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156 results on '"Nanayakkara, Merlin"'

4. The protective role of Lactobacillus rhamnosus GG postbiotic on the alteration of autophagy and inflammation pathways induced by gliadin in intestinal models

Author

Furone, Francesca, primary, Bellomo, Claudia, additional, Carpinelli, Martina, additional, Nicoletti, Martina, additional, Hewa-Munasinghege, Francesca Natasha, additional, Mordaa, Majed, additional, Mandile, Roberta, additional, Barone, Maria Vittoria, additional, and Nanayakkara, Merlin, additional

Published
2023
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12. Inflammation Is Present, Persistent and More Sensitive to Proinflammatory Triggers in Celiac Disease Enterocytes

Author

Porpora, Monia, primary, Conte, Mariangela, additional, Lania, Giuliana, additional, Bellomo, Claudia, additional, Rapacciuolo, Luciano, additional, Chirdo, Fernando Gabriel, additional, Auricchio, Renata, additional, Troncone, Riccardo, additional, Auricchio, Salvatore, additional, Barone, Maria Vittoria, additional, and Nanayakkara, Merlin, additional

Published
2022
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13. 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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14. PTPRK, an EGFR Phosphatase, Is Decreased in CeD Biopsies and Intestinal Organoids.

Author

Nanayakkara, Merlin, Bellomo, Claudia, Furone, Francesca, Maglio, Mariantonia, Marano, Antonella, Lania, Giuliana, Porpora, Monia, Nicoletti, Martina, Auricchio, Salvatore, and Barone, Maria Vittoria

Subjects
*ORGANOIDS, *EPIDERMAL growth factor receptors, *PROTEIN-tyrosine phosphatase, *WHEAT proteins, *PHOSPHOPROTEIN phosphatases, *GLIADINS, *GLUTEN
Abstract

Background & Aims: Celiac disease (CeD) is an immune-mediated enteropathy triggered in genetically susceptible (HLA-DQ2/8) individuals by a group of wheat proteins and related prolamins from cereals. The celiac intestine is characterized by an inversion of the differentiation/proliferation program of the enterocytes, with an increase in the proliferative compartment and crypt hyperplasia, which are the mechanisms that regulate the increased proliferation in CeD that arenot completely understood.The aim of this study is to understand the role of Protein Tyrosine Phosphatase Receptor Type K (PTPRK), a nodal phosphatase that regulates EGFR activation in the proliferation of the enterocytes from CeD biopsies and organoids. Methods: The levels of PTPRK were evaluated by RT PCR, western blot (WB) and immunofluorescence techniques in intestinal biopsies and organoids from CeD patients and controls. Additionally, pEGFR and pERK were evaluated by WB and proliferation by BrdU incorporation. PTPRK si-RNA was silenced in CTR organoids and was overexpressed in CeD organoids. Results: PTPRK was reduced in Gluten Containing Diet–Celiac Disease (GCD–CeD) and Potential-Celiac Disease(Pot-CeD) biopsies (p < 0.01–p < 0.05) whereas pEGFR (p < 0.01 p < 0.01), pERK (p < 0.01 p < 0.01) and proliferation were increased. (p < 0.05 p < 0.05) respect to the controls.The CeD organoids reproduced these same alterations. Silencing of PTPRK in CTR organoids increased pEGFR, pERK and proliferation. The overexpression of PTPRK in CeD organoids reduced pEGFR, pERK and proliferation. Conclusions: modulation of PTPRK levels can reduce or increase pEGFR, pERK and proliferation in CeD or CTR organoids, respectively. The CeD organoids can be a good model to study the mechanisms of the disease. [ABSTRACT FROM AUTHOR]

Published
2023
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15. Pro-Pre and Postbiotic in Celiac Disease

Author

Conte, Mariangela, primary, Porpora, Monia, additional, Nigro, Federica, additional, Nigro, Roberto, additional, Budelli, Andrea Luigi, additional, Barone, M. Vittoria, additional, and Nanayakkara, Merlin, additional

Published
2021
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16. Pediatric Celiac Disease Patients Show Alterations of Dendritic Cell Shape and Actin Rearrangement

Author

Discepolo, Valentina, primary, Lania, Giuliana, additional, Ten Eikelder, Maria Leonarda Gertrude, additional, Nanayakkara, Merlin, additional, Sepe, Leandra, additional, Tufano, Rossella, additional, Troncone, Riccardo, additional, Auricchio, Salvatore, additional, Auricchio, Renata, additional, Paolella, Giovanni, additional, and Barone, Maria Vittoria, additional

Published
2021
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17. Bile acids modulate tight junction structure and barrier function of Caco-2 monolayers via EGFR activation

Author

Raimondi, Francesco, Santoro, Pasquale, Barone, Maria Vittoria, Pappacoda, Serena, Barretta, Maria Luisa, Nanayakkara, Merlin, Apicella, Carmela, Capasso, Letizia, and Paludetto, Roberto

Subjects
Bile acids -- Physiological aspects, Bile acids -- Research, Intestines -- Injuries, Intestines -- Risk factors, Intestines -- Care and treatment, Intestines -- Research, Biological sciences
Abstract

Intestinal and systemic illnesses have been linked to increased gut permeability. Bile acids, whose luminal profile can be altered in human disease, modulate intestinal paracellular permeability. We investigated the mechanism by which selected bile acids increase gut permeability using a validated in vitro model. Human intestinal Caco-2 cells were grown in monolayers and challenged with a panel of bile acids. Transepithelial electrical resistance and luminal-to-basolateral fluxes of 10-kDa Cascade blue-conjugated dextran were used to monitor paracellular permeability. Immunoprecipitation and immunoblot analyses were employed to investigate the intracellular pathway. Redistribution of tight junction proteins was studied by confocal laser microscopy. Micromolar concentrations of cholic acid, deoxycholic acid (DCA), and chenodeoxycholic acid (CDCA) but not ursodeoxycholic acid decreased transepithelial electrical resistance and increased dextran flux in a reversible fashion. Coincubation of 50 [micro]M CDCA or DCA with EGF, anti-EGF monoclonal antibody, or specific src inhibitor 4-Amino-5-(4-chlorophenyl)7-(t-butyl)pyrazolo[3,4-d]pyrimidine (PP-2) abolished the effect. A concentration of 50 [micro]M of either CDCA or DCA also induced EGF receptor phosphorylation, occludin dephosphorylation, and occludin redistribution at the tight junction level in the same time frame and in a reversible fashion. We conclude that selected bile acids modulate intestinal permeability via EGF receptor autophosphorylation, occludin dephosphorylation, and rearrangement at the tight junction level The effect is mediated by the src family kinases and is abolished by EGF treatment. These data also support the role of bile acids in the genesis of necrotizing enterocolitis and the protective effect of EGF treatment. epithelial growth factor receptor; epidermal growth factor; intestinal permeability

Published
2008

22. 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

24. Crosstalk between EGFR and Extranuclear Steroid Receptors

Author

MIGLIACCIO, ANTIMO, CASTORIA, GABRIELLA, DI DOMENICO, MARINA, CIOCIOLA, ALESSANDRA, LOMBARDI, MARIA, DE FALCO, ANTONIETTA, NANAYAKKARA, MERLIN, BOTTERO, DANIELA, DE STASIO, ROSINA, VARRICCHIO, LILIAN, and AURICCHIO, FERDINANDO

Published
2006

26. Celiac disease‐associated Neisseria flavescens decreases mitochondrial respiration in CaCo‐2 epithelial cells: Impact of Lactobacillus paracasei CBA L74 on bacterial‐induced cellular imbalance

Author

Labruna, Giuseppe, primary, Nanayakkara, Merlin, additional, Pagliuca, Chiara, additional, Nunziato, Marcella, additional, Iaffaldano, Laura, additional, D'Argenio, Valeria, additional, Colicchio, Roberta, additional, Budelli, Andrea L., additional, Nigro, Roberto, additional, Salvatore, Paola, additional, Barone, Maria Vittoria, additional, and Sacchetti, Lucia, additional

Published
2019
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31. Both innate immunity and growth factor receptor (EGFR) contribute to P31-43 induced proliferation effects in CACO2 cells and celiac enterocytes

Author

BARONE MV, GIANFRANI C, LANZILLO M, SANTAGATA S, TROIANO R, PALUMBO M, ZANZI, DELIA, NANAYAKKARA, Merlin, MAGLIO, MARIANTONIA, LANIA, GIULIANA, TRONCONE, RICCARDO, AURICCHIO, SALVATORE, Barone, Mv, Zanzi, Delia, Nanayakkara, Merlin, Maglio, Mariantonia, Gianfrani, C, Lania, Giuliana, Lanzillo, M, Santagata, S, Troiano, R, Palumbo, M, Troncone, Riccardo, and Auricchio, Salvatore

Published
2007

33. Su1165 Virus-Enhanced Upregulation of Type-1 Interferon Promotes Loss of Oral Tolerance in Celiac Disease

Author

Discepolo, Valentina, primary, Bouziat, Romain, additional, Hinterleitner, Reinhard, additional, Ikizler, Mine, additional, Lania, Giuliana, additional, Nanayakkara, Merlin, additional, Barone, Maria Vittoria, additional, Troncone, Riccardo, additional, Dermody, Terence, additional, Barreiro, Luis, additional, and Jabri, Bana, additional

Published
2016
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34. In the Intestinal Mucosa of Children With Potential Celiac Disease IL-21 and IL-17A are Less Expressed than in the Active Disease

Author

Borrelli, Melissa, primary, Gianfrani, Carmen, additional, Lania, Giuliana, additional, Aitoro, Rosita, additional, Ferrara, Katia, additional, Nanayakkara, Merlin, additional, Ponticelli, Domenico, additional, Zanzi, Delia, additional, Discepolo, Valentina, additional, Vitale, Serena, additional, Barone, Maria Vittoria, additional, Troncone, Riccardo, additional, Auricchio, Renata, additional, and Maglio, Mariantonia, additional

Published
2016
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37. Viral infections upregulate type-1 interferon and induce loss of oral tolerance in celiac disease

Author

Discepolo, Valentina, primary, Bouziat, Romain, additional, Stencel, Jennifer, additional, Ikizler, Mine, additional, Lania, Giuliana, additional, Nanayakkara, Merlin, additional, Carrella, Alessandra, additional, Cuomo, Marialaura, additional, Ferrara, Katia, additional, Auricchio, Renata, additional, Troncone, Riccardo, additional, Barone, Maria Vittoria, additional, Dermody, Terence, additional, Barreiro, Luis Bruno, additional, and Jabri, Bana, additional

Published
2014
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38. Lactobacillus paracaseiCBA L74 interferes with gliadin peptides entrance in Caco-2 cells

Author

Sarno, Marco, primary, Lania, Giuliana, additional, Cuomo, Marialaura, additional, Nigro, Federica, additional, Passannanti, Francesca, additional, Budelli, Andrea, additional, Fasano, Francesca, additional, Troncone, Riccardo, additional, Auricchio, Salvatore, additional, Barone, Maria Vittoria, additional, Nigro, Roberto, additional, and Nanayakkara, Merlin, additional

Published
2014
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39. A Celiac Cellular Phenotype, with Altered LPP Sub-Cellular Distribution, Is Inducible in Controls by the Toxic Gliadin Peptide P31-43

Author

Nanayakkara, Merlin, primary, Kosova, Roberta, additional, Lania, Giuliana, additional, Sarno, Marco, additional, Gaito, Alessandra, additional, Galatola, Martina, additional, Greco, Luigi, additional, Cuomo, Marialaura, additional, Troncone, Riccardo, additional, Auricchio, Salvatore, additional, Auricchio, Renata, additional, and Barone, Maria Vittoria, additional

Published
2013
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41. Immunogenicity of two oat varieties, in relation to their safety for celiac patients

Author

Maglio, Mariantonia, primary, Mazzarella, Giuseppe, additional, Barone, Maria Vittoria, additional, Gianfrani, Carmen, additional, Pogna, Norberto, additional, Gazza, Laura, additional, Stefanile, Rosita, additional, Camarca, Alessandra, additional, Colicchio, Barbara, additional, Nanayakkara, Merlin, additional, Miele, Erasmo, additional, Iaquinto, Gaetano, additional, Giardullo, Nicola, additional, Maurano, Francesco, additional, Santoro, Pasquale, additional, Troncone, Riccardo, additional, and Auricchio, Salvatore, additional

Published
2011
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42. Gliadin-Mediated Proliferation and Innate Immune Activation in Celiac Disease Are Due to Alterations in Vesicular Trafficking

Author

Barone, M. Vittoria, primary, Zanzi, Delia, additional, Maglio, Mariantonia, additional, Nanayakkara, Merlin, additional, Santagata, Sara, additional, Lania, Giuliana, additional, Miele, Erasmo, additional, Ribecco, Maria Teresa Silvia, additional, Maurano, Francesco, additional, Auricchio, Renata, additional, Gianfrani, Carmen, additional, Ferrini, Silvano, additional, Troncone, Riccardo, additional, and Auricchio, Salvatore, additional

Published
2011
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43. Gliadin Peptide P31-43 Localises to Endocytic Vesicles and Interferes with Their Maturation

Author

Barone, Maria Vittoria, primary, Nanayakkara, Merlin, additional, Paolella, Giovanni, additional, Maglio, Mariantonia, additional, Vitale, Virginia, additional, Troiano, Raffaele, additional, Ribecco, Maria Teresa Silvia, additional, Lania, Giuliana, additional, Zanzi, Delia, additional, Santagata, Sara, additional, Auricchio, Renata, additional, Troncone, Riccardo, additional, and Auricchio, Salvatore, additional

Published
2010
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44. Lactobacillus paracasei CBA L74 interferes with gliadin peptides entrance in Caco-2 cells.

Author

Sarno, Marco, Lania, Giuliana, Cuomo, Marialaura, Nigro, Federica, Passannanti, Francesca, Budelli, Andrea, Fasano, Francesca, Troncone, Riccardo, Auricchio, Salvatore, Barone, Maria Vittoria, Nigro, Roberto, and Nanayakkara, Merlin

Subjects
LACTOBACILLUS casei, GLIADINS, CELIAC disease treatment, THERAPEUTIC use of probiotics, IMMUNE response, ENTEROCYTES
Abstract

Several recent reports describe a role of probiotics as a therapeutic approach for celiac disease (CD). Two undigested A-gliadin peptides, P31-43 and P57-68, are central to CD pathogenesis, inducing an innate and an adaptive immune response, respectively. They enter enterocytes and localize to vesicular compartment to induce their toxic/immunogenics effects. In this article, we tested the effect of probiotic Lactobacillus paracasei (LP) CBA L74 (International Depository Accession Number LMG P-24778), its supernatant and LP-fermented cereals on gliadin peptides, P31-43 and P57-68, entrance in Caco-2 cells. Both LP CBA L74 and its supernatant inhibit P31-43 (intensity of fluorescence; FI: 75%) and P57-68 (FI: 50%) entrance in Caco2 cells, indicating that this biological effect is due to some product included in LP CBA L74 supernatant. This effect was present also after fermentation of cereals. This study describes a novel effect of probiotics in the prevention of undigested gliadin peptides toxic effects. [ABSTRACT FROM AUTHOR]

Published
2014
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45. Steroid Receptor Regulation of Epidermal Growth Factor Signaling through Src in Breast and Prostate Cancer Cells: Steroid Antagonist Action

Author

Migliaccio, Antimo, primary, Di Domenico, Marina, additional, Castoria, Gabriella, additional, Nanayakkara, Merlin, additional, Lombardi, Maria, additional, de Falco, Antonietta, additional, Bilancio, Antonio, additional, Varricchio, Lilian, additional, Ciociola, Alessandra, additional, and Auricchio, Ferdinando, additional

Published
2005
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46. Gliadin Peptide P31-43 Induces mTOR/NFkβ Activation and Reduces Autophagy: The Role of Lactobacillus paracasei CBA L74 Postbiotc

Author

Mariangela Conte, Federica Nigro, Monia Porpora, Claudia Bellomo, Francesca Furone, Andrea Luigi Budelli, Roberto Nigro, Maria Vittoria Barone, Merlin Nanayakkara, Conte, Mariangela, Nigro, Federica, Porpora, Monia, Bellomo, Claudia, Furone, Francesca, Budelli, Andrea Luigi, Nigro, Roberto, Barone, Maria Vittoria, and Nanayakkara, Merlin

Subjects
mTOR/NFkβ activation, celiac disease (CD), digestive system, Catalysis, Gliadin, Inorganic Chemistry, Peptide Fragment, Autophagy, Lactobacillus paracasei, Physical and Theoretical Chemistry, Intestinal Mucosa, Molecular Biology, Spectroscopy, Inflammation, Caco-2 Cell, TOR Serine-Threonine Kinase, Organic Chemistry, nutritional and metabolic diseases, General Medicine, digestive system diseases, Computer Science Applications, Celiac Disease, gliadin peptide P31-43, Lactobacillus paracasei CBA L74 postbiotc, Peptide, Human
Abstract

Celiac disease (CD) is an autoimmune disease characterized by an altered immune response stimulated by gliadin peptides that are not digested and cause damage to the intestinal mucosa. The aim of this study was to investigate whether the postbiotic Lactobacillus paracasei (LP) could prevent the action of gliadin peptides on mTOR, autophagy, and the inflammatory response. Most of the experiments performed were conducted on intestinal epithelial cells Caco-2 treated with a peptic-tryptic digest of gliadin (PTG) and P31-43. Furthermore, we pretreated the Caco-2 with the postbiotic LP before treatment with the previously described stimuli. In both cases, we evaluated the levels of pmTOR, p70S6k, and p4EBP-1 for the mTOR pathway, pNFkβ, and pERK for inflammation and LC 3 and p62 for autophagy. For autophagy, we also used immunofluorescence analysis. Using intestinal organoids derivate from celiac (CD) patients, we analyzed the effect of gliadin after postbiotic pretreatment with LP on inflammation marker NFkβ. Through these experiments, we showed that gliadin peptides are able to induce the increase of the inflammatory response in a more complex model of intestinal epithelial cells. LP postbiotic was able to induce autophagy in Caco-2 cells and prevent gliadin effects. In conclusion, postbiotic pretreatment with LP could be considered for in vivo clinical trials.

Published
2022
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47. Pivotal Role of Inflammation in Celiac Disease

Author

Maria Vittoria Barone, Renata Auricchio, Merlin Nanayakkara, Luigi Greco, Riccardo Troncone, Salvatore Auricchio, Barone, Maria Vittoria, Auricchio, Renata, Nanayakkara, Merlin, Greco, Luigi, Troncone, Riccardo, and Auricchio, Salvatore

Subjects
Glutens, viral infections, Organic Chemistry, Mediterranean and Western diet, General Medicine, Gliadin, Catalysis, Gastrointestinal Microbiome, Computer Science Applications, Inorganic Chemistry, inflammation, gluten, microbiota, Humans, Intestinal Mucosa, Physical and Theoretical Chemistry, Molecular Biology, Spectroscopy, celiac disease
Abstract

Celiac disease (CD) is an immune-mediated enteropathy triggered in genetically susceptible individuals by gluten-containing cereals. A central role in the pathogenesis of CD is played by the HLA-restricted gliadin-specific intestinal T cell response generated in a pro-inflammatory environment. The mechanisms that generate this pro-inflammatory environment in CD is now starting to be addressed. In vitro study on CD cells and organoids, shows that constant low-grade inflammation is present also in the absence of gluten. In vivo studies on a population at risk, show before the onset of the disease and before the introduction of gluten in the diet, cellular and metabolic alterations in the absence of a T cell-mediated response. Gluten exacerbates these constitutive alterations in vitro and in vivo. Inflammation, may have a main role in CD, adding this disease tout court to the big family of chronic inflammatory diseases. Nutrients can have pro-inflammatory or anti-inflammatory effects, also mediated by intestinal microbiota. The intestine function as a crossroad for the control of inflammation both locally and at distance. The aim of this review is to discuss the recent literature on the main role of inflammation in the natural history of CD, supported by cellular fragility with increased sensitivity to gluten and other pro-inflammatory agents.

Published
2022

48. Constitutive Differential Features of Type 2 Transglutaminase in Cells Derived from Celiac Patients and from Healthy Subjects

Author

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

Subjects
0301 basic medicine, Tissue transglutaminase, Peptide, type 2 transglutaminase, Gliadin, lcsh:Chemistry, Pathogenesis, skin-derived fibroblasts, lcsh:QH301-705.5, Spectroscopy, Skin, chemistry.chemical_classification, biology, General Medicine, gliadin peptide 31–43, Healthy Volunteers, Computer Science Applications, Antibody, Adult, Adolescent, Endosome, Catalysis, Gliadin peptide 31-43, Article, Antibodies, Inorganic Chemistry, 03 medical and health sciences, Diet, Gluten-Free, Young Adult, GTP-Binding Proteins, Humans, Protein Glutamine gamma Glutamyltransferase 2, Physical and Theoretical Chemistry, Molecular Biology, Autoantibodies, Transglutaminases, 030102 biochemistry & molecular biology, Organic Chemistry, Autophagy, nutritional and metabolic diseases, Fibroblasts, Subcellular localization, Celiac cellular phenotype, Celiac disease, Skin-derived fibroblasts, Type 2 transglutaminase, digestive system diseases, skin-derived fibroblast, Celiac Disease, 030104 developmental biology, lcsh:Biology (General), lcsh:QD1-999, chemistry, Immunology, biology.protein, Peptides, celiac cellular phenotype
Abstract

Type 2 transglutaminase (TG2) is a ubiquitous enzyme able to modify gliadin peptides introduced into the organism through the diet. By means of its catalytic activity, TG2 seems to have an important pathogenetic role in celiac disease (CD), an inflammatory intestinal disease caused by the ingestion of gluten-containing cereals. A strong autoimmune response to TG2 characterizes CD development. Anti-TG2 antibodies specifically derange the uptake of the &alpha, gliadin peptide 31&ndash, 43 by control, but not by celiac dermal fibroblasts, underlying some different constitutive features regarding TG2 in healthy and celiac subjects. Our aim was to investigate whether these differences depended on a different TG2 subcellular distribution and whether peptide 31&ndash, 43 differentially regulated TG2 expression and activity in cells of the two groups of subjects. We found that TG2 was more abundantly associated with membranes of celiac fibroblasts than of control cells, in particular with the early endosomal and autophagic compartments. We also found that peptide 31&ndash, 43 differentially affected TG2 expression and activity in the two groups of cells, activating TG2 more in control than in celiac cells and inducing TG2 expression in celiac cells, but not in control ones. The different TG2 subcellular localization and the different way the peptide 31&ndash, 43 modulates TG2 activity and availability into control and CD cells suggested that TG2 is involved in the definition of a constitutive CD cellular phenotype, thus having an important and still undefined role in CD pathogenesis.

Published
2020

49. Pro-Pre and Postbiotic in Celiac Disease

Author

Monia Porpora, Roberto Nigro, M. Vittoria Barone, Merlin Nanayakkara, Andrea Budelli, Mariangela Conte, Federica Nigro, Conte, Mariangela, Porpora, Monia, Nigro, Federica, Nigro, Roberto, Budelli, Andrea Luigi, Barone, M. Vittoria, and Nanayakkara, Merlin

Subjects
Technology, QH301-705.5, QC1-999, Inflammation, Disease, pro- pre- and post-biotic, Immune system, Intestinal mucosa, In vivo, medicine, Genetic predisposition, General Materials Science, Biology (General), QD1-999, Instrumentation, Fluid Flow and Transfer Processes, Autoimmune disease, business.industry, Physics, Process Chemistry and Technology, General Engineering, nutritional and metabolic diseases, Engineering (General). Civil engineering (General), medicine.disease, Computer Science Applications, Chemistry, inflammation, Immunology, TA1-2040, medicine.symptom, business, Dysbiosis, celiac disease
Abstract

Celiac Disease (CD) is an autoimmune disease characterized by inflammation of the intestinal mucosa due to an immune response to wheat gliadins. It presents in subjects with genetic susceptibility (HLA-DQ2/DQ8 positivity and non-HLA genes) and under the influence of environmental triggers, such as viral infections and intestinal microbiota dysbiosis. The only treatment currently available in CD is a gluten-free diet for life. Despite this, the intestinal dysbiosis that is recorded in celiac subjects persists, even with adherence to dietary therapy. In this review, we have analyzed the literature over the past several decades, which have focused on the use of pro-, pre- and post-biotics in vitro and in vivo in CD. The study of probiotics and their products in CD could be interesting for observing their various effects on several different pathways, including anti-inflammatory properties.

Published
2021

50. Constitutive alterations in vesicular trafficking increase the sensitivity of cells from celiac disease patients to gliadin

Author

Monia Porpora, Mariantonia Maglio, Salvatore Auricchio, Merlin Nanayakkara, Maria Antonietta De Matteis, Giuliana Lania, Maria Vittoria Barone, Renata Auricchio, Riccardo Rizzo, Valentina Discepolo, Alberto Luini, Mariangela Conte, Riccardo Troncone, Lania, Giuliana, Nanayakkara, Merlin, Maglio, Mariantonia, Auricchio, Renata, Porpora, Monia, Conte, Mariangela, De Matteis, Maria Antonietta, Rizzo, Riccardo, Luini, Alberto, Discepolo, Valentina, Troncone, Riccardo, Auricchio, Salvatore, and Barone, Maria Vittoria

Subjects
0301 basic medicine, Medicine (miscellaneous), Inflammation, Endosomes, Biology, digestive system, Article, General Biochemistry, Genetics and Molecular Biology, Coeliac disease, 03 medical and health sciences, 0302 clinical medicine, Immune system, Intestinal mucosa, medicine, lcsh:QH301-705.5, Autoimmune disease, Innate immune system, food and beverages, nutritional and metabolic diseases, medicine.disease, digestive system diseases, 030104 developmental biology, lcsh:Biology (General), Interleukin 15, 030220 oncology & carcinogenesis, Immunology, biology.protein, medicine.symptom, General Agricultural and Biological Sciences, Gliadin
Abstract

Celiac Disease (CD) is an autoimmune disease characterized by inflammation of the intestinal mucosa due to an immune response to wheat gliadins. Some gliadin peptides (e.g., A-gliadin P57-68) induce an adaptive Th1 pro-inflammatory response. Other gliadin peptides (e.g., A-gliadin P31-43) induce a stress/innate immune response involving interleukin 15 (IL15) and interferon α (IFN-α). In the present study, we describe a stressed/inflamed celiac cellular phenotype in enterocytes and fibroblasts probably due to an alteration in the early-recycling endosomal system. Celiac cells are more sensitive to the gliadin peptide P31-43 and IL15 than controls. This phenotype is reproduced in control cells by inducing a delay in early vesicular trafficking. This constitutive lesion might mediate the stress/innate immune response to gliadin, which can be one of the triggers of the gliadin-specific T-cell response., Giuliana Lania, Merlin Nanayakkara et al. show that cells from celiac disease patients have delays in early endocytic trafficking and an increase sensitivity to gliadin peptide P31-43. Delaying early vesicular trafficking in control cells induces a celiac-like cellular phenotype, highlighting a role for the early-recycling endosomal system in celiac disease.

Published
2019

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