scholarly journals Abnormal redox status of membrane-protein thiols in sickle erythrocytes.

1985 ◽  
Vol 75 (5) ◽  
pp. 1531-1537 ◽  
Author(s):  
B H Rank ◽  
J Carlsson ◽  
R P Hebbel
Blood ◽  
1988 ◽  
Vol 72 (3) ◽  
pp. 1060-1063 ◽  
Author(s):  
BH Rank ◽  
NL Moyer ◽  
RP Hebbel

Abstract Since it is not known why sickle RBCs tend to undergo microvesiculation, we have investigated their susceptibility to thermal stress. While normal RBCs start to vesiculate at 49.0 +/- 0 degrees C (n = 14), sickle RBCs begin to vesiculate at 47.9 +/- 0.5 degrees C, with a range of 46.5 to 48.5 degrees C (n = 14). This abnormality is reproduced by treating normal RBCs with phenazine methosulfate (PMS), which stimulates the excess intracellular generation of superoxide characteristic of sickle RBCs. For PMS-treated RBCs, there is a strong correlation between membrane protein thiol oxidation and vesiculation temperature (r = .977, P less than .001). The abnormal vesiculation temperature of both unmanipulated sickle RBCs and PMS-treated RBCs is significantly improved by treatment of the RBCs with dithiothreitol. The most dense sickle RBCs are most prone to vesiculation during thermal stress, and they are the subpopulation having the greatest amount of thiol oxidation. We conclude that the tendency of sickle RBCs to vesiculate during thermal stress is further evidence for functional abnormality of the RBC cytoskeleton due to thiol oxidation.


Author(s):  
Nada Hashem Ayad ◽  
Hanaa Hibishy Gaballah ◽  
Hesham Abd El-Aziz Salem ◽  
Sobhy Abd El-Hamid Hassan ◽  
Safwat Mohamed Kasem

Background: Endometriosis is a gynecological disorder characterized by the presence of ectopic endometrium outside the uterus. It is a multi-factorial disease, where different processes facilitate the implantation and survival of ectopic endometrial tissue.  The Aim: This study aims to evaluate the levels of the expression patterns of mitogen-inducible gene 6 (Mig-6) in eutopic and ectopic endometrial tissues of endometriosis patients and their relevance to the levels of phosphorylated extracellular signal-regulated kinase 1/2 (pERK1/2) and redox status. Methods: Relative gene expression levels of Mig-6 and the levels of pERK1/2 were assessed in endometrial tissues of control group and in both eutopic and ectopic endometrial tissues of endometriosis patients .Serum levels of total protein thiols and total protein carbonyls were also assessed in endometriosis and control groups. Results: Relative gene expression levels of Mig- 6 showed significant lower values in endometriosis group as compared to control group, and they were associated with significant increase in pERK 1/2 levels and altered redox status. Conclusion: These data, signified a significant role of downregulated Mig-6 expression, and activated ERK 1/2 signaling in the pathogenesis of endometriosis. Moreover, it suggested that oxidative stress indicated by high protein carbonyls level contributes to the pathogenesis of endometriosis and that protein thiols have a defensive role against oxidative stress.


Nutrients ◽  
2019 ◽  
Vol 11 (10) ◽  
pp. 2318 ◽  
Author(s):  
Sara Baldelli ◽  
Fabio Ciccarone ◽  
Dolores Limongi ◽  
Paola Checconi ◽  
Anna Teresa Palamara ◽  
...  

Glutathione (GSH) is the main non-enzymatic antioxidant playing an important role in detoxification, signal transduction by modulation of protein thiols redox status and direct scavenging of radicals. The latter function is not only performed against reactive oxygen species (ROS) but GSH also has a fundamental role in buffering nitric oxide (NO), a physiologically-produced molecule having-multifaceted functions. The efficient rate of GSH synthesis and high levels of GSH-dependent enzymes are characteristic features of healthy skeletal muscle where, besides the canonical functions, it is also involved in muscle contraction regulation. Moreover, NO production in skeletal muscle is a direct consequence of contractile activity and influences several metabolic myocyte pathways under both physiological and pathological conditions. In this review, we will consider the homeostasis and intersection of GSH with NO and then we will restrict the discussion on their role in processes related to skeletal muscle function and degeneration.


2017 ◽  
Vol 474 (7) ◽  
pp. 1175-1193 ◽  
Author(s):  
Rachel Gergondey ◽  
Camille Garcia ◽  
Christophe H. Marchand ◽  
Stephane D. Lemaire ◽  
Jean-Michel Camadro ◽  
...  

The potential biological consequences of oxidative stress and changes in glutathione levels include the oxidation of susceptible protein thiols and reversible covalent binding of glutathione to the –SH groups of proteins by S-glutathionylation. Mitochondria are central to the response to oxidative stress and redox signaling. It is therefore crucial to explore the adaptive response to changes in thiol-dependent redox status in these organelles. We optimized the purification protocol of glutathionylated proteins in the yeast Saccharomyces cerevisiae and present a detailed proteomic analysis of the targets of protein glutathionylation in cells undergoing constitutive metabolism and after exposure to various stress conditions. This work establishes the physiological importance of the glutathionylation process in S. cerevisiae under basal conditions and provides evidence for an atypical and unexpected cellular distribution of the process between the cytosol and mitochondria. In addition, our data indicate that each oxidative condition (diamide, GSSG, H2O2, or the presence of iron) elicits an adaptive metabolic response affecting specific mitochondrial metabolic pathways, mainly involved in the energetic maintenance of the cells. The correlation of protein modifications with intracellular glutathione levels suggests that protein deglutathionylation may play a role in protecting mitochondria from oxidative stress. This work provides further insights into the diversity of proteins undergoing glutathionylation and the role of this post-translational modification as a regulatory process in the adaptive response of the cell.


2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Jen-Hsiang Tsai ◽  
Haw-Wen Chen ◽  
Yi-Wan Chen ◽  
Jer-Yuh Liu ◽  
Chong-Kuei Lii

We investigated the effect of vitamin E on membrane protein thiols under oxidative stress, which we induced by treating hepatocytes withtert-butyl hydroperoxide (TBH) for 60 mins. Those cells which we pretreated with vitamin E formed fewer blebs (22.3% compared to 60.0% in nonvitamin E-treated cells) and maintained cytosolic calcium concentration and the number of membrane protein thiols instead of showing the usual symptoms in cells undergoing oxidative stress. Dithiothreitol (DTT) also commonly reduces bleb formation in hepatocytes affected by TBH. However, our experiments clearly demonstrate that DTT does not prevent the changes in cytosolic calcium and membrane protein thiols in the blebbing cells. Consequently, we decided to pretreat cells with both DTT and vitamin E and found that the influence of TBH was entirely prevented. These findings may provide us with a new aspect for investigating the mechanism of bleb formation under oxidative stress.


2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Rosa E. Hansen ◽  
Mieko Otsu ◽  
Ineke Braakman ◽  
Jakob R. Winther

Plasma cells produce and secrete massive amounts of disulfide-containing antibodies. To accommodate this load on the secretory machinery, the differentiation of resting B cells into antibody-secreting plasma cells is accompanied by a preferential expansion of the secretory compartments of the cells and by an up-regulation of enzymes involved in redox regulation and protein folding. We have quantified the absolute levels of protein thiols, protein disulfides, and glutathionylated proteins in whole cells. The results show that while the global thiol-disulfide state is affected to some extent by the differentiation, steady-state levels of glutathionylated protein thiols are less than 0.3% of the total protein cysteines, even in fully differentiated cells, and the overall protein redox state is not affected until late in differentiation, when large-scale IgM production is ongoing. A general expansion of the ER does not affect global protein redox status until an extensive production of cargo proteins has started.


2015 ◽  
Vol 469 (3) ◽  
pp. 347-355 ◽  
Author(s):  
Matthew Dodson ◽  
Matthew Redmann ◽  
Namakkal S. Rajasekaran ◽  
Victor Darley-Usmar ◽  
Jianhua Zhang

Maintaining cellular redox status to allow cell signalling to occur requires modulation of both the controlled production of oxidants and the thiol-reducing networks to allow specific regulatory post-translational modification of protein thiols. The oxidative stress hypothesis captured the concept that overproduction of oxidants can be proteotoxic, but failed to predict the recent finding that hyperactivation of the KEAP1–NRF2 system also leads to proteotoxicity. Furthermore, sustained activation of thiol redox networks by KEAP1–NRF2 induces a reductive stress, by decreasing the lifetime of necessary oxidative post-translational modifications required for normal metabolism or cell signalling. In this context, it is now becoming clear why antioxidants or hyperactivation of antioxidant pathways with electrophilic therapeutics can be deleterious. Furthermore, it suggests that the autophagy–lysosomal pathway is particularly important in protecting the cell against redox-stress-induced proteotoxicity, since it can degrade redox-damaged proteins without causing aberrant changes to the redox network needed for metabolism or signalling. In this context, it is important to understand: (i) how NRF2-mediated redox signalling, or (ii) the autophagy-mediated antioxidant/reductant pathways sense cellular damage in the context of cellular pathogenesis. Recent studies indicate that the modification of protein thiols plays an important role in the regulation of both the KEAP1–NRF2 and autophagy pathways. In the present review, we discuss evidence demonstrating that the KEAP1–NRF2 pathway and autophagy act in concert to combat the deleterious effects of proteotoxicity. These findings are discussed with a special emphasis on their impact on cardiovascular disease and neurodegeneration.


Horticulturae ◽  
2021 ◽  
Vol 7 (11) ◽  
pp. 455
Author(s):  
Antonio López-Orenes ◽  
Conceição Santos ◽  
Maria Celeste Dias ◽  
Helena Oliveira ◽  
María Á. Ferrer ◽  
...  

Lead (Pb) soil contamination remains a major ecological challenge. Zygophyllum fabago is a candidate for the Pb phytostabilisation of mining tailings; nevertheless, the cytogenotoxic effects of low doses of Pb on this species are still unknown. Therefore, Z. fabago seeds collected from non-mining (NM) and mining (M) areas were exposed to 0, 5 and 20 µM Pb for four weeks, after which seedling growth, Pb cytogenotoxic effects and redox status were analyzed. The data revealed that Pb did not affect seedling growth in M populations, in contrast to the NM population. Cell cycle progression delay/arrest was detected in both NM and M seedlings, mostly in the roots. DNA damage (DNAd) was induced by Pb, particularly in NM seedlings. In contrast, M populations, which showed a higher Pb content, exhibited lower levels of DNAd and protein oxidation, together with higher levels of antioxidants. Upon Pb exposure, reduced glutathione (GSH) and non-protein thiols were upregulated in shoots and were unaffected/decreased in roots from the NM population, whereas M populations maintained higher levels of flavanols and hydroxycinnamic acids in shoots and triggered GSH in roots and shoots. These differential organ-specific mechanisms seem to be a competitive strategy that allows M populations to overcome Pb toxicity, contrarily to NM, thus stressing the importance of seed provenance in phytostabilisation programs.


Sign in / Sign up

Export Citation Format

Share Document