Thiol levels, protein carbonylation and anaerobic sulfur metabolism in erythrocytes of peritoneal dialysis and predialysis patients

Włodek, Przemysław J; Marcykiewicz, Bernadeta; Iciek, Małgorzata; Suliga, Małgorzata; Smoleński, O; Kowalczyk-Pachel, Danuta

doi:10.1111/j.1440-1797.2010.01353.x

Cited by 7 publications

(6 citation statements)

References 24 publications

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“…Whether these observed responses are physiologically relevant depends on the endogenous concentrations of 3‐MP (in mitochondria, in whole cells or in the extracellular space). At this point, only limited data are available in this respect; some studies estimate endogenous 3‐MP concentrations in the micromolar range (47, 48).…”

Section: Discussionmentioning

confidence: 99%

Intramitochondrial hydrogen sulfide production by 3‐mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics

et al. 2012

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It is well established that exposure of mammalian cells to hydrogen sulfide (H(2)S) suppresses mitochondrial function by inhibiting cytochrome-c oxidase (CcOX; complex IV). However, recent experimental data show that administration of H(2)S to mammalian cells can serve as an electron donor and inorganic source of energy. The aim of our study was to investigate the role of endogenously produced H(2)S in the regulation of mitochondrial electron transport and oxidative phosphorylation in isolated liver mitochondria and in the cultured murine hepatoma cell line Hepa1c1c7. Low concentrations of H(2)S (0.1-1 μM) elicited a significant increase in mitochondrial function, while higher concentrations of H(2)S (3-30 μM) were inhibitory. The positive bioenergetic effect of H(2)S required a basal activity of the Krebs cycle and was most pronounced at intermediate concentrations of succinate. 3-mercaptopyruvate (3-MP), the substrate of the mitochondrial enzyme 3-mercaptopyruvate sulfurtransferase (3-MST) stimulated mitochondrial H(2)S production and enhanced mitochondrial electron transport and cellular bioenergetics at low concentrations (10-100 nM), while at higher concentrations, it inhibited cellular bioenergetics. SiRNA silencing of 3-MST reduced basal bioenergetic parameters and prevented the stimulating effect of 3-MP on mitochondrial bioenergetics. Silencing of sulfide quinone oxidoreductase (SQR) also reduced basal and 3-MP-stimulated bioenergetic parameters. We conclude that an endogenous intramitochondrial H(2)S-producing pathway, governed by 3-MST, complements and balances the bioenergetic role of Krebs cycle-derived electron donors. This pathway may serve a physiological role in the maintenance of mitochondrial electron transport and cellular bioenergetics.

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Section: Discussionmentioning

confidence: 99%

Intramitochondrial hydrogen sulfide production by 3‐mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics

et al. 2012

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“…Previous studies revealed a decreased level of sulfane sulfur in plasma of patients with a chronic kidney disease (CKD) undergoing hemodialysis (HD) (Wlodek et al, 2001), and a continuous ambulatory peritoneal dialysis (CAPD) (Wlodek et al, 2010). On the other hand, studies performed with erythrocytes of CKD patients showed a lower level of sulfane sulfur in the CKD predialysis group, while in the CAPD group the level of sulfane sulfur remained at the level observed in healthy controls (Włodek et al, 2010). This suggests that CAPD (as a replacement therapy) helps to preserve the anaerobic sulfur metabolism in erythrocytes.…”

Section: Sulfane Sulfur In the Chronic Kidney Diseasementioning

confidence: 84%

Sulfane sulfur – new findings on an old topic

2019

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Sulfane sulfur is a divalent sulfur atom bonded to another sulfur which is very reactive and labile. Compounds containing this reactive sulfur include persulfides, polysulfides, thiosulfate, thiosulfinates, polythionates, and elemental sulfur. Sulfane sulfur appears in a number of biologically important compounds, including thiocysteine, thiocystine and thiotaurine, products of the cysteine metabolism, as well as glutathione persulfide. Sulfane sulfur compounds can modify cysteine residues in proteins via an S-sulfhydration reaction to produce protein persulfides. It has been also postulated that cysteine persulfides can be incorporated into proteins during translation. Recently, the sulfane sulfur compounds, especially the persulfides and polysulfides, have attracted increasing interest due to their regulatory and antioxidant properties. Compounds containing sulfane sulfur are also regarded as a form of H2S storage, which can easily release this gasotransmitter in response to biological signals. Both reactive sulfur species (H2S and sulfane sulfur) always coexist in biological systems. This review is focused on new findings in the field of sulfane sulfur’s biological role, and disruption of its level in some patho/physiological conditions. A few sulfane sulfur donors with potential applications are presented. In recent years, in parallel to increasing interest in biological importance of sulfane sulfur, new analytical methods have been developed for sensitive and reliable determination of its level in the cells and tissues.

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“…Moreover, the structure of Hb in ESRD patients is impaired, and these alterations are enhanced during HD [ 143 ]. Regarding RBC thiol stress in HD and PD, LMM-SH (i.e., GSH) in the RBCs of patients on continuous ambulatory PD remain at a physiological level [ 144 ], whereas the GSH level in RBCs decreases before HD, and increases after HD [ 144 , 145 ]. However, in HD patients the increase in LMM-SH level is short-lasting and limited to a brief post-HD period, while the increase in the level of LMM-SH in the RBCs of PD patients is continuous and persistent [ 144 ].…”

Section: Discussionmentioning

confidence: 99%

“…Regarding RBC thiol stress in HD and PD, LMM-SH (i.e., GSH) in the RBCs of patients on continuous ambulatory PD remain at a physiological level [ 144 ], whereas the GSH level in RBCs decreases before HD, and increases after HD [ 144 , 145 ]. However, in HD patients the increase in LMM-SH level is short-lasting and limited to a brief post-HD period, while the increase in the level of LMM-SH in the RBCs of PD patients is continuous and persistent [ 144 ]. Thus, both PD and HD therapies increase the antioxidant power of RBC, but PD does so continuously, while the effect of HD is short-lasting and intermittent.…”

Section: Discussionmentioning

confidence: 99%

Blood Thiol Redox State in Chronic Kidney Disease

Garavaglia

Giustarini

Colombo

et al. 2022

IJMS

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Thiols (sulfhydryl groups) are effective antioxidants that can preserve the correct structure of proteins, and can protect cells and tissues from damage induced by oxidative stress. Abnormal levels of thiols have been measured in the blood of patients with moderate-to-severe chronic kidney disease (CKD) compared to healthy subjects, as well as in end-stage renal disease (ESRD) patients on haemodialysis or peritoneal dialysis. The levels of protein thiols (a measure of the endogenous antioxidant capacity inversely related to protein oxidation) and S-thiolated proteins (mixed disulphides of protein thiols and low molecular mass thiols), and the protein thiolation index (the molar ratio of the S-thiolated proteins to free protein thiols in plasma) have been investigated in the plasma or red blood cells of CKD and ESRD patients as possible biomarkers of oxidative stress. This type of minimally invasive analysis provides valuable information on the redox status of the less-easily accessible tissues and organs, and of the whole organism. This review provides an overview of reversible modifications in protein thiols in the setting of CKD and renal replacement therapy. The evidence suggests that protein thiols, S-thiolated proteins, and the protein thiolation index are promising biomarkers of reversible oxidative stress that could be included in the routine monitoring of CKD and ESRD patients.

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Thiol levels, protein carbonylation and anaerobic sulfur metabolism in erythrocytes of peritoneal dialysis and predialysis patients

Abstract: The CAPD as a replacement therapy helps to preserve thiol levels and anaerobic sulfur metabolism in erythrocytes.

Cited by 7 publications

References 24 publications

Intramitochondrial hydrogen sulfide production by 3‐mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics

Intramitochondrial hydrogen sulfide production by 3‐mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics

Sulfane sulfur – new findings on an old topic

Blood Thiol Redox State in Chronic Kidney Disease

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