Výsledky vyhledávání - "Paolo Di Simplicio"

DOES RISK OF HYPERHOMOCYSTEINEMIA DEPEND ON THIOL-DISULFIDE EXCHANGE REACTIONS OF ALBUMIN AND HOMOCYSTEINE?

Autor: Lucia Coppo, Simona Scheggi, Graziella DeMontis, Raffaella Priora, Simona Frosali, Antonio Margaritis, Domenico Summa, Danila Di Giuseppe, Monica Ulivelli, Paolo Di Simplicio

Publikováno v: Antioxidantsredox signaling.

Increased plasma concentrations of total homocysteine (tHcy) (mild-moderate hyperhomocysteinemia: 15-50 µM tHcy) are considered an independent risk factor for onset/progression of various diseases, but it is not known how the increase in tHcy causes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f821dd9c187555bcc92e6a603e63c35
https://pubmed.ncbi.nlm.nih.gov/36352822

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The control of hyperhomocysteinemia through thiol exchange mechanisms by mesna

Autor: Lucia Coppo, Domenico Summa, Monica Ulivelli, Danila Di Giuseppe, Simona Frosali, Paolo Di Simplicio, Antonios Margaritis, Raffaella Priora, Sabina Bartalini

Publikováno v: Amino Acids. 46:429-439

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 homo

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https://doi.org/10.1007/s00726-013-1636-4

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Quantification of Global Protein Disulfides and Thiol-Protein Mixed Disulfides to Study the Protein Dethiolation Mechanisms

Autor: Pietro Ghezzi, Sonia Salzano, Lucia Coppo, Raffaella Priora, Paolo Di Simplicio

Publikováno v: American Journal of Analytical Chemistry. :9-19

The redox state of cellular thiols is widely studied because it was recently linked to many different diseases and pathologies. In this work we quantified the concentrations of protein disulfides (PSSP) and thiol-protein mixed disulfides (XSSP) in ra

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https://doi.org/10.4236/ajac.2013.410a1002

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

Autor: Lucia Coppo, G. P. Pessina, Domenico Summa, Paolo Di Simplicio, Danila Di Giuseppe, Antonios Margaritis, Carlo Aldinucci, Raffaella Priora, Simona Frosali, Anna Di Stefano

Publikováno v: Pharmacological Research. 64:289-297

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ed69fbbea27d33e06d2051bef19a102
https://doi.org/10.1016/j.phrs.2011.03.014

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

Autor: Lucia Coppo, Paolo Di Simplicio, Simona Frosali, Antonios Margaritis, Raffaella Priora, Jongyun Heo, Domenico Summa, Danila Di Giuseppe

Publikováno v: Toxicology and Applied Pharmacology. 242:333-343

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::066ea817be1eaaeedd5b5f8b942c9745
https://doi.org/10.1016/j.taap.2009.11.003

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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

Autor: Anna Di Stefano, Francesca Cherubini Di Simplicio, Simona Frosali, Anna Ettorre, Paolo Di Simplicio, Alessandra Leonini, Raffaella Priora

Publikováno v: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 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

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Biochemical and Biological Aspects of Protein Thiolation in Cells and Plasma

Autor: Raffaella Priora, Paolo Di Simplicio, Francesca Cherubini Di Simplicio, Anna Di Stefano, Domenico Summa, Simona Frosali, Danila Di Giuseppe

Publikováno v: Antioxidants & Redox Signaling. 7:951-963

Protein thiolation is elicited by oxidation by different mechanisms and is involved in a variety of biological processes. Thiols, protein SH (PSH) and non-protein SH groups (NPSH, namely GSH), are in competition in all biological environments in the

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https://doi.org/10.1089/ars.2005.7.951

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

Autor: Carla Cellesi, Hieronim Jakubowski, Simona Frosali, Pier Leopoldo Capecchi, Pietro Enea Lazzerini, Paolo Di Simplicio, Franco Laghi Pasini, Francesca Cherubini Di Simplicio, Giuseppe Buonocore, Raffaella Priora, Danila Di Giuseppe

Publikováno v: Journal of Laboratory and Clinical Medicine. 144:235-245

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 di

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https://doi.org/10.1016/j.lab.2004.06.006

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Glutathione Recycling and Antioxidant Enzyme Activities in Erythrocytes of Term and Preterm Newborns at Birth

Autor: Danila Di Giuseppe, Paolo Di Simplicio, Mariangela Longini, Serafina Perrone, Giuseppe Buonocore, Donatella Tanganelli, Simona Frosali

Publikováno v: Neonatology. 85:188-194

We previously demonstrated a high susceptibility of neonatal red blood cells (RBC) to oxidative stress at birth. The aim of this study was to compare the RBC antioxidant capacity and redox cycle enzyme activities as well as glutathione (GSH) recyclin

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https://doi.org/10.1159/000075814

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