Human Erythrocytes Are Protected against Chromate-Induced Peroxidation

Férnandes, Meg da Silva; Mota, Idalina M.; Silva, Maria T.L.; Oliveira, Catarina R.; Geraldes, Carlos F. G. C.; Alpoím, Maria C.

doi:10.1006/eesa.1998.1755

Cited by 5 publications

(12 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Previous studies performed in our laboratory showed that chromate-induced haemoglobin oxidation and membrane peroxidation in human erythrocytes (Alpoim et al, 1995;Fernandes et al, 1999). It also promoted oxidation of GSH, inhibition of glutathione reductase and methaemoglobin reductase, and the echinocytic shape transformation of erythrocytes.…”

Section: Introductionmentioning

confidence: 77%

“…In our recent study, it was suggested that during the intracellular human erythrocytes chromium(VI) reduction to chromium(V) intermediates, by glutathione, glutathione reductase and NADH-methaemoglobin reductase, ROS are produced via the Haber-Weiss cycle or through a Fenton-like reaction (Fernandes, et al, 1999). It was also suggested that chromate-induced human erythrocytes haemoglobin oxidation is due to the electron transfers between the haemoglobin-Fe 2 + and chromium(V) intermediates, and that chromate-induced haemoglobin oxidation protects the cells against chromate-induced peroxidation (Fernandes et al, 1999).…”

Section: Discussionmentioning

confidence: 99%

“…It was also suggested that chromate-induced human erythrocytes haemoglobin oxidation is due to the electron transfers between the haemoglobin-Fe 2 + and chromium(V) intermediates, and that chromate-induced haemoglobin oxidation protects the cells against chromate-induced peroxidation (Fernandes et al, 1999). The oxidation of haemoglobin (Alpoim et al, 1995), which is the main protein inside human erythrocytes will readily reduce chromium(VI) and chromium(V) to the stable oxidation state chromium(III), which remain bound to the oxidized protein (Connett and Wetterhahn, 1983) not allowing ROS generation.…”

Section: Discussionmentioning

confidence: 99%

“…It also promoted oxidation of GSH, inhibition of glutathione reductase and methaemoglobin reductase, and the echinocytic shape transformation of erythrocytes. However, chromate was without effect on the activities of catalase, gluthatione peroxidase, and superoxide dismutase, as well as on the osmotic fragility of the cells (Fernandes et al, 1999). Based on these findings it was suggested that chromate may be cytotoxic to human erythrocytes.…”

Section: Introductionmentioning

confidence: 96%

“…Based on these findings it was suggested that chromate may be cytotoxic to human erythrocytes. It should be taken into account that in human erythrocytes the intracellular redox balance glutathione reduced/glutathione oxidized, haemoglobin/methaemoglobin ratio, and the cell shape, which are crucial for cell functions and survival, are irreversibly disrupted (Fernandes et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Chromate-induced human erythrocytes haemoglobin oxidation and peroxidation: influence of vitamin E, vitamin C, salicylate, deferoxamine, and N-ethylmaleimide

Férnandes¹,

Geraldes²,

Oliveira³

et al. 2000

Toxicology Letters

View full text Add to dashboard Cite

In order to attenuate or to prevent chromate-induced human erythrocytes injury, the influence of vitamin E, vitamin C, salicylate, deferoxamine, and N-ethylmaleimide on chromate-induced human erythrocytes haemoglobin oxidation and peroxidation were investigated. It was observed that pretreatment of human erythrocytes with vitamin E (20 mM), vitamin C (1 mM), salicylate (3 mM), and deferoxamine (4 mM) significantly increased (P =0.0001) chromate-induced human erythrocytes haemoglobin oxidation in a time dependent manner, while it was significantly decreased (P= 0.0001) by pretreatment with N-ethylmaleimide (1 mM). In contrast, pretreatment of human erythrocytes with deferoxamine (4 mM) immediately inhibited (P =0.0001) chromate-induced human erythrocytes peroxidation, while it was significantly increased (P= 0.0001) by pretreatment with N-ethylmaleimide (1 mM) during the first 4 h of cells exposition to chromate. For time periods superior to 6 h pretreatment with N-ethylmaleimide (1 mM) significantly decreased (P=0.0001) chromate-induced human erythrocytes peroxidation. It was concluded that care must be taken as these drugs are used to prevent against toxicity induced by chromium(VI) compounds.

show abstract

Section: Introductionmentioning

confidence: 77%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Chromate-induced human erythrocytes haemoglobin oxidation and peroxidation: influence of vitamin E, vitamin C, salicylate, deferoxamine, and N-ethylmaleimide

Férnandes¹,

Geraldes²,

Oliveira³

et al. 2000

Toxicology Letters

View full text Add to dashboard Cite

show abstract

Effects of NADH and H2O2 on Chromate-Induced Human Erythrocytes Hemoglobin Oxidation and Peroxidation

Férnandes

Geraldes

Oliveira

et al. 2000

Ecotoxicology and Environmental Safety

Self Cite

View full text Add to dashboard Cite

The effects of NADH and H(2)O(2) on chromate-induced human erythrocyte hemoglobin oxidation and peroxidation were studied. It was observed that NADH decreases the levels of chromate-induced human erythrocyte hemoglobin oxidation and peroxidation. H(2)O(2) decreases the levels of chromate-induced hemoglobin oxidation, but increases the levels of chromate-induced peroxidation. The ability of H(2)O(2) to decrease the levels of chromate-induced hemoglobin oxidation is higher than that observed for NADH. Furthermore, H(2)O(2) increases the inhibitory effect of NADH on chromate-induced hemoglobin oxidation, but decreases the NADH effect on chromate-induced peroxidation. The meaning of these results is discussed in terms of involvement of reactive chromium(V) species and reactive oxygen species in the mechanism by which chromate induces its effects in human erythrocytes.

show abstract

The effects of chromium(VI) on the thioredoxin system: Implications for redox regulation

Myers

2012

Free Radical Biology and Medicine

View full text Add to dashboard Cite

Hexavalent chromium [Cr(VI)] compounds are highly redox active and have long been recognized as potent cytotoxins and carcinogens. The intracellular reduction of Cr(VI) generates reactive Cr intermediates, which are themselves strong oxidants, as well as superoxide, hydrogen peroxide, and hydroxyl radical. These probably contribute to the oxidative damage and effects on redox-sensitive transcription factors that have been reported. However, the identification of events that initiate these signaling changes has been elusive. More recent studies show that Cr(VI) causes irreversible inhibition of thioredoxin reductase (TrxR) and oxidation of thioredoxin (Trx) and peroxiredoxin (Prx). Mitochondrial Trx2/Prx3 are more sensitive to Cr(VI) treatment than cytosolic Trx1/Prx1, although both compartments show thiol oxidation with higher doses or longer treatments. Thiol redox proteomics demonstrate that Trx2, Prx3, and Trx1 are among the most sensitive proteins in cells to Cr(VI) treatment. Their oxidation could therefore represent initiating events that have widespread implications for protein thiol redox control and for multiple aspects of redox signaling. This review summarizes the effects of Cr(VI) on the TrxR/Trx system and how these events could influence a number of downstream redox signaling systems that are influenced by Cr(VI) exposure. Some of the signaling events discussed include the activation of apoptosis signal regulating kinase and MAP kinases (p38 and JNK) and the modulation of a number of redox-sensitive transcription factors including AP-1, NF-κB, p53, and Nrf2.

show abstract

Human Erythrocytes Are Protected against Chromate-Induced Peroxidation

Cited by 5 publications

References 42 publications

Chromate-induced human erythrocytes haemoglobin oxidation and peroxidation: influence of vitamin E, vitamin C, salicylate, deferoxamine, and N-ethylmaleimide

Chromate-induced human erythrocytes haemoglobin oxidation and peroxidation: influence of vitamin E, vitamin C, salicylate, deferoxamine, and N-ethylmaleimide

Effects of NADH and H2O2 on Chromate-Induced Human Erythrocytes Hemoglobin Oxidation and Peroxidation

The effects of chromium(VI) on the thioredoxin system: Implications for redox regulation

Contact Info

Product

Resources

About