Francesca Uberti
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Francesca Uberti has a total of 50 co-authors. Here are the top co-authors by number of shared publications:
Cinzia Ballabio
Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Via Balzaretti 9, 20133 Milano, Italy
7 shared publications- Elena Peñas
Institute of Food Science, Technology and Nutrition (ICTAN-CSIC), José Antonio Novais 6, 28040 Madrid, Spain
7 shared publications - Patrizia Restani
Faculty of Pharmacy, Università degli Studi di Milano, 20133 Milano, Italy
7 shared publications Patrizia Restani
University of Milan, Milan, Italy
6 shared publicationsChiara Di Lorenzo
Dipartimento di Scienze Farmacologiche e Biomolecolari Università degli Studi di Milano Milano Italy
5 shared publicationsChiara Tarantino
Euroclone SpA, via Figino 20/22, 20016 Pero, MI, Italy
4 shared publications
Latest Publications
- 1 September 2014
- Published by Elsevier in Food Chemistry
- Vol. 159, 343-352
Immunochemical investigation of allergenic residues in experimental and commercially-available wines fined with egg white proteins
- 1 September 2014
- Published by Elsevier in Food Chemistry
- Vol. 159, 343-352
Immunochemical investigation of allergenic residues in experimental and commercially-available wines fined with egg white proteins
- Open Access
- 20 November 2013
- Published by Springer Nature in Food Analytical Methods
- Vol. 7 (3) , 706-712
Collaborative Interlaboratory Studies for the Validation of ELISA Methods for the Detection of Allergenic Fining Agents Used in Wine According to the Criteria of OIV Resolution 427–2010 Modified by OIV–Comex 502–2012
- 20 November 2013
- Published by Springer Nature in Food Analytical Methods
- Vol. 7 (3) , 706-712
Open AccessCollaborative Interlaboratory Studies for the Validation of ELISA Methods for the Detection of Allergenic Fining Agents Used in Wine According to the Criteria of OIV Resolution 427–2010 Modified by OIV–Comex 502–2012
- Open Access
- 19 November 2013
- Published by Springer Nature in European Journal of Nutrition
- Vol. 53 (5) , 1177-1186
Diversity of oat varieties in eliciting the early inflammatory events in celiac disease
Purpose Celiac disease (CD) is an autoimmune enteropathy, triggered by dietary gluten. The only treatment is a strict gluten-free diet. Oats are included in the list of gluten-free ingredients by European Regulation, but the safety of oats in CD is still a matter of debate. The present study examined the capability of different oat cultivars of activating the gliadin-induced transglutaminase-2 (TG2)-dependent events in some in vitro models of CD. In addition, we compared this capability with the electrophoresis pattern of peptic–tryptic digests of the proteins of the oat cultivars. Methods K562(S) cells agglutination, transepithelial electrical resistance of T84-cell monolayers, intracellular levels of TG2 and phosphorylated form of protein 42–44 in T84 cells were the early gliadin-dependent events studied. Results The results showed that the Nave oat cultivar elicited these events, whereas Irina and Potenza varieties did not. The ability of a cultivar to activate the above-described events was associated with the electrophoretic pattern of oat proteins and their reactivity to anti-gliadin antibodies. Conclusion We found significant differences among oat cultivars in eliciting the TG2-mediated events of CD inflammation. Therefore, the safety of an oat cultivar in CD might be screened in vitro by means of biochemical and biological assays, before starting a clinical trial to definitely assess its safety.
- 19 November 2013
- Published by Springer Nature in European Journal of Nutrition
- Vol. 53 (5) , 1177-1186
Open AccessDiversity of oat varieties in eliciting the early inflammatory events in celiac disease
Purpose Celiac disease (CD) is an autoimmune enteropathy, triggered by dietary gluten. The only treatment is a strict gluten-free diet. Oats are included in the list of gluten-free ingredients by European Regulation, but the safety of oats in CD is still a matter of debate. The present study examined the capability of different oat cultivars of activating the gliadin-induced transglutaminase-2 (TG2)-dependent events in some in vitro models of CD. In addition, we compared this capability with the electrophoresis pattern of peptic–tryptic digests of the proteins of the oat cultivars. Methods K562(S) cells agglutination, transepithelial electrical resistance of T84-cell monolayers, intracellular levels of TG2 and phosphorylated form of protein 42–44 in T84 cells were the early gliadin-dependent events studied. Results The results showed that the Nave oat cultivar elicited these events, whereas Irina and Potenza varieties did not. The ability of a cultivar to activate the above-described events was associated with the electrophoretic pattern of oat proteins and their reactivity to anti-gliadin antibodies. Conclusion We found significant differences among oat cultivars in eliciting the TG2-mediated events of CD inflammation. Therefore, the safety of an oat cultivar in CD might be screened in vitro by means of biochemical and biological assays, before starting a clinical trial to definitely assess its safety.
- 17 November 2013
- Published by Wiley in Pediatric Allergy and Immunology
- Vol. 25 (1) , 98-100
Clinical monosensitivity to salmon and rainbow trout: a case report
- 17 November 2013
- Published by Wiley in Pediatric Allergy and Immunology
- Vol. 25 (1) , 98-100
Clinical monosensitivity to salmon and rainbow trout: a case report
- 1 September 2013
- Published by Codon Publications in Allergologia et Immunopathologia
- Vol. 41 (5) , 349-350
Allergy to all mammalian Bovidae proteins but cow's milk in a child
- 1 September 2013
- Published by Codon Publications in Allergologia et Immunopathologia
- Vol. 41 (5) , 349-350
Allergy to all mammalian Bovidae proteins but cow's milk in a child
- 1 May 2013
- Published by Springer Nature in Plant Foods for Human Nutrition
- Vol. 68 (2) , 149-154
Correlation Between Catechin Content and NF-κB Inhibition by Infusions of Green and Black Tea
This study investigates whether infusions of green and black tea inhibit the NF-κB driven transcription in human epithelial gastric AGS cells. Water extracts were prepared from different brands of green and black tea available on the Italian market. Teas with or without caffeine were studied. An industrially prepared freeze-dried water extract of green tea was also tested. Catechin and caffeine contents were measured by HPLC analysis. The decrease in phenol and catechin content three months after the expiry date was also investigated. The NF-κB driven transcription and the free radical scavenger activity were inhibited, and this effect was related to catechin levels. The potency of epigallocatechin 3-gallate in inhibiting NF-κB driven transcription is so great that tea extracts low in epigallocatechin 3-gallate are still highly active. In one decaffeinated sample of green tea, the phenol and catechin content was very low, probably as a consequence of caffeine removal. The decrease in catechin levels after 3 months did not reduce the inhibition of NF-κB driven transcription by tea infusions. This is the first paper reporting the inhibitory effect of NF-κB of commercial green and black infusions at the gastric level, evaluating their stability as well.
- 1 May 2013
- Published by Springer Nature in Plant Foods for Human Nutrition
- Vol. 68 (2) , 149-154
Correlation Between Catechin Content and NF-κB Inhibition by Infusions of Green and Black Tea
This study investigates whether infusions of green and black tea inhibit the NF-κB driven transcription in human epithelial gastric AGS cells. Water extracts were prepared from different brands of green and black tea available on the Italian market. Teas with or without caffeine were studied. An industrially prepared freeze-dried water extract of green tea was also tested. Catechin and caffeine contents were measured by HPLC analysis. The decrease in phenol and catechin content three months after the expiry date was also investigated. The NF-κB driven transcription and the free radical scavenger activity were inhibited, and this effect was related to catechin levels. The potency of epigallocatechin 3-gallate in inhibiting NF-κB driven transcription is so great that tea extracts low in epigallocatechin 3-gallate are still highly active. In one decaffeinated sample of green tea, the phenol and catechin content was very low, probably as a consequence of caffeine removal. The decrease in catechin levels after 3 months did not reduce the inhibition of NF-κB driven transcription by tea infusions. This is the first paper reporting the inhibitory effect of NF-κB of commercial green and black infusions at the gastric level, evaluating their stability as well.
- 3 April 2013
- Published by Wiley in Pediatric Allergy and Immunology
- Vol. 24 (3) , 270-275
Characterization of the sensitization profile to lupin in peanut‐allergic children and assessment of cross‐reactivity risk
Background: Case reports of allergy to lupin, due to primary sensitization or cross‐reactions with other legumes, are increasing as a consequence of the augmented use of lupin flour in bakery, pasta formulations and other food items. The main allergens that have been associated with the sensitization to lupin are α‐ and β‐conglutins and, to a lesser extent, γ‐ and δ‐conglutin, but no conclusive data are available so far. The aim of this study was to characterize the sensitization pattern to lupin in a group of 12 Italian children allergic to peanut and identify the specific lupin proteins involved in the cross‐reactivity with peanut.Methods: The immunochemical cross‐reactivity among peanut and lupin was evaluated by both in vitro immunoblotting and in vivo fresh food skin prick test (FFSPT).Results: The results showed that β‐conglutin was recognized by cutaneous IgEs from 7/12 peanut‐allergic children in FFSPT and serum IgEs from 5/12 in immunoblotting, while 4/12 and 8/12 patients tested positive to γ‐conglutin in FFSPT and immunoblotting, respectively. No significant immunoreactive responses were observed to α‐ and δ‐conglutins under non‐reducing conditions, but they were bound in FFSPT by the sera of 5/12 and 3/12 patients, respectively.Conclusion: In this group of allergic children, β‐conglutin has been identified as the major lupin allergen involved both in vitro and in vivo cross‐reactivity with peanut proteins. The role of γ‐conglutin in the cross‐reactivity between lupin and peanut proteins was also relevant and clear, despite the observed unspecificity of the immunoblotting responses.
- 3 April 2013
- Published by Wiley in Pediatric Allergy and Immunology
- Vol. 24 (3) , 270-275
Characterization of the sensitization profile to lupin in peanut‐allergic children and assessment of cross‐reactivity risk
Background: Case reports of allergy to lupin, due to primary sensitization or cross‐reactions with other legumes, are increasing as a consequence of the augmented use of lupin flour in bakery, pasta formulations and other food items. The main allergens that have been associated with the sensitization to lupin are α‐ and β‐conglutins and, to a lesser extent, γ‐ and δ‐conglutin, but no conclusive data are available so far. The aim of this study was to characterize the sensitization pattern to lupin in a group of 12 Italian children allergic to peanut and identify the specific lupin proteins involved in the cross‐reactivity with peanut.Methods: The immunochemical cross‐reactivity among peanut and lupin was evaluated by both in vitro immunoblotting and in vivo fresh food skin prick test (FFSPT).Results: The results showed that β‐conglutin was recognized by cutaneous IgEs from 7/12 peanut‐allergic children in FFSPT and serum IgEs from 5/12 in immunoblotting, while 4/12 and 8/12 patients tested positive to γ‐conglutin in FFSPT and immunoblotting, respectively. No significant immunoreactive responses were observed to α‐ and δ‐conglutins under non‐reducing conditions, but they were bound in FFSPT by the sera of 5/12 and 3/12 patients, respectively.Conclusion: In this group of allergic children, β‐conglutin has been identified as the major lupin allergen involved both in vitro and in vivo cross‐reactivity with peanut proteins. The role of γ‐conglutin in the cross‐reactivity between lupin and peanut proteins was also relevant and clear, despite the observed unspecificity of the immunoblotting responses.
- 29 October 2012
- Published by Wiley in Pediatric Allergy and Immunology
- Vol. 23 (8) , 761-764
Children monosensitized to pine nuts have similar patterns of sensitization
Background Several cases of pine nut allergies and anaphylaxis have been reported in the literature, but only few pine nut allergens have been characterized. The aim of this research is to identify through immunoelectrophoretic techniques the major pine nut allergens in a group of children monosensitized to pine nuts. Methods We studied five children with pine nut allergies and no other sensitization to food except to pine nuts, confirmed by in vivo (prick test, prick-to-prick) and in vitro tests (specific IgE determinations [CAP-FEIA]). The protein profile of pine nuts was analyzed by Sodium Dodecyl sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE). Immunoblotting was performed after incubation of membranes with the sera from the children included in the present study. Results Immunoblotting (SDS-PAGE) demonstrated five similar bands between 6 and 47 kDa in all the subjects studied. Conclusion These bands should be considered the potential allergens for pine nut allergic children.
- 29 October 2012
- Published by Wiley in Pediatric Allergy and Immunology
- Vol. 23 (8) , 761-764
Children monosensitized to pine nuts have similar patterns of sensitization
Background Several cases of pine nut allergies and anaphylaxis have been reported in the literature, but only few pine nut allergens have been characterized. The aim of this research is to identify through immunoelectrophoretic techniques the major pine nut allergens in a group of children monosensitized to pine nuts. Methods We studied five children with pine nut allergies and no other sensitization to food except to pine nuts, confirmed by in vivo (prick test, prick-to-prick) and in vitro tests (specific IgE determinations [CAP-FEIA]). The protein profile of pine nuts was analyzed by Sodium Dodecyl sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE). Immunoblotting was performed after incubation of membranes with the sera from the children included in the present study. Results Immunoblotting (SDS-PAGE) demonstrated five similar bands between 6 and 47 kDa in all the subjects studied. Conclusion These bands should be considered the potential allergens for pine nut allergic children.
- 3 September 2012
- Published by Wiley in Drug Testing and Analysis
- Vol. 5 (2) , 116-121
Could 1,3 dimethylamylamine (DMAA) in food supplements have a natural origin?
1,3 dimethylamylamine or methylexaneamine (DMAA) is a synthetic pharmaceutical patented in the 1940s as a nasal decongestant which can be used as a recreational stimulant. Alleged to occur in nature, DMAA has become a widely used ingredient in sports food supplements, despite its status as a doping agent and concerns over its safety. There is now some doubt as to whether it can be sourced naturally or whether it actually occurs naturally at all. The presence of DMAA was investigated by high performance liquid chromatography (HPLC) in extracts of the leaves and stems of four geranium species and of three well‐known cultivars. The amounts of DMAA in commercial geranium (Pelargonium graveolens) oil and the leading sports supplement which uses the ingredient were also measured. DMAA was not found in any of the leaves or stems or in the commercial geranium oil included in this study. Approximately 30 mg per daily dose was found in the food supplement. Therefore, the amount of DMAA found in the supplement is most unlikely to have been sourced in nature, and it must be concluded that synthetic DMAA, known to be capable of causing severe adverse physiological effects, has been added. Copyright © 2012 John Wiley & Sons, Ltd.
- 3 September 2012
- Published by Wiley in Drug Testing and Analysis
- Vol. 5 (2) , 116-121
Could 1,3 dimethylamylamine (DMAA) in food supplements have a natural origin?
1,3 dimethylamylamine or methylexaneamine (DMAA) is a synthetic pharmaceutical patented in the 1940s as a nasal decongestant which can be used as a recreational stimulant. Alleged to occur in nature, DMAA has become a widely used ingredient in sports food supplements, despite its status as a doping agent and concerns over its safety. There is now some doubt as to whether it can be sourced naturally or whether it actually occurs naturally at all. The presence of DMAA was investigated by high performance liquid chromatography (HPLC) in extracts of the leaves and stems of four geranium species and of three well‐known cultivars. The amounts of DMAA in commercial geranium (Pelargonium graveolens) oil and the leading sports supplement which uses the ingredient were also measured. DMAA was not found in any of the leaves or stems or in the commercial geranium oil included in this study. Approximately 30 mg per daily dose was found in the food supplement. Therefore, the amount of DMAA found in the supplement is most unlikely to have been sourced in nature, and it must be concluded that synthetic DMAA, known to be capable of causing severe adverse physiological effects, has been added. Copyright © 2012 John Wiley & Sons, Ltd.
- 21 March 2012
- Published by Elsevier in Food Chemistry
- Vol. 134 (3) , 1438-1445
Absence of allergenic residues in experimental and commercial wines fined with caseinates
- 21 March 2012
- Published by Elsevier in Food Chemistry
- Vol. 134 (3) , 1438-1445
Absence of allergenic residues in experimental and commercial wines fined with caseinates