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172 results on '"SORAGNA AND, A"'

1. Lung Ultrasound-Implemented Diagnosis of Acute Decompensated Heart Failure in the ED

Author

Pivetta, Emanuele, Goffi, Alberto, Lupia, Enrico, Tizzani, Maria, Porrino, Giulio, Ferreri, Enrico, Volpicelli, Giovanni, Balzaretti, Paolo, Banderali, Alessandra, Iacobucci, Antonello, Locatelli, Stefania, Casoli, Giovanna, Stone, Michael B., Maule, Milena M., Baldi, Ileana, Merletti, Franco, Cibinel, Gian Alfonso, Baron, Paolo, Battista, Stefania, Buonafede, Giuseppina, Busso, Valeria, Conterno, Andrea, Del Rizzo, Paola, Ferrera, Patrizia, Pecetto, Paolo Fascio, Moiraghi, Corrado, Morello, Fulvio, Steri, Fabio, Ciccone, Giovannino, Calasso, Cosimo, Caserta, Mimma A, Civita, Marina, Condo', Carmen, D'Alessandro, Vittorio, Del Colle, Sara, Ferrero, Stefania, Griot, Giulietta, Laurita, Emanuela, Lazzero, Alberto, Lo Curto, Francesca, Michelazzo, Marianna, Nicosia, Vincenza, Palmari, Nicola, Ricchiardi, Alberto, Rolfo, Andrea, Rostagno, Roberto, Bar, Fabrizio, Boero, Enrico, Frascisco, Mauro, Micossi, Ilaria, Mussa, Alessandro, Stefanone, Valerio, Agricola, Renzo, Cordero, Gabriele, Corradi, Federica, Runzo, Cristina, Soragna, Aldo, Sciullo, Daniela, Vercillo, Domenico, Allione, Attilio, Artana, Nicoletta, Corsini, Fabrizio, Dutto, Luca, Lauria, Giuseppe, Morgillo, Teresa, Tartaglino, Bruno, Bergandi, Daniela, Cassetta, Ilaria, Masera, Clotilde, Garrone, Mario, Ghiselli, Gianluca, Ausiello, Livia, Barutta, Letizia, Bernardi, Emanuele, Bono, Alessia, Forno, Daniela, Lamorte, Alessandro, Lison, Davide, Lorenzati, Bartolomeo, Maggio, Elena, Masi, Ilaria, Maggiorotto, Matteo, Novelli, Giulia, Panero, Francesco, Perotto, Massimo, Ravazzoli, Marco, Saglio, Elisa, Soardo, Flavia, Tizzani, Alessandra, Tizzani, Pietro, Tullio, Mattia, Ulla, Marco, and Romagnoli, Elisa

Published
2015
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2. Social service at DEA: experience in Mauriziano Hospital, Turin

Author

Daniela Pons, Iolanda Vigna, Nadia Veronese, Pier Carla Carillo, Paola Malvasio, Liliana Pala, and Aldo Soragna

Subjects
Medicine (General), R5-920
Abstract

This work-report presents the findings of the activities carried out by the Social Service at DEA through the five-year period 2002- 2006; the presence of the Social Worker at the DEA was essential in the hours immediately after the clients’ admittance to Casualty, where the Social Welfare Service were able to provide prompt assistance. The targets were to provide clients an emergency service and to assure the quickest possible solution through taking immediate action. This Service has been used by 877 clients, 80,5% of whom were over 65 years of age; was provided by 2 Social Workers; altogether, a total of 1370 actions of various kinds were carried out. In evaluating the experience in global terms, the results have been more than positive for both targets; in particular, one must underline that, 54,5% of the cases a solution to each single problem was found directly at DEA, thereby allowing the patient to be discharged in safety, without burdening Casualty and DEA with the need for hospitalisation.

Published
2007
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3. Prevalence of hepatitis C virus infection in non-dialysis CKD patients: a multicentre study in renal clinics

Author

Luca De Nicola, Giorgio Soragna, Roberto Minutolo, Marcora Mandreoli, Felice Nappi, Pietro Manuel Ferraro, Adamasco Cupisti, Maura Ravera, Minutolo, R., Ravera, M., Cupisti, A., Nappi, F., Mandreoli, M., Soragna, G., Ferraro, P. M., and De Nicola, L.

Subjects
Transplantation, medicine.medical_specialty, business.industry, Hepatitis C virus, medicine.medical_treatment, Hepacivirus, Hepatitis C, Chronic, medicine.disease_cause, Hepatitis C, Multicenter study, Nephrology, Renal Dialysis, Internal medicine, Prevalence, Medicine, Humans, Renal Insufficiency, Chronic, business, Dialysis
Published
2021

5. Interaction between lysine 102 and aspartate 338 in the insect amino acid cotransporter KAAT1

Author

Castagna, M., Soragna, A., Mari, S.A., Santacroce, M., Bette, S., Mandela, P.G., Rudnick, G., Peres, A., and Sacchi, V.F.

Subjects
Lysine -- Properties, Aspartate -- Properties, Biological transport -- Evaluation, Physiological research, Biological sciences
Abstract

KAAT1 is a lepidopteran neutral amino acid transporter belonging to the NSS super family (SLC6), which has an unusual cation selectivity, being activated by [K.sup.+] and [Li.sup.+] in addition to [Na.sup.+]. We have previously demonstrated that Asp338 is essential for KAAT1 activation by [K.sup.+] and for the coupling of amino acid and driver ion fluxes. By comparing sequences of NSS family members, site-directed mutagenesis, and expression in Xenopus laevis oocytes, we identified Lysl02 as a residue likely to interact with Asp338. Compared with wild type, the single mutants K102V and D338E each showed altered leucine uptake and transport-associated currents in the presence of both [Na.sup.+] and [K.sup.+]. However, in K102V/D338E double mutant, the K102V mutation reversed both the inhibition of [Na.sup.+]-dependent transport and the block in [K.sup.+]-dependent transport that characterize the D338E mutant. [K.sup.+]-dependent leucine currents were not observed in any mutants with D338E. In the presence of the oxidant Cu(II) [(1,10-phenanthroline).sub.3], we observed specific and reversible inhibition of K102C/D338C mutant, but not of the corresponding single cysteine mutants, suggesting that these residues are sufficiently close to form a disulfide bond. Thus both structural and functional evidence suggests that these two residues interact. Similar results have been obtained mutating the bacterial transporter homolog TnaT. Asp338 corresponds to Asn286, a residue located in the [Na.sup.+] binding site in the recently solved crystal structure of the NSS transporter [LeuT.sub.Aa] (41). Our results suggest that Lysl02, interacting with Asp338, could contribute to the spatial organization of KAAT1 cation binding site and permeation pathway. residue interaction; oxidants; tertiary structure

Published
2007

6. Oligomeric structure of the neutral amino acid transporters KAAT1 and CAATCH1

Author

Bossi, Elena, Soragna, Andrea, Miszner, Andreea, Giovannardi, Stefano, Frangione, Valeria, and Peres, Antonio

Subjects
Oligomers -- Research, Biological sciences
Abstract

The highly homologous neutral amino acid transporters KAAT1 and CAATCH1, cloned from the midgut epithelium of the Manduca sexta larva, are members of the [Na.sup.+]/[Cl.sup.-] dependent transporter family. Recent evidence indicates that transporters of this family form constitutive oligomers. CAATCH1 and KAAT1 give rise to specific kinds of current depending on the transported amino acid, cotransported ion, pH, and membrane voltage. Different substrates induce notably distinct transport-associated currents in the two proteins that represent useful tools in structural-functional studies. To determine whether KAAT1 and CAATCH1 form functional oligomers, we have constructed four concatameric proteins for electrophysiological analysis, consisting of one KAAT1 protein covalently linked to another KAAT1 (K-K concatamer) or to CAATCH1 (K-C concatamer) and vice versa (C-C concatamer and C-K concatamer), and eight constructs where the two transporters were linked to yellow or cyan fluorescent protein in the N[H.sub.2] or COOH terminus, to determine the oligomer formation and the relative distance between the different subunits by fluorescence resonance energy transfer (FRET) analysis. Heterologous expression of the concatenated constructs and coinjection of the original proteins in different proportions allowed us to compare the characteristics of the currents to those of the oocytes expressing only the wild-type proteins. All the constructs were fully active, and their electrophysiological behavior was consistent with the activity as monomeric proteins. However, the FRET studies indicate that these transporters form oligomers in agreement with the LeU[T.sub.Aa] atomic structure and confirm that the COOH termini of the adjacent subunits are closer than N[H.sub.2] termini. transport; oligomerization; Slc6; fret

Published
2007

9. Structural domains involved in substrate selectivity in two neutral amino acid transporters

Author

Soragna, Andrea, Anna Mari, Stefania, Pisani, Rossana, Peres, Antonio, Castagna, Michela, Sacchi, V. Franca, and Bossi, Elena

Subjects
Amino acid metabolism, Epithelium, Larvae, Biological sciences
Abstract

The ability of the two highly homologous [Na.sup.+]/[Cl.sup.-]-dependent neutral amino acid transporters KAAT1 and CAATCH1, cloned from the midgut epithelium of the larva Manduca sexta, to transport different amino acids depends on the cotransported ion, on pH, and on the membrane voltage. Different organic substrates give rise to transport-associated currents with their own characteristics, which are notably distinct between the two proteins. Differences in amplitude, kinetics, and voltage dependence of the transport-associated currents have been observed, as well as different substrate selectivity patterns measured by radioactive amino acid uptake assays. These diversities represent useful tools to investigate the structural determinants involved in the substrate selectivity. To identify these regions, we built four chimeric proteins between the two transporters. These proteins, heterologously expressed in Xenopus laevis oocytes, were analyzed by two-electrode voltage clamp and uptake measurements. Initially, we exchanged the first three domains, obtaining the chimeras C3K9 and K3C9 (where numbers indicate the transmembrane domains and letters represent the original proteins), which showed electrophysiological and [[sup.3]H]amino acid uptake characteristics resembling those of KAAT1 and CAATCH1, respectively. Subsequent substitution of the last four domains in C3K9 and K3C9 gave the proteins C3K5C4 and K3C5K4, which showed the same behavior as KAAT1 and CAATCH1 in electrophysiological and transport determinations. These results suggest that in KAAT1 and CAATCH1, only the central transmembrane domains (from 4 to 8) of the protein are responsible for substrate selectivity. structure and function; Manduca sexta

Published
2004

18. NOVEL AND KNOWN MUTATIONS IDENTIFIED BY CLINICAL EXOME SEQUENCING FOR THE DIAGNOSIS OF POLYCYSTIC KIDNEY DISEASE

Author

Vaisitti, Tiziana, Sorbini, Monica, Callegari, Martina, Kalantari, Silvia, Bracciama, Valeria, Arruga, Francesca, Vanzino, Silvia Bruna, Pelle, Alessandra, Giachino, Daniela, Cocchi, Enrico, Simone Baldovino, Rollino, Cristiana, Fenoglio, Roberta, Tamagnone, Michela, Gherzi, Maurizio, Soragna, Giorgio, Vitale, Corrado, Berta, Valentina, Calabrese, Giovanni, Leonardi, Gianluca, Biancone, Luigi, Strampelli, Emanuela, Maroni, Serena, Santi, Sonia, Funaro, Loredana, Borzumati, Maurizio, Bertinetto, Patrizia, Viglino, Giusto, Gianoglio, Bruno, Peruzzi, Licia, Roccatello, Dario, Amoroso, Antonio, and Deaglio, Silvia

Published
2020

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