Search results for: Raffaella Priora

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Homocysteinemia control by cysteine in cerebral vascular patients after methionine loading test: evidences in physiological and pathological conditions in cerebro-vascular and multiple sclerosis patients

Monica Ulivelli, Raffaella Priora, Danila Giuseppe, Lucia Coppo, more

Amino Acids > 2016 > 48 > 6 > 1477-1489

The toxicity risk of hyperhomocysteinemia is prevented through thiol drug administration which reduces plasma total homocysteine (tHcy) concentrations by activating thiol exchange reactions. Assuming that cysteine (Cys) is a homocysteinemia regulator, the hypothesis was verified in healthy and pathological individuals after the methionine loading test (MLT). The plasma variations of redox species...

article

The control of hyperhomocysteinemia through thiol exchange mechanisms by mesna

Danila Giuseppe, Raffaella Priora, Lucia Coppo, Monica Ulivelli, more

Amino Acids > 2014 > 46 > 2 > 429-439

In hyperhomocysteinemic patients, after reaction with homocysteine-albumin mixed disulfides (HSS-ALB), mesna (MSH) forms the mixed disulfide with Hcy (HSSM) which can be removed by renal clearance, thus reducing the plasma concentration of total homocysteine (tHcy). In order to assess the HSS-ALB dethiolation via thiol exchange reactions, the distribution of redox species of cysteine, cysteinylglycine,...

article

Effects of cryoablation and radiofrequency ablation on endothelial and blood clotting activation

Paolo Pieragnoli, Anna Maria Gori, Giuseppe Ricciardi, Gianmarco Carrassa, more

Internal and Emergency Medicine > 2014 > 9 > 8 > 853-860

Cryoablation (CA) emerged as an alternative procedure to radiofrequency (RF). The aim of this study was to compare haemostatic system alterations in patients undergoing RF or CA for atrioventricular nodal reentrant tachycardia ablation. von Willebrand factor (vWF), spontaneous whole blood platelet aggregation, prothrombin fragment F1 + 2 (F1 + 2), thrombin-antithrombin complex (TAT), plasminogen activator...

article

In vitro inhibition of human and rat platelets by NO donors, nitrosoglutathione, sodium nitroprusside and SIN-1, through activation of cGMP-independent pathways

Raffaella Priora, Antonios Margaritis, Simona Frosali, Lucia Coppo, more

Pharmacological Research > 2011 > 64 > 3 > 289-297

Three different NO donors, S-nitrosoglutathione (GSNO), sodium nitroprusside (SNP) and 3-morpholino-sydnonimine hydrochloride (SIN-1) were used in order to investigate mechanisms of platelet inhibition through cGMP-dependent and -independent pathways both in human and rat. To this purpose, we also evaluated to what extent cGMP-independent pathways were related with the entity of NO release from each...

article

A structurally driven analysis of thiol reactivity in mammalian albumins

Ottavia Spiga, Domenico Summa, Simone Cirri, Andrea Bernini, more

Biopolymers > 95 > 4 > 278 - 285

Understanding the structural basis of protein redox activity is still an open question. Hence, by using a structural genomics approach, different albumins have been chosen to correlate protein structural features with the corresponding reaction rates of thiol exchange between albumin and disulfide DTNB. Predicted structures of rat, porcine, and bovine albumins have been compared with the experimentally...

article

The role of protein sulfhydryl groups and protein disulfides of the platelet surface in aggregation processes involving thiol exchange reactions

Antonios Margaritis, Raffaella Priora, Simona Frosali, Danila Di Giuseppe, more

Pharmacological Research > 2011 > 63 > 1 > 77-84

Blood platelets are central to haemostasis and platelet aggregation is considered to be a direct index of platelet function. Although protein disulfides (PSSP) are structural components of most proteins, current evidence suggests that PSSP work together with protein SH groups (PSH) to activate various platelet functions in dynamic processes involving thiol/disulfide exchange reactions.Based on these...

article

The control of S-thiolation by cysteine via gamma-glutamyltranspeptidase and thiol exchanges in erythrocytes and plasma of diamide-treated rats

Raffaella Priora, Lucia Coppo, Antonios Margaritis, Danila Di Giuseppe, more

Toxicology and Applied Pharmacology > 2010 > 242 > 3 > 333-343

Protein thiol modifications including cysteinylation (CSSP) and glutathionylation (GSSP) in erythrocytes of rat treated with diamide have been reported, but mechanism and origin of CSSP formation are unknown. Experiments were performed to relate CSSP formation to GSH hydrolysis via gamma-glutamyltranspeptidase (gamma-GT) and know whether cysteine may act as deglutathionylation factor. Time-dependent...

article

Regulation of redox forms of plasma thiols by albumin in multiple sclerosis after fasting and methionine loading test

Danila Giuseppe, Monica Ulivelli, Sabina Bartalini, Stefania Battistini, more

Amino Acids > 2010 > 38 > 5 > 1461-1471

Increases in plasma concentrations of total homocysteine (tHcy) have recently been reported in multiple sclerosis (MS) as the alteration of the methionine cycle for the onset of autoimmune diseases. Homocysteine (Hcy) and cysteine (Cys) are generated by the methionine cycle and transsulfuration reactions. Their plasma levels are subjected to complex redox changes by oxidation and thiol/disulfide (SH/SS)...

article

GSH depletion, protein S-glutathionylation and mitochondrial transmembrane potential hyperpolarization are early events in initiation of cell death induced by a mixture of isothiazolinones in HL60 cells

Anna Di Stefano, Simona Frosali, Alessandra Leonini, Anna Ettorre, more

BBA - Molecular Cell Research > 2006 > 1763 > 2 > 214-225

We recently described that brief exposure of HL60 cells to a mixture of 5-chloro-2-methyl-4-isothiazolin-3-one (CMI) and 2-methyl-4-isothiazolin-3-one (MI) induces apoptosis at low concentrations (0.001–0.01%) and necrosis at higher concentrations (0.05–0.1%). In this study, we show that glutathione (GSH) depletion, reactive oxygen species generation, hyperpolarization of mitochondrial transmembrane...

article

The effects of age and hyperhomocysteinemia on the redox forms of plasma thiols

Danila Di Giuseppe, Simona Frosali, Raffaella Priora, Francesca Cherubini Di Simplicio, more

The Journal of Laboratory and Clinical Medicine > 2004 > 144 > 5 > 235-245

We assayed the redox forms of cysteine (reduced [CSH], oxidized [CSSC], and bound to protein [CS-SP]), cysteinylglycine (CGSH; cysteinylgycine disulfide [CGSSGC] and cysteinylglycine-protein mixed disulfide [CGS-SP]), glutathione (GSH; glutathione disulfide [GSSG] and glutathione-protein mixed disulfide [GS-SP]), homocysteine (Hcy; homocystine [HcyS] and homocystine-protein mixed disulfides [bHcy]),...

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