The level and half‐life of glutathione in human plasma

Wendel, Albrecht; Cikryt, Peter

doi:10.1016/0014-5793(80)80299-7

Cited by 154 publications

(65 citation statements)

References 15 publications

(1 reference statement)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…SNO-Cys was incubated with GSH in physiological buffer, and formation of SNO-Glu was measured by HPLC with electrochemical detection. The incubation of equimolar concentrations (50 1iM) of SNO-Cys and GSH at room temperature for 3 min led to the formation of 36.0±9.2 .tM of SNOGlu and a concomitant decrease in the concentration of SNOCys by 30.0±5.0 MM. These data indicate that the addition of exogenous SNO-Cys leads to the transfer of NO to another physiological low-molecular-weight thiol, forming SNO-Glu.…”

Section: Measurement Ofmentioning

confidence: 98%

Glutathione peroxidase potentiates the inhibition of platelet function by S-nitrosothiols.

Freedman

Frei²,

Welch³

et al. 1995

J. Clin. Invest.

136

View full text Add to dashboard Cite

GSH peroxidase (Px) catalyzes the reduction of lipid hydroperoxides (LOOH), known metabolic products of platelets and vascular cells. Because interactions between these cells are modulated by nitric oxide (NO) and LOOH inactivate NO, we investigated the effect of GSH-Px on the inhibition of platelet function by the naturally occurring S-nitrosothiol, S-nitroso-glutathione (SNO-Glu). Concentrations of SNO-Glu that alone did not inhibit platelet function (subthreshold inhibitory concentrations) were added to plateletrich plasma together with GSH-Px (0.2-20 U/ml); this led to a dose-dependent inhibition of platelet aggregation with an IC50 of 0.6 U/ml GSH-Px. In the presence of subthreshold inhibitory concentrations of SNO-Glu, the LOOH, 5-hydroperoxy-6,8,11,14-eicosatetraenoic acid, increased platelet aggregation, an effect reversed by GSH-Px. Glutathione and SNO-Glu were equally effective as cosubstrates for GSHPx. Incubation of SNO-Glu with GSH-Px for 1 min led to a 48.5% decrease in the concentration of SNO-Glu. Incubation of SNO-Glu with serum albumin led to the formation of S-nitroso-albumin, an effect enhanced by GSH-Px. These observations suggest that GSH-Px has two functions: reduction of LOOH, thereby preventing inactivation of NO, and metabolism of SNO-Glu, thereby liberating NO and/or supporting further transnitrosation reactions. (J. Clin. Invest. 1995. 96:394-400.) Key words: nitric oxide * S-nitrosothiols * endothelium-derived relaxing factor * lipid peroxides glutathione peroxidase

show abstract

Section: Measurement Ofmentioning

confidence: 98%

Glutathione peroxidase potentiates the inhibition of platelet function by S-nitrosothiols.

Freedman

Frei²,

Welch³

et al. 1995

J. Clin. Invest.

136

View full text Add to dashboard Cite

show abstract

“…Oral supplementation of healthy volunteers with up to 3 g GSH did not alter plasma levels of cysteine or GSH [72], perhaps because the intestinal mucosal epithelia and liver have very high levels of GGT and the supplemented GSH was rapidly metabolized. The half-life of GSH in human plasma is less than 3 min [73]. Attempts to increase GSH levels by increasing cysteine stores using lipoic acid [74] or whey protein [75,76] have met with some success.…”

Section: Human Studies Of Gsh Supplementationmentioning

confidence: 99%

Antioxidants in cystic fibrosis☆Conclusions from the CF Antioxidant Workshop, Bethesda, Maryland, November 11-12, 2003

Cantin

White

Cross

et al. 2007

Free Radical Biology and Medicine

View full text Add to dashboard Cite

Although great strides are being made in the care of individuals with cystic fibrosis (CF), this condition remains the most common fatal hereditary disease in North America. Numerous links exist between progression of CF lung disease and oxidative stress. The defect in CF is the loss of function of the transmembrane conductance regulator (CFTR) protein; recent evidence that CFTR expression and function are modulated by oxidative stress suggests that the loss may result in a poor adaptive response to oxidants. Pancreatic insufficiency in CF also increases susceptibility to deficiencies in lipophilic antioxidants. Finally the airway infection and inflammatory processes in the CF lung are potential sources of oxidants that can affect normal airway physiology and contribute to the mechanisms causing characteristic changes associated with bronchiectasis and loss of lung function. These multiple abnormalities in the oxidant/antioxidant balance raise several possibilities for therapeutic interventions that must be carefully assessed. IntroductionCystic fibrosis (CF) is the most common fatal disease caused by a single gene defect in Europe and North America [1,2]. The defective gene was identified in 1989 [3][4][5] and shown to encode the cystic fibrosis trans-membrane conductance regulator protein (CFTR). CFTR is a cyclic AMP-regulated anion channel with greatest selectivity for chloride, and bicarbonate [6][7][8]. Furthermore, CFTR regulates sodium transport across epithelial membranes through interactions with the epithelial sodium channel ENaC [9], and facilitates the trans-membrane export of the small organic anionic peptide glutathione [10]. The expression of CFTR is located in the apical membrane of epithelial cells that line mucous membranes and submucosal glands ☆ A list of participants may be found in the Acknowledgments.

show abstract

“…The lungs, like the liver and the kidney, also show a high rate of GSH turnover, and might even be a greater importer of GSH than the kidney. Plasma half-life of GSH is less than 2 min, and cellular half-life has been determined to be about 3-4 h [20]. Many biological functions have been ascribed to GSH, including: 1) maintenance of SH groups in a reduced state in proteins and other molecules; 2) destruction of hydrogen peroxide, other peroxides and free radicals; 3) catalysis of disulphide exchange reactions; 4) acting as a co-enzyme for certain enzymes (e.g.…”

Section: Glutathione In Perspectivementioning

confidence: 99%

Cellular glutathione turnover in vitro, with emphasis on type II pneumocytes

Klaveren¹,

Demedts²,

Nemery³

1997

Eur Respir J

View full text Add to dashboard Cite

The most important extracellular antioxidant in the lung is glutathione (GSH). The epithelial lining fluid of normal lungs contains very high concentrations of this tripeptide, about 100 times higher than that found in the extracellular fluid of many other tissues. How these high extracellular GSH levels are established and the mechanisms for increases (e.g. smokers) or decreases (e.g. lung fibrosis) are still unknown, but more insight into the regulation of GSH turnover in type II pneumocytes has recently become available.The purpose of this review is to give an overview of the literature concerning cellular GSH turnover for different cell types in vitro, with an emphasis on alveolar type II epithelial cells. The main messages of this review are that: 1) GSH is, in fact, an important vehicle for stabilizing, detoxifying and transferring cysteine; 2) cysteine is the rate-limiting substrate for GSH synthesis, especially under conditions of oxidative stress; 3) various transport systems exist for the uptake of the constituents of GSH, of which γ-glutamyltransferase appears to be important; 4) intracellular GSH levels of the type II cells are governed by different factors, including, probably, the extracellular redox state; and 5) a more reduced extracellular redox state appears to favour GSH efflux, whilst an oxidized state leads to retention of GSH inside the cell.These concepts should lead to reconsideration of some of the conventional approaches to increasing intracellular glutathione levels.

show abstract

The level and half‐life of glutathione in human plasma

Cited by 154 publications

References 15 publications

Glutathione peroxidase potentiates the inhibition of platelet function by S-nitrosothiols.

Glutathione peroxidase potentiates the inhibition of platelet function by S-nitrosothiols.

Antioxidants in cystic fibrosis☆Conclusions from the CF Antioxidant Workshop, Bethesda, Maryland, November 11-12, 2003

Cellular glutathione turnover in vitro, with emphasis on type II pneumocytes

Contact Info

Product

Resources

About