,Biology ,Biochemistry ,chemistry.chemical_compound ,Structural Biology ,Oxidoreductase ,Complex I ,Cyclic AMP ,Genetics ,Humans ,Genetic Predisposition to Disease ,Phosphorylation ,Molecular Biology ,chemistry.chemical_classification ,Electron Transport Complex I ,Superoxide ,NADH Dehydrogenase ,Cell Biology ,Cyclic AMP-Dependent Protein Kinases ,Respiratory chain complex I ,Cell biology ,Mitochondrial respiratory chain ,chemistry ,Mutation ,Nervous System Diseases ,Signal transduction ,Biogenesis ,Signal Transduction - Abstract
In mammals, complex I (NADH-ubiquinone oxidoreductase) of the mitochondrial respiratory chain has 31 supernumerary subunits in addition to the 14 conserved from prokaryotes to humans. Multiplicity of structural protein components, as well as of biogenesis factors, makes complex I a sensible pace-maker of mitochondrial respiration. The work reviewed here shows that the cAMP/PKA pathway regulates the biogenesis, assembly and catalytic activity of complex I and mitochondrial oxygen superoxide production. The structural, functional and regulatory complexity of complex I, renders it particularly vulnerable to genetic and sporadic pathological factors. Complex I dysfunction has, indeed, been found, to be associated with several human diseases. Knowledge of the pathogenetic mechanisms of these diseases can help to develop new therapeutic strategies. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
- Published
- 2011
41. Rat Embryo Exposure to All-Trans Retinoic Acid Results in Postnatal Oxidative Damage of Respiratory Complex I in the Cerebellum
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Anna Signorile, Maria Rosaria Carratù, Salvatore Scacco, Francesco Papa, Domenico De Rasmo, Pietro Borracci, Nicola Sardaro, and Sergio Papa
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Male ,medicine.medical_specialty ,Cerebellum ,Offspring ,Respiratory chain ,Retinoic acid ,Tretinoin ,Biology ,Random Allocation ,chemistry.chemical_compound ,Pregnancy ,Respiratory Complex I ,Internal medicine ,medicine ,Animals ,neoplasms ,Pharmacology ,chemistry.chemical_classification ,Electron Transport Complex I ,organic chemicals ,Embryo ,Embryonic stem cell ,biological factors ,Rats ,Oxidative Stress ,Endocrinology ,medicine.anatomical_structure ,Enzyme ,Animals, Newborn ,Biochemistry ,chemistry ,Prenatal Exposure Delayed Effects ,Molecular Medicine ,Female - Abstract
The results of the present work show that the exposure of pregnant rats to low doses of all-trans-retinoic acid (ATRA) (2.5 mg/kg body weight) results in postnatal dysfunction of complex I of the respiratory chain in the cerebellum of the offspring. ATRA had no effect on the postnatal expression of complex I and did not exert any direct inhibitory effect on the enzymatic activity of the complex. The ATRA embryonic exposure resulted, however, in a marked increase in the level of carbonylated proteins in the mitochondrial fraction of the cerebellum, in particular of complex I subunits. The postnatal increase of the carbonylated proteins correlated directly with the inhibition of the activity of complex I. ATRA had, on the other hand, no effect on oxygen free-radical scavengers. It is proposed that embryonic exposure to ATRA results in impairment of protein surveillance in the cerebellum, which persists after birth and results in accumulation of oxidatively damaged complex I.
- Published
- 2011
42. The β-adrenoceptor agonist isoproterenol promotes the activity of respiratory chain complex I and lowers cellular reactive oxygen species in fibroblasts and heart myoblasts
- Author
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Consiglia Pacelli, Loris Micelli, Arcangela Santeramo, Tiziana Cocco, Francesco Papa, M Scivetti, Maria Larizza, Nicola Sardaro, Domenico De Rasmo, Giuliano Gattoni, Anna Signorile, and Serena Milano
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Agonist ,medicine.medical_specialty ,medicine.drug_class ,Respiratory chain ,Mitochondrion ,Biology ,chemistry.chemical_compound ,Isoprenaline ,Internal medicine ,Cyclic AMP ,medicine ,Humans ,Phosphorylation ,Fibroblast ,Cells, Cultured ,Pharmacology ,chemistry.chemical_classification ,Reactive oxygen species ,Electron Transport Complex I ,Infant, Newborn ,Isoproterenol ,Okadaic acid ,Adrenergic beta-Agonists ,Fibroblasts ,Mitochondria ,Endocrinology ,medicine.anatomical_structure ,chemistry ,Reactive Oxygen Species ,Myoblasts, Cardiac ,medicine.drug - Abstract
A study is presented on the effect of the β-adrenoceptor agonist isoproterenol on mitochondrial oxygen metabolism in fibroblast and heart myoblast cultures. Isoproterenol treatment of serum-limited fibroblasts and proliferating myoblasts results in the promotion of mitochondrial complex I activity and decrease of the cellular level of reactive oxygen species. These effects of isoproterenol are associated with cAMP-dependent phosphorylation of complex I subunit(s). Addition of okadaic acid, inhibitor of protein phosphatase(s), reverses the decline of complex I activity in serum-limited fibroblast cultures and activates the complex in proliferating myoblast cultures. The effects of isoproterenol on complex I activity and reactive oxygen species balance can contribute to the therapeutic effect of the drug.
- Published
- 2011
43. cAMP-dependent protein kinase regulates post-translational processing and expression of complex I subunits in mammalian cells
- Author
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Emilio Roca, Raffaella Scaringi, Francesco Papa, Raffaella Trentadue, Sergio Papa, Domenico De Rasmo, Maria Larizza, Arcangela Santeramo, Salvatore Scacco, Damiano Panelli, Anna Signorile, and Annarita Nicastro
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Protein subunit ,Molecular Sequence Data ,Respiratory chain ,Biophysics ,In Vitro Techniques ,All trans retinoic acid ,CREB ,Models, Biological ,Biochemistry ,Mice ,Cell growth ,Complex I ,Animals ,Humans ,Protein phosphorylation ,PKA ,Amino Acid Sequence ,Phosphorylation ,Cyclic AMP Response Element-Binding Protein ,Protein kinase A ,Transcription factor ,Cells, Cultured ,Electron Transport Complex I ,Mitochondrial import ,biology ,NADH Dehydrogenase ,Protein phosphatase 2 ,Cell Biology ,Cyclic AMP-Dependent Protein Kinases ,Rats ,Cell biology ,Protein Subunits ,cAMP cascade ,biology.protein ,Protein Processing, Post-Translational - Abstract
Work is presented on the role of cAMP-dependent protein phosphorylation in post-translational processing and biosynthesis of complex I subunits in mammalian cell cultures. PKA-mediated phosphorylation of the NDUFS4 subunit of complex I promotes in cell cultures in vivo import/maturation in mitochondria of the precursor of this protein. The import promotion appears to be associated with the observed cAMP-dependent stimulation of the catalytic activity of complex I. These effects of PKA are counteracted by activation of protein phosphatase(s). PKA and the transcription factor CREB play a critical role in the biosynthesis of complex I subunits. CREB phosphorylation, by PKA and/or CaMKs, activates at nuclear and mitochondrial level a transcriptional regulatory cascade which promotes the concerted expression of nuclear and mitochondrial encoded subunits of complex I and other respiratory chain proteins.
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- 2010
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44. Pathogenetic mechanisms in hereditary dysfunctions of complex I of the respiratory chain in neurological diseases
- Author
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Nazzareno Capitanio, M Scivetti, Giuseppe De Michele, Damiano Panelli, Claudia Piccoli, Teresa Rizza, Raffaella Trentadue, Arcangela Iuso, Francesco Papa, Domenico De Rasmo, Vittoria Petruzzella, Enrico Bertini, Salvatore Scacco, Anna Maria Sardanelli, Rita Vitale, and Sergio Papa
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Models, Molecular ,NDUFS4 ,Molecular Sequence Data ,Molecular Conformation ,Biophysics ,Respiratory chain ,PINK1 ,Neurological disorder ,Biology ,DNA, Mitochondrial ,Biochemistry ,Familiar Parkinsonism ,Mitochondrial Encephalomyopathies ,Complex I ,medicine ,Humans ,NDUFS1 ,Amino Acid Sequence ,Genetics ,Electron Transport Complex I ,Epilepsy ,mtDNA mutation ,NADH Dehydrogenase ,Parkinson Disease ,Cell Biology ,medicine.disease ,Chronic epilepsy ,ROS balance ,Mutation ,Hereditary Diseases ,Nervous System Diseases ,Reactive Oxygen Species ,Mitochondrial encephalopathy - Abstract
This paper covers genetic and biochemical aspects of mitochondrial bioenergetics dysfunction in hereditary neurological disorders associated with complex I defects. Three types of hereditary complex I dysfunction are dealt with: (i) homozygous mutations in the nuclear genes NDUFS1 and NDUFS4 of complex I, associated with mitochondrial encephalopathy; (ii) a recessive hereditary epileptic neurological disorder associated with enhanced proteolytic degradation of complex I; (iii) homoplasmic mutations in the ND5 and ND6 mitochondrial genes of the complex, cohexistent with mutation in the nuclear PINK1 gene in familial Parkinsonism. The genetic and biochemical data examined highlight different mechanisms by which mitochondrial bioenergetics is altered in these hereditary defects of complex I. This knowledge, besides clarifying molecular aspects of the pathogenesis of hereditary diseases, can also provide hints for understanding the involvement of complex I in sporadic neurological disorders and aging, as well as for developing therapeutical strategies.
- Published
- 2009
45. In Vitro Stem Cell Cultures from Human Dental Pulp and Periodontal Ligament: New Prospects in Dentistry
- Author
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G. De Frenza, Stefano Tetè, Filiberto Mastrangelo, Maria Grano, Francesco Papa, Felice Roberto Grassi, Stefania Cantore, and Andrea Ballini
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Periodontal ligament stem cells ,Periodontal Ligament ,Cellular differentiation ,Immunology ,Dentistry ,Biology ,Regenerative medicine ,03 medical and health sciences ,0302 clinical medicine ,stomatognathic system ,Dental pulp stem cells ,Animals ,Humans ,Immunology and Allergy ,Periodontal fiber ,Bone regeneration ,Cells, Cultured ,Dental Pulp ,Pharmacology ,business.industry ,Stem Cells ,Cell Differentiation ,Transplantation ,030220 oncology & carcinogenesis ,Stem cell ,business ,Stem Cell Transplantation ,030215 immunology - Abstract
In spite of the vast knowledge of tooth development and of the various kinds of specialized bone/tooth-associated cells, the characteristics and properties of their precursor cell populations present in the postnatal organism are little known, as is their possible therapeutic use. Taken together dental pulp stem cells (DPSCs) and periodontal ligament stem cells (PDLSCs) possess stem-cell-like qualities, including self-renewal capability and multi-lineage differentiation. Regenerative medicine is based on stem cells, signals and scaffolds. Transplantation of those cells, which can be obtained from an easily accessible tissue resource and expanded in vitro, holds promise as a therapeutic approach for reconstruction of tissues and bone in vivo.
- Published
- 2007
46. Regulation by the cAMP Cascade of Oxygen Free Radical Balance in Mammalian Cells
- Author
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Tiziana Cocco, Anna Maria Sardanelli, Sergio Papa, Nazzareno Capitanio, Claudia Piccoli, Salvatore Scacco, Francesco Bellomo, Annamaria D'Aprile, Domenico Boffoli, Antonio Gaballo, Rosella Scrima, Francesco Papa, and Anna Signorile
- Subjects
Aging ,Free Radicals ,Physiology ,Clinical Biochemistry ,Kinases ,Biochemistry ,Mice ,chemistry.chemical_compound ,Cytosol ,Oxidoreductase ,Cyclic AMP ,Animals ,Humans ,Protein kinase A ,Molecular Biology ,General Environmental Science ,chemistry.chemical_classification ,Glutathione Peroxidase ,Mice, Inbred BALB C ,Reactive oxygen species ,biology ,Superoxide Dismutase ,Hydrogen Peroxide ,Cell Biology ,Glutathione ,Fibroblasts ,Catalase ,Cyclic AMP-Dependent Protein Kinases ,Mitochondria ,Cell biology ,Oxygen ,chemistry ,Cell culture ,NIH 3T3 Cells ,biology.protein ,General Earth and Planetary Sciences ,Reactive Oxygen Species ,Cell Survival and Death ,Peroxidase - Abstract
A study is presented of the effect of the cAMP cascade on oxygen metabolism in mammalian cell cultures. Serum-starvation of the cell cultures resulted in depression of the forward NADH-ubiquinone oxidoreductase activity of complex I, decreased content of glutathione, and enhancement of the cellular level of H2O2. Depressed transcription of cytosolic Cu/Zn-SOD 1, mitochondrial glutathione peroxidase and catalase was also observed. Activation of the cAMP cascade reversed the depression of the activity of complex I and the accumulation of H2O2. The effect of cAMP involved the cAMP-dependent protein kinase.
- Published
- 2006
47. Systemic Inflammation, Blood Pressure, and Stroke Outcome
- Author
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Francesco Papa and Mario Di Napoli
- Subjects
medicine.medical_specialty ,Endocrinology, Diabetes and Metabolism ,Ischemia ,Blood Pressure ,Inflammation ,Systemic inflammation ,Risk Assessment ,Brain Ischemia ,Risk Factors ,Internal Medicine ,medicine ,Humans ,cardiovascular diseases ,Risk factor ,Intensive care medicine ,Stroke ,Review Paper ,business.industry ,medicine.disease ,C-Reactive Protein ,Treatment Outcome ,Blood pressure ,Pathophysiology of hypertension ,Acute Disease ,Hypertension ,Physical therapy ,medicine.symptom ,Cardiology and Cardiovascular Medicine ,Risk assessment ,business ,Biomarkers - Abstract
Hypertension is the most important modifiable risk factor for ischemic stroke, and antihypertensive treatment is of paramount importance to reduce the incidence of stroke mortality and morbidity. The significance and best management of hypertension during the first hours after stroke onset, however, are still matters of debate. Cerebral ischemia results in a complex inflammatory cascade; inflammatory mechanisms are also important participants in the pathophysiology of hypertension. There has been a convergence of evidence that is important to consider in managing systemic blood pressure after stroke to ensure an optimal outcome. The identification of useful markers will allow progress in our ability to treat blood pressure in the acute phase of a stroke. The determination of levels of C-reactive protein, an acute-phase inflammation marker, may help to guide our approach in the management of blood pressure in acute ischemic stroke. Whether this target will be useful in the development of risk prediction strategies or therapies for the treatment of stroke in humans is far from clear.
- Published
- 2006
48. Kidins220/ARMS modulates brain morphology and anxiety-like traits in adult mice
- Author
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Amanda Almacellas-Barbanoj, Martina Albini, Annyesha Satapathy, Fanny Jaudon, Caterina Michetti, Alicja Krawczun-Rygmaczewska, Huiping Huang, Francesca Manago, Francesco Papaleo, Fabio Benfenati, and Fabrizia Cesca
- Subjects
Neoplasms. Tumors. Oncology. Including cancer and carcinogens ,RC254-282 ,Cytology ,QH573-671 - Abstract
Abstract Kinase D interacting substrate of 220 kDa (Kidins220), also known as ankyrin repeat-rich membrane spanning (ARMS), is a transmembrane scaffold protein that participates in fundamental aspects of neuronal physiology including cell survival, differentiation, and synaptic plasticity. The Kidins220 constitutive knockout line displays developmental defects in the nervous and cardiovascular systems that lead to embryonic lethality, which has so far precluded the study of this protein in the adult. Moreover, Kidins220 mRNA is tightly regulated by alternative splicing, whose impact on nervous system physiology has not yet been addressed in vivo. Here, we have asked to what extent the absence of Kidins220 splicing and the selective knockout of Kidins220 impact on adult brain homeostasis. To answer this question, we used a floxed line that expresses only the full-length, non-spliced Kidins220 mRNA, and a forebrain-specific, CaMKII-Cre driven Kidins220 conditional knockout (cKO) line. Kidins220 cKO brains are characterized by enlarged ventricles in the absence of cell death, and by deficient dendritic arborization in several cortical regions. The deletion of Kidins220 leads to behavioral changes, such as reduced anxiety-like traits linked to alterations in TrkB-BDNF signaling and sex-dependent alterations of hippocampal-dependent spatial memory. Kidins220 floxed mice present similarly enlarged brain ventricles and increased associative memory. Thus, both the absolute levels of Kidins220 expression and its splicing pattern are required for the correct brain development and related expression of behavioral phenotypes. These findings are relevant in light of the increasing evidence linking mutations in the human KIDINS220 gene to the onset of severe neurodevelopmental disorders.
- Published
- 2022
- Full Text
- View/download PDF
49. Contractility In Vitro and Mitochondrial Response in Small and Large Rabbit Bowel after Anastomosis
- Author
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Germana Lissidini, Luigi Loiotila, Piero Portincasa, Francesco Papa, Salvatore Scacco, Mario Testini, G. M. Bonomo, Giuseppe Piccinni, Francesco Minerva, and Giuseppe Palasciano
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Male ,medicine.medical_specialty ,Pathology ,Surgical stress ,Colon ,Ileum ,Anastomosis ,Oxidative Phosphorylation ,Contractility ,Surgical anastomosis ,medicine ,Animals ,business.industry ,Anastomosis, Surgical ,Postoperative complication ,Muscle, Smooth ,Small intestine ,Mitochondria, Muscle ,Surgery ,medicine.anatomical_structure ,Rabbits ,medicine.symptom ,business ,Muscle Contraction ,Muscle contraction - Abstract
Leakage of a large bowel anastomosis remains the most serious postoperative complication in gastrointestinal surgery. In a recent experimental study we found that surgically induced hypoxia resulted in more derangement of a variety of biochemical markers in the large bowel (LB) than in the small bowel (SB). We explored the question of whether spontaneous and agonist-induced contractility of SB and LB muscle strips was influenced by surgical procedures and how contractility was related to energetic oxidative metabolism capacity in smooth muscle mitochondria. Sixty male New Zealand rabbits were operated on under general anesthesia. Segments of ileum and colon were resected from each rabbit, and an end-to-end anastomosis was constructed. A representative subset of segments from SB (n = 14) and LB (n = 14) at time 0 was used as controls. Tracts containing an anastomosis were resected at days 2, 7, and 14 after operation. At each time point, 20 segments adjacent to the anastomosis of both SB and LB were used for tensiometric and biochemical studies. Tensiometric studies demonstrated modifications in the smooth muscle function at both the acute and chronic stages with intestinal inflammation that may contribute to surgical stress-associated abnormal motility. Biochemical data showed that the respiratory capacity of the resected LB was more impaired than that of the SB. In both SB and LB, changes in respiratory activity preceded tensiometric changes. Thus abnormalities of contractility after surgical stress are more evident in LB than SB in segments adjacent to the anastomoses. This could be the consequence of abnormal biochemical changes, as adenosine triphosphate (ATP) is required for membrane potential maintenance, calcium homeostasis, and actin-myosin interactions.
- Published
- 2002
50. Morphological and biochemical characterization of mitochondria in Torpedo red blood cells
- Author
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Alessandra Pica, Francesco Papa, Emanuele De Nitto, Salvatore Scacco, Sergio Papa, Pica, Alessandra, Scacco, S., Papa, F., DE NITTO, E., and Papa, S. .
- Subjects
Erythrocytes ,Red-blood cell ,Physiology ,Cell ,Respiratory chain ,Mitochondrion ,Biology ,Torpedo ,Biochemistry ,law.invention ,Electron Transport ,Oxygen Consumption ,In vivo ,law ,medicine ,Animals ,Respiratory system ,Molecular Biology ,Erythroblast ,Electron transport chain ,Mitochondria ,Cell biology ,Staining ,Microscopy, Electron ,medicine.anatomical_structure ,Spectrophotometry ,Cytochromes - Abstract
A study is presented on the morphology and respiratory functions of mitochondria from Torpedo marmorata red blood cells. In vivo staining of red blood cells and transmission electron microscopy showed the existence of a considerable number of vital and orthodox mitochondria which decreased from young erythroblasts to mature erythrocytes from 60-50 to 30-20 per cell. In erythrocytes mitochondria exhibited a canonical, functional respiratory chain. The content and activity of cytochromes in erythrocytes were, however, significantly lower as compared to mammalian tissues.
- Published
- 2001
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