Blood glutathione as independent marker of lipid peroxidation in heart failure

Campolo, Jonica; Maria, Renata De; Caruso, Raffaele; Accinni, R.; Turazza, F.; Parolini, Marina; Roubina, Elèna; Chiara, Benedetta De; Cighetti, Giuliana; Frigerio, Maria; Vitali, Ettore; Parodi, Oberdan

doi:10.1016/j.ijcard.2006.04.065

Cited by 35 publications

(26 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…increase in TBARS concentration, indicative of ROS presence). There is often a directly proportional correlation between the magnitude of this elevation and the degree of HF progression [16,20,[26][27][28][29][30][31]. Polidori et al [28] reported higher plasma concentrations of MDA in NYHA class III patients as compared with NYHA class II patients, as well as an inverse correlation between MDA concentration and LVEF.…”

Section: Discussionmentioning

confidence: 99%

Influence of cardiac resynchronization therapy on oxidative stress markers in patients with chronic heart failure

et al. 2014

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Influence of cardiac resynchronization therapy on oxidative stress markers in patients with chronic heart failure

et al. 2014

View full text Add to dashboard Cite

show abstract

“…The significance of this change is unclear; however, it may indicate decreased (extracellular) GPx-3 activity, secondary to severe renal dysfunction in heart failure, as the kidney is the principal source of GPx-3. 35 Glutathiolation is a reversible posttranslational modification that occurs by direct interaction of protein-SH with GSH under oxidizing conditions, by thiol disulfide exchange between a protein-SH and GSSG, or by reaction of protein-SH with S-nitrosoglutathione. 36 To date, no specific glutathiolated plasma proteins have been reported; however, glutathiolation has been demonstrated for the intracellular forms of 1-Cys peroxiredoxins (Prx), Trxs, and Grxs and other cellular proteins, 37,38 such as RAS and SERCA.…”

Section: Glutathione (Gsh)mentioning

confidence: 99%

Redox Regulation in the Extracellular Environment

Ottaviano

Handy

Loscalzo

2008

Circ J

128

100

View full text Add to dashboard Cite

Molecular oxygen is involved in the oxidation of substrates used to produce energy; however, normal metabolism can also generate harmful (bio)chemical byproducts. These deleterious products are partially reduced forms of oxygen, and include free radicals such as superoxide anion radical, hydroxyl radical, or highly oxidizing non-radical species such as hydrogen peroxide (H2O2) and lipid peroxides, which are collectively known as ROS. 1 ROS typically derive from normal metabolism, activated leukocytes, and ambient oxygen in the environment. The production and accumulation of ROS and their downstream effects can be controlled or attenuated by antioxidants. When the ability of antioxidants to eliminate harmful cellular and extracellular ROS is compromised, the balance between ROS generation and antioxidant function to eliminate ROS is shifted in favor of an accumulation of oxidants, which defines the state of oxidative stress in a cell or organism. Oxidative damage can affect DNA, lipids, and proteins, and eventually compromise cell integrity. Many studies have implicated ROS in the pathological processes leading to heart disease, cancer, aging, AIDS, and inflammatory and autoimmune diseases.Oxidants, especially free radicals, are highly reactive. Superoxide can react within milliseconds with nitric oxide (NO) to produce peroxynitrite (ONOO -), a reactive nitrogen species (RNS). The nitrosium cation and nitroxyl anion are other RNS derived from NO. 2 Peroxynitrite is a strong oxidant involved in the nitrosative modification of proteins and lipids. Owing to its rapid reaction with NO, superoxide may modulate NO bioavailability and, subsequently, regulate vascular function. 3 Circulation Journal Vol.72, January 2008The cytosol, mitochondria, peroxisomes, and plasma are all potential sites of ROS formation. 4 The major sources of ROS are enzymatic via nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (Nox), xanthine oxidase, myeloperoxidase, endothelial NO synthase (eNOS), or as a consequence of normal mitochondrial respiration. In vascular cells, other enzymatic sources of ROS include cytochrome P450 isoenzymes, lipoxygenase, cyclooxygenase, heme oxygenase, and glucose oxidase. 1,3,[5][6][7] Most reviews to date have focused on the role of intracellular antioxidants that eliminate ROS from the intracellular environment. There are, however, several extracellular antioxidants that also play an equally important role in limiting ROS accumulation in the extracellular environment. Along with limiting ROS accumulation, extracellular redox status is essential for maintaining protein stability and function.The major enzymes important for the elimination of extracellular H2O2 are glutathione peroxidase-3 (GPx-3) and peroxiredoxin IV (Prx IV). Other extracellular antioxidants involved in ROS elimination include paraoxonase (PON), thioredoxin (Trx), Trx reductase (TrxR), glutaredoxin (Grx), extracellular superoxide dismutase (EC-SOD), and extracellular glutathione (GSH).Some of these antioxidants, notably glutathione...

show abstract

“…9, 11 Abnormalities in intracellular cycle of glutathione (GSH), the main aminothiol modulator of redox environment, were found in chronic HF patients, 12 whereas deficiency of the GSH peroxidase (GPx) has been observed in animal models of LV remodeling associated with HF. 13, 14 GSH has been reported to modulate the activity of recombinant MMP-2 and -1 by modifying the cysteine (Cys) residue in the auto-inhibitory domain of the zymogen, a condition that keeps the MMP in a latent inhibitory form.…”

mentioning

confidence: 99%

Relationship Between Myocardial Redox State and Matrix Metalloproteinase Activity in Patients on Left Ventricular Assist Device Support

Caruso

Caselli

Boroni

et al. 2011

Circ J

Self Cite

View full text Add to dashboard Cite

Background: Redox aminothiols have been reported to modulate the activity of recombinant metalloproteinases (MMP). The aim of the present study was to investigate the effects of myocardial redox state on the activities of MMP-2 and -9 implicated in cardiac remodeling in end-stage heart failure patients supported by left ventricular assist device (LVAD). Methods and Results:During heart transplant (HT) surgery, myocardial specimens (MS) from right ventricular walls and LV walls were obtained from 7 LVAD recipients (LVAD group, MS n=35) and from 7 stable HT candidates on medical therapy (MT group, MS n=35). Myocardial MMP-2 and -9 activities and expression, tissue inhibitor of MMP (TIMP)-1 and -4, transforming growth factor (TGF)-β1 and aminothiol concentrations were measured. MMP-2 and -9 activities were evaluated also by incubating MS with different amounts of reduced and oxidized glutathione (GSH). MMP-2 and -9 activities and expression were lower in the LVAD group, whereas myocardial TIMP-1 and -4 concentrations were comparable to those of MT patients. Higher GSH and TGF-β1 concentrations were found in LVAD-recipients. Only GSH concentrations were inversely related to MMP-2 and -9 activities. In vitro, GSH had an inhibitory effect on MMP-2 and -9 activities.Conclusions: LVAD recipients show reduced myocardial MMP-2 and -9 activities and expression when compared to medically treated patients. Changes of myocardial redox state, predominantly GSH-dependent, appear to modulate MMP-2 and -9 activities by an inhibitory effect dependent on thiol content. These data support a role of GSH cycle in modulating the extracellular matrix in end-stage heart failure patients supported by LVAD. (Circ J 2011; 75: 2387 - 2396

show abstract

Blood glutathione as independent marker of lipid peroxidation in heart failure

Cited by 35 publications

References 32 publications

Influence of cardiac resynchronization therapy on oxidative stress markers in patients with chronic heart failure

Influence of cardiac resynchronization therapy on oxidative stress markers in patients with chronic heart failure

Redox Regulation in the Extracellular Environment

Relationship Between Myocardial Redox State and Matrix Metalloproteinase Activity in Patients on Left Ventricular Assist Device Support

Contact Info

Product

Resources

About