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593 results on '"Gianazza, Elisabetta"'

35. Redox regulation of surface protein thiols: identification of integrin [alpha]-4 as a molecular target by using redox proteomics

Author

Laragione, Teresa, Bonetto, Valentina, Casoni, Filippo, Massignan, Tania, Bianchi, Giancarlo, Gianazza, Elisabetta, and Ghezzi, Pietro

Subjects
Proteins -- Research, Thiols -- Research, Science and technology
Abstract

Thiols affect a variety of cell functions, an effect known as redox regulation. We show here that treatment (1-2 h) of cells with 0.1-5 mM N-acetyl-L-cysteine (NAC) increases surface protein thiol expression in human peripheral blood mononuclear cells. This effect is not associated with changes in cellular glutathione (GSH) and is also observed with a non-GSH precursor thiol N-acetyI-D-cysteine or with GSH itself, which is not cell-permeable, suggesting a direct reducing action. NAC did not augment protein SH in the cytosol, indicating that they are already maximally reduced under normal, nonstressed, conditions. By using labeling with a non permeable, biotinylated SH reagent followed by two-dimensional gel electrophoresis and analysis by MS, we identified some of the proteins associated with the membrane that are reduced by NAC. These proteins include the following: integrin [alpha]-4, myosin heavy chain (nonmuscle type A), myosin light-chain alkali (nonmuscle isoform), and [beta]-actin. NAC pretreatment augmented integrin [alpha]-4-dependent fibronectin adhesion and aggregation of Jurkat cells without changing its expression by fluorescence-activated cell sorter, suggesting that reduction of surface disulfides can affect proteins function. We postulate that some of the activities of NAC or other thiol antioxidants may not only be due to free radical scavenging or increase of intracellular GSH and subsequent effects on transcription factors, but could modify the redox state of functional membrane proteins with exofacial SH critical for their activity.

Published
2003

36. A proteomic investigation of isolated soy proteins with variable effects in experimental and clinical studies

Author

Gianazza, Elisabetta, Eberini, Ivano, Arnoldi, Anna, Wait, Robin, and Sirtori, Cesare R.

Subjects
Hypercholesterolemia -- Care and treatment, Proteomics -- Models, Soybean products -- Composition, Soybean products -- Physiological aspects, Food/cooking/nutrition
Abstract

Dietary preparations of soy proteins used for clinical studies, particularly of hypercholesterolemia, in Europe and the United States were the subject of a proteomic comparison because differences in their composition may explain variability in experimental and clinical results. After two-dimensional electrophoresis, identities of the protein components (globulin subunits and their breakdown products) were established by matrix-assisted laser desorption/ionization mass spectrometry. The soy concentrates (Cholsoy/Croksoy), which were used in most of the Italian and Swiss studies in which reductions in cholesterolemia occurred, exhibited a predominance of breakdown products of the 7S globulin and mainly intact 11S globulin subunits. Soy isolates used in the United States (SUPRO) showed none of the major components corresponding to 7S globulin subunits; only some of the light chains of 11S were intact, and heavy chains of 11S also were fragmented. Ethanol- and nonethanol-treated SUPRO products showed considerable variability in their isoflavone concentrations and there seemed to be differential protein recoveries due to ethanol processing. These findings indicate differences in the protein composition of soy products used in clinical studies. We suggest that standardization should be improved before products are assessed for clinical outcome studies. KEY WORDS: * soy proteins * proteomics * ethanol extraction * hypercholesterolemia * soy globulins.

Published
2003

37. pH and ionic strength dependence of protein (Un)folding and ligand binding to bovine beta-lactoglobulins A and

Author

Beringhelli, Tiziana, Eberini, Ivano, Galliano, Monica, Pedoto, Armando, Perduca, Massimiliano, Sportiello, Alessandro, Fontana, Elena, Monaco, Hugo L., and Gianazza, Elisabetta

Subjects
Conformational analysis -- Research, Hydrogen-ion concentration -- Physiological aspects, Hydrogen-ion concentration -- Influence, Ionic solutions -- Physiological aspects, Ionic solutions -- Influence, Proteins -- Denaturation, Biological sciences, Chemistry
Abstract

Research shows that the stability of bovine beta-lactoglobulins against unfolding is markedly affected by the medium pH with both A and B variants of the protein stabilizing against urea and sodium dodesylsulfate denaturations at acidic and alkaline pH, respectively. Furthermore, complex formation of the variant B with oleic and palmitic acid is different from that of apoprotein and occurs at neutral pH.

Published
2002

42. Development of the first in vivo GPR17 ligand through an iterative drug discovery pipeline: A novel disease-modifying strategy for multiple sclerosis

Author

Parravicini, Chiara, primary, Lecca, Davide, additional, Marangon, Davide, additional, Coppolino, Giusy Tindara, additional, Daniele, Simona, additional, Bonfanti, Elisabetta, additional, Fumagalli, Marta, additional, Raveglia, Luca, additional, Martini, Claudia, additional, Gianazza, Elisabetta, additional, Trincavelli, Maria Letizia, additional, Abbracchio, Maria P., additional, and Eberini, Ivano, additional

Published
2020
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46. DISC867317_SupplementalMaterial – Supplemental material for SLC6A14, a Pivotal Actor on Cancer Stage: When Function Meets Structure

Author

Palazzolo, Luca, Paravicini, Chiara, Laurenzi, Tommaso, Adobati, Sara, Saporiti, Simona, Guerrini, Uliano, Gianazza, Elisabetta, Indiveri, Cesare, Anderson, Catriona M. H., Thwaites, David T., and Eberini, Ivano

Subjects
FOS: Clinical medicine, 111599 Pharmacology and Pharmaceutical Sciences not elsewhere classified
Abstract

Supplemental material, DISC867317_SupplementalMaterial for SLC6A14, a Pivotal Actor on Cancer Stage: When Function Meets Structure by Luca Palazzolo, Chiara Paravicini, Tommaso Laurenzi, Sara Adobati, Simona Saporiti, Uliano Guerrini, Elisabetta Gianazza, Cesare Indiveri, Catriona M. H. Anderson, David T. Thwaites and Ivano Eberini in SLAS Discovery

Published
2019
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48. Denaturation and self-association of apolipoprotein A-I investigated by electrophoretic techniques

Author

Gianazza, Elisabetta, Calabresi, Laura, Santi, Ombretta, Sirtori, Cesare R., and Franceschini, Guido

Subjects
Electrophoresis -- Research, Apolipoproteins -- Research, Biological sciences, Chemistry
Abstract

The apolipoprotein A-I mechanisms of chaotrope concentration function were studied to evaluate shifts in the extent of self-association and protein surface charge changes. Results show that no primary structural changes exists between compared species on the apoA-I behavior. This suggests that disaggregation and unfolding happen when the smaller assemblies are being affected by the larger ones .

Published
1997

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