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291 results on '"Rigo, Adelio"'

1. Serum Vascular Adhesion Protein-1 and Endothelial Dysfunction in Hepatic Cirrhosis: Searching for New Prognostic Markers.

Author

Fasolato, Silvano, Bonaiuto, Emanuela, Rossetto, Monica, Vanzani, Paola, Ceccato, Fabio, Vittadello, Fabio, Zennaro, Lucio, Rigo, Adelio, Mammano, Enzo, Angeli, Paolo, Pontisso, Patrizia, and Di Paolo, Maria Luisa

Subjects
PROGNOSIS, ENDOTHELIAL cells, VASCULAR cell adhesion molecule-1, ENDOTHELIUM diseases, CIRRHOSIS of the liver, CD54 antigen
Abstract

Endothelial dysfunction plays a key role in the development of liver cirrhosis. Among the biomarkers of endothelial dysfunction, the soluble form of Vascular Adhesion Protein-1 (sVAP-1) is an unconventional and less known adhesion molecule endowed also with amine oxidase activity. The aim of this study was to explore and correlate the behavior of sVAP-1 with that of the soluble vascular cell adhesion molecule-1 (sVCAM-1) and intercellular adhesion molecule-1 (sICAM-1) and with the severity of liver cirrhosis. A cross-sectional study was carried out by enrolling 28 controls, 59 cirrhotic patients without hepatocellular carcinoma, and 56 patients with hepatocellular carcinoma (HCC), mainly caused by alcohol abuse. The levels of adhesion molecules and of the pro-inflammatory cytokines (IL-6 and TNF-αα) were determined by immunoassay and the enzymatic activity of sVAP-1 by a fluorometric assay. In non-diabetic patients without HCC, a specific behavior of sVAP-1 was highlighted. Differently from sVCAM-1, sICAM-1, and cytokines, the sVAP-1 level was significantly increased only in the early stage of disease, and then, it decreased in the last stage (866 ± 390 ng/mL vs. 545 ± 316 ng/mL, in Child–Pugh class A vs. C, respectively, p < 0.05). Bivariate analysis correlates sVAP-1 to sVCAM-1, in the absence of HCC (Spearman's rho = 0.403, p < 0.01). Multiple linear regression analysis revealed that sVCAM-1 appears to be a predictor of sVAP-1 (β coefficient = 0.374, p = 0.021). In conclusion, in non-diabetic and non-HCC cirrhotic patients, sVAP-1 may be a potential prognostic biomarker that, together with sVCAM-1 and pro-inflammatory cytokines, may provide information on the progression of sinusoidal liver endothelium damage. [ABSTRACT FROM AUTHOR]

Published
2024
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17. Ab initio study of the mechanism of the binding of triplet O2 to hemocyanin

Author

Bernardi, Fernando, Bottoni, Andrea, Casadio, Rita, Fariselli, Piero, and Rigo, Adelio

Subjects
Carrier proteins -- Analysis, Oxygen -- Analysis, Ligand binding (Biochemistry) -- Models, Chemistry
Abstract

The density functional theory approach (DFT) on two model systems was utilized to evaluate the oxygen binding mechanism of triplet O2 to hemocyanin. The simple orbital interaction model indicates the role of copper ligands in enhancing the stability of singlet O2 state compared to the triplet O2 state at bonding distance. The energy difference between higher order molecular orbitals and lower order molecular orbitals also indicates the stability of the singlet state.

Published
1996

18. Ascorbate oxidation catalyzed by bis(histidine)cooper(II)

Author

Scarpa, Marina, Vianello, Fabio, Signor, Luca, Zennaro, Lucio, and Rigo, Adelio

Subjects
Vitamin C -- Analysis, Oxidation-reduction reaction -- Analysis, Copper compounds -- Analysis, Chemistry
Abstract

Bis(histidine)copper(II) (CuLsub2sup2+) was utilized as a catalysis for observing oxidation mechanism between ascorbate by molecular oxygen. Saturation of the reaction rate was detected at increasing concentrations of O2, ascorbate and CuLsub2sup2+ due to the enzymatic activity of Cu(II) on ascorbate oxidation. The saturation effect was also caused by the superoxide dismutase-like activity of the CuLsub2sup2+ complex. The reaction mechanism also involves the formation of mixed-ligand complexes in O2-catalyst-substrate order.

Published
1996

35. Active site residue involvement in monoamine or diamine oxidation catalysed by pea seedling amine oxidase

Author

DI PAOLO, MARIA LUISA, Lunelli, Michele, Fuxreiter, M, Rigo, Adelio, Simon, I, and Scarpa, Marina

Subjects
Models, Molecular, amine oxidase, computational pKa, Osmolar Concentration, Peas, Temperature, Hydrogen-Ion Concentration, computational docking, Structure-function relationships, Catalysis, Substrate Specificity, Kinetics, Seedlings, Cadaverine, Catalytic Domain, Amine Oxidase (Copper-Containing), Amines, Monoamine Oxidase, Oxidation-Reduction
Abstract

The structures of copper amine oxidases from various sources show good similarity, suggesting similar catalytic mechanisms for all members of this enzyme family. However, the optimal substrates for each member differ, depending on the source of the enzyme and its location. The structural factors underlying substrate selectivity still remain to be discovered. With this in view, we examined the kinetic behaviour of pea seedling amine oxidase with cadaverine and hexylamine, the first bearing two, and the second only one, positively charged amino group. The dependence of K(m) and catalytic constant (k(c)) values on pH, ionic strength and temperature indicates that binding of the monoamine is driven by hydrophobic interactions. Instead, binding of the diamine is strongly facilitated by electrostatic factors, controlled by polar side-chains and two titratable residues present in the active site. The position of the docked substrate is also essential for the participation of titratable amino acid residues in the following catalytic steps. A new mechanistic model explaining the substrate-dependent kinetics of the reaction is discussed.

Published
2011

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