Search

Your search keyword '"IRACE, GAETANO"' showing total 31 results
Start Over Author "IRACE, GAETANO" Publisher wiley
31 results on '"IRACE, GAETANO"'

29. Unraveling amyloid toxicity pathway in NIH3T3 cells by a combined proteomic and1H-NMR metabonomic approach

Author

Ivana Sirangelo, Maria Luisa Balestrieri, Fausto Acernese, Fabrizio Barone, Rosa Maritato, Rocco Romano, Gaetano Irace, Silvia Vilasi, Annalisa Vilasi, Vilasi, A, Vilasi, S, Romano, R, Acernese, F, Barone, F, Balestrieri, Maria Luisa, Maritator, Irace, Gaetano, and Sirangelo, Ivana

Subjects
Proteomics, Amyloid, Magnetic Resonance Spectroscopy, Physiology, Blotting, Western, Clinical Biochemistry, Cell, Protein aggregation, Biology, medicine.disease_cause, Mice, medicine, Animals, Metabolomics, metabonomics, Electrophoresis, Gel, Two-Dimensional, Cytotoxicity, apoptosis, Reproducibility of Results, Cell Biology, Fibroblasts, amyloid toxicity, proteomics, Cell biology, medicine.anatomical_structure, Biochemistry, Apoptosis, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Toxicity, NIH 3T3 Cells, Signal transduction, Oxidative stress, Signal Transduction
Abstract

A range of debilitating human diseases is known to be associated with the formation of stable highly organized protein aggregates known as amyloid fibrils. The early prefibrillar aggregates behave as cytotoxic agents and their toxicity appears to result from an intrinsic ability to impair fundamental cellular processes by interacting with cellular membranes, causing oxidative stress and increase in free Ca2+ that lead to apoptotic or necrotic cell death. However, specific signaling pathways that underlie amyloid pathogenicity remain still unclear. This work aimed to clarify cell impairment induced by amyloid aggregated. To this end, we used a combined proteomic and one-dimensional 1H-NMR approach on NIH-3T3 cells exposed to prefibrillar aggregates from the amyloidogenic apomyoglobin mutant W7FW14F. The results indicated that cell exposure to prefibrillar aggregates induces changes of the expression level of proteins and metabolites involved in stress response. The majority of the proteins and metabolites detected are reported to be related to oxidative stress, perturbation of calcium homeostasis, apoptotic and survival pathways, and membrane damage. In conclusion, the combined proteomic and 1H-NMR metabonomic approach, described in this study, contributes to unveil novel proteins and metabolites that could take part to the general framework of the toxicity induced by amyloid aggregates. These findings offer new insights in therapeutic and diagnostic opportunities. J. Cell. Physiol. 228: 1359–1367, 2013. © 2012 Wiley Periodicals, Inc.

Published
2013

30. Tryptophanyl substitutions in apomyoglobin affect conformation and dynamic properties of AGH subdomain

Author

Clorinda Malmo, Ivana Sirangelo, Clara Iannuzzi, Gaetano Irace, Sirangelo, Ivana, Iannuzzi, Clara, Malmo, C, and Irace, Gaetano

Subjects
Protein Conformation, Stereochemistry, Mutant, Biophysics, Biochemistry, Biomaterials, Residue (chemistry), Animals, Molecule, Horses, Indole test, Acrylamide, Myoglobin, Chemistry, Organic Chemistry, Tryptophan, Whales, Wild type, General Medicine, Iodides, Protein superfamily, Solvent, Spectrometry, Fluorescence, Amino Acid Substitution, Apoproteins
Abstract

The solvent accessibilities to the tryptophanyl microenvironments of wild type sperm whale apomyoglobin (apoMb) and two mutants (W7F and W14F) containing a single tryptophan are measured by fluorescence quenching studies. The results are compared to those relative to horse apoMb. In the wild type sperm whale protein, no difference is noticed in the solvent accessibility of the two indole residues, as documented by the values of the Stern-Volmer constants. By contrast, the two tryptophan residues of horse apoMb are exposed to the solvent in a different way, thus indicating that some local conformational differences exist between the two homologous proteins in solution. The single W 3 F substitution at either position 7 or 14 determines local conformational changes that increase the accessibility of the remaining indole residue but do not affect the overall architecture of the protein molecule. © 2003 Wiley Periodicals, Inc. Biopolymers (Biospectros- copy) 70: 649 - 654, 2003

Published
2003

31. RESOLUTION OF THE INDIVIDUAL TRYPTOPHANYL CONTRIBUTIONS TO THE NEAR-ULTRAVIOLET DICHROIC ACTIVITY OF APOMYOGLOBIN

Author

Gaetano Irace, Ivana Sirangelo, Ettore Bismuto, Sirangelo, Ivana, Irace, Gaetano, and Bismuto, E.

Subjects
Indole test, Circular dichroism, Myoglobin, Photochemistry, Chemistry, Circular Dichroism, Tryptophan, General Medicine, Chromophore, Dichroic glass, Biochemistry, Spectral line, chemistry.chemical_compound, Bromide, Native state, Animals, Moiety, Spectrophotometry, Ultraviolet, Physical and Theoretical Chemistry, Apoproteins
Abstract

The individual tryptophanyl contributions to the near-ultraviolet dichroic activity of apomyoglobin in its native conformation have been resolved. This was accomplished by comparing the spectra of two classes of apomyoglobin with different aromatic residue contents and observing the effect of a specific modification of indole residues. The circular dichroism (CD) spectra of apomyoglobins containing two tryptophanyl residues, i.e. Trp A-5 and A-12, show the presence of a positive peak centered at 292 nm, attributable to indolic chromophore, which is missing in the CD spectrum of tuna apomyoglobin possessing only Trp A-12. Moreover, the specific modification of Trp A-5 by 2-hydroxy-5-nitrobenzyl bromide is shown by the lack of the 292 nm peak and the appearance of a positive band at longer wavelength. The pH dependence of the position of this band suggests that it arises from the 2-hydroxy-5-nitrobenzyl moiety. The results suggest that Trp A-12 does not substantially contribute to the optical activity in the near ultraviolet.

Published
1994

Catalog

Books, media, physical & digital resources
See catalog results