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2. In Vitro Investigation of Biological and Toxic Effects of 4-Octylphenol on Human Cells.

Author

Romanelli, Antonio Massimiliano, Montefusco, Antonio, Sposito, Silvia, Scafuri, Bernardina, Caputo, Ivana, and Paolella, Gaetana

Abstract

Alkylphenols are byproducts of anthropogenic activities that widely contaminate waters, soils and air; among them, the most represented are 4-nonylphenol (4-NP) and 4-octylphenol (4-OP). These compounds tend to bioaccumulate in animal and plant tissues and also represent a risk to human health. Indeed, humans are constantly exposed to alkylphenols through ingestion of contaminated water and food, inhalation and dermal absorption. In the present work, we characterized the cytotoxic ability of 4-OP towards several human cell lines, representing the potential main targets in the human body, also comparing its effect with that of 4-NP and of a mixture of both 4-OP and 4-NP in a range of concentrations between 1 and 100 μM. Viability assays demonstrated that each cell type had a peculiar sensitivity to 4-OP and that, in some cases, a combination of the two alkylphenols displayed a higher cytotoxic activity with respect to the single compound. Then, we focused our attention on a liver cell line (HepG2) in which we observed that 4-OP increased cell death and also caused interference with protective physiological cell processes, such as the unfolded protein response, autophagy and the antioxidant response. Finally, our experimental data were compared and correlated with ADMET properties originating from an in silico analysis. Altogether, our findings highlight a possible contribution of this pollutant to deregulation of the normal homeostasis in human liver cells. [ABSTRACT FROM AUTHOR]

Published
2024
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4. An operational platform for fire danger prevention and monitoring: insights from the OFIDIA2 project

Author

Bacciu, Valentina, primary, Mirto, Maria, additional, Fiore, Sandro Luigi, additional, Sirca, Costantino, additional, Saura, Josè Maria Costa, additional, Scardigno, Sonia, additional, Scardigno, Valentina, additional, Nassisi, Paola, additional, Nuzzo, Alessandra, additional, D’Anca, Alessandro, additional, Aloisio, Antonio, additional, Verri, Giorgia, additional, Coppini, Giovanni, additional, Caputo, Ivana, additional, Pirone, Lucio, additional, Spano, Donatella, additional, and Aloisio, Giovanni, additional

Published
2022
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7. Civil Protection Organisational and Procedural Interoperability Profile

Author

Piwiński, Jan, Lanziani, Biagio, Ronco, Francesco, Caputo, Ivana, Kacprzyk, Janusz, Series editor, Pal, Nikhil R., Advisory editor, Bello Perez, Rafael, Advisory editor, Corchado, Emilio S., Advisory editor, Hagras, Hani, Advisory editor, Kóczy, László T., Advisory editor, Kreinovich, Vladik, Advisory editor, Lin, Chin-Teng, Advisory editor, Lu, Jie, Advisory editor, Melin, Patricia, Advisory editor, Nedjah, Nadia, Advisory editor, Nguyen, Ngoc Thanh, Advisory editor, Wang, Jun, Advisory editor, Szewczyk, Roman, editor, and Havlik, Denis, editor

Published
2018
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18. OFIDIA2: An Operational Platform for Fire Danger Prevention and Monitoring

Author

Mirto, Maria, primary, Fiore, Sandro Luigi, additional, Bacciu, Valentina, additional, Sirca, Costantino, additional, Saura, Josè Maria Costa, additional, Scardigno, Sonia, additional, Scardigno, Valentina, additional, Nassisi, Paola, additional, Nuzzo, Alessandra, additional, D’Anca, Alessandro, additional, Aloisio, Antonio, additional, Verri, Giorgia, additional, Coppini, Giovanni, additional, Caputo, Ivana, additional, Pirone, Lucio, additional, Valentini, Riccardo, additional, Spano, Donatella, additional, and Aloisio, Giovanni, additional

Published
2022
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23. Peculiar Ca 2+ Homeostasis, ER Stress, Autophagy, and TG2 Modulation in Celiac Disease Patient-Derived Cells.

Author

Sposito, Silvia, Secondo, Agnese, Romanelli, Antonio Massimiliano, Montefusco, Antonio, Nanayakkara, Merlin, Auricchio, Salvatore, Barone, Maria Vittoria, Caputo, Ivana, and Paolella, Gaetana

Subjects
CELIAC disease, ENDOPLASMIC reticulum, HOMEOSTASIS, AUTOPHAGY, INTESTINAL diseases, WESTERN immunoblotting, FIBROBLASTS
Abstract

Celiac disease (CD) is an inflammatory intestinal disease caused by the ingestion of gluten-containing cereals by genetically predisposed individuals. Constitutive differences between cells from CD patients and control subjects, including levels of protein phosphorylation, alterations of vesicular trafficking, and regulation of type 2 transglutaminase (TG2), have been reported. In the present work, we investigated how skin-derived fibroblasts from CD and control subjects responded to thapsigargin, an endoplasmic reticulum ER stress inducer, in an attempt to contribute to the comprehension of molecular features of the CD cellular phenotype. We analyzed Ca2+ levels by single-cell video-imaging and TG2 activity by a microplate assay. Western blots and PCR analyses were employed to monitor TG2 levels and markers of ER stress and autophagy. We found that the cytosolic and ER Ca2+ level of CD cells was lower than in control cells. Treatments with thapsigargin differently activated TG2 in control and CD cells, as well as caused slightly different responses regarding the activation of ER stress and the expression of autophagic markers. On the whole, our findings identified further molecular features of the celiac cellular phenotype and highlighted that CD cells appeared less capable of adapting to a stress condition and responding in a physiological way. [ABSTRACT FROM AUTHOR]

Published
2023
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34. The toxic alpha-gliadin peptide 31–43 enters cells without a surface membrane receptor

Author

Paolella, Gaetana, Lepretti, Marilena, Martucciello, Stefania, Nanayakkara, Merlin, Auricchio, Salvatore, Esposito, Carla, Barone, Maria Vittoria, Caputo, Ivana, Paolella, Gaetana, Lepretti, Marilena, Martucciello, Stefania, Nanayakkara, Merlin, Auricchio, Salvatore, Esposito, Carla, Barone, Maria Vittoria, and Caputo, Ivana

Subjects
Antibodie, Cell Count, Receptors, Cell Surface, Gliadin peptide 31-43, Antibodies, Gliadin, HEK293 Cell, Peptide Fragment, GTP-Binding Proteins, Celiac disease, Cell-penetrating peptides, Chemical cross-linking, Peptide internalization, Type 2 transglutaminase, Cell Biology, type 2 transglutaminase, Humans, Protein Glutamine gamma Glutamyltransferase 2, Intestinal Mucosa, Caco-2 Cell, Transglutaminases, Endocytosi, gliadin peptide 31–43, chemical cross-linking, Transglutaminase, Endocytosis, Peptide Fragments, Immunity, Innate, Celiac Disease, HEK293 Cells, Peptide, peptide internalization, Caco-2 Cells, Peptides, cell-penetrating peptide, GTP-Binding Protein, Human
Abstract

Alpha-gliadin peptide 31-43 is considered to be the main peptide responsible for the innate immune response in celiac disease patients. Recent evidence indicates that peptide 31-43 rapidly enters cells and interacts with the early endocytic vesicular compartment. However, the mechanism of its uptake is not completely understood. Our aim is to characterize, isolate and identify possible cell surface proteins involved in peptide 31-43 internalization by Caco-2 cells. In this study, we used a chemical cross-linker to block peptide 31-43 on cell surface proteins, and pulled-down peptide-proteins complexes using antibodies raised against peptide 31-43. Through this experimental approach, we did not observe any specific complex between cell proteins and peptide 31-43 in Coomassie-stained denaturating gels or by Western blotting. We also found that type 2 transglutaminase was not necessary for peptide 31-43 internalization, even though it had a regulatory role in the process. Finally, we demonstrated that peptide 31-43 did not behave as a classical ligand, indeed the labeled peptide did not displace the unlabeled peptide in a competitive binding assay. On the basis of these findings and of previous evidence demonstrating that peptide 31-43 is able to interact with a membrane-like environment in vitro, we conclude that membrane composition and organization, rather than a specific receptor protein, may have a major role in peptide 31-43 internalization by cells.

Published
2018

40. Application of a computational approach to identify protein targets for 4-nonylphenol

Author

Giordano, D, De Vita, M, Scafuri, Bernardina, Caputo, Ivana, Gay, Flaminia, Capaldo, Anna, Esposito, Carla, Marabotti, Anna, Italian Society of Biochemistry and Molecular Biology, Giordano, Deborah, Vita, Maria De, Scafuri, Bernardina, Caputo, Ivana, Gay, Flaminia, Capaldo, Anna, Esposito, Carla, and Marabotti, Anna

Published
2015

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