Cadmium activates the mitogen-activated protein kinase (MAPK) pathway via induction of reactive oxygen species and inhibition of protein phosphatases 2A and 5

Chen, Long; Liu, Lei; Huang, Shile

doi:10.1016/j.freeradbiomed.2008.07.011

Cited by 246 publications

(237 citation statements)

References 55 publications

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“…It is found widely in nature and present in air, all soils and aquatic systems and mainly released from the burning of fossil fuels, regional wastes and metals refining (Chen et al, 2008;Kour et al, 2014). Raised levels of Cd in soil may be found as a result of agricultural activities (e.g.…”

Section: Introductionmentioning

confidence: 99%

The role of vitamin E or clay in growing Japanese quail fed diets polluted by cadmium at various levels

Abou-Kassem

Mahrose

Alagawany

2016

Animal

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This study was conducted to verify whether vitamin (Vit) E or natural clay as feed additives has the potential to modulate the deleterious effects resulting from exposure to cadmium (Cd) in growing Japanese quail. 648 Japanese quail chicks (1 week old) were used to evaluate the effects of dietary Cd (0, 40, 80 and 120 mg/kg diet) and two levels of Vit E (0, 250 mg/kg diet) or two levels of natural clay (0 and 100 mg/kg diet) to study the influences of Cd, Vit E, clay or their different combinations on growth performance, carcass traits, some blood biochemical components and Cd residues in muscles and liver. Live BW and weight gain of quails were linearly decreased with increasing dietary Cd levels. Moreover, feed conversion was significantly worsened with increasing Cd level. Mortality percentage was linearly increased as dietary Cd level increased up to 120 mg/kg diet. Carcass percentage was linearly decreased as dietary Cd level increased. While, giblets percentage were linearly and quadratically differed as dietary Cd level increased. Cd caused significant changes in total plasma protein, albumin, globulin, A/G ratio, creatinine, urea-N and uric acid concentrations as well as ALT, AST and ALP activities. Increasing dietary Cd level was associated with its increase in the muscles and liver. Dietary supplementation with 250 mg of Vit E/kg diet or 100 mg clay/kg improved live BW, BW gain and feed conversion when compared with the un-supplemented diet. Quails fed diet contained 250 mg Vit E/kg and those fed 100 mg clay/kg had the highest percentages of carcass and dressing than those fed the un-supplemented diet. Blood plasma biochemical components studied were better when birds received 250 mg of Vit E/kg diet and those received 100 mg clay/kg. Cd residues in the muscles and liver were significantly less in the birds had 250 mg of Vit E/kg or those received 100 mg clay/kg diet than those un-supplemented with Vit E. Growth performance traits and blood plasma biochemical components studied were significantly affected linearly by the interactions among Cd and each of Vit E and clay levels. In conclusion, the present results indicate that the deleterious effects induced by Cd plays a role in decreasing the performance of Japanese quail and that dietary supplementation with natural clay or Vit E may be useful in partly alleviating the adverse effects of Cd.

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Section: Introductionmentioning

confidence: 99%

The role of vitamin E or clay in growing Japanese quail fed diets polluted by cadmium at various levels

Abou-Kassem

Mahrose

Alagawany

2016

Animal

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“…It could be that other SMAD2/3 interacting partners could be dephosphorylated by PP5. Thirdly, PP5 has been implicated in the regulation of multiple pathways, including adipogenesis by controlling the GRα and PPARγ phosphorylation (34), DNA-damage repair by controlling the ATM/ATR/Chk1 and p53 pathway components (21,31,34-37), MAPK-mediated growth and differentiation (38)(39)(40)(41)(42)(43)(44), and cell cycle arrest (45). Interestingly, GRα has also been implicated in the repression of the TGFβ pathway by its association with SMAD3 (46).…”

Section: Discussionmentioning

confidence: 99%

Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor‐β pathway

Bruce

Macartney

Yong

et al. 2012

Cellular Signalling

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Protein phosphatases play a key role in balancing cellular responses to transforming growth factor-β (TGFβ) signals. Several protein phosphatases have been attributed roles in the regulation of the TGFβ pathway. Among these, PPM1A is the only phosphatase reported to dephosphorylate SMAD2/3 in the nucleus. However we observed PPM1A exclusively in the cytoplasmic fractions independently of TGFβ treatment in all cells tested. These observations imply that a bona fide nuclear SMAD2/3 phosphatase remains elusive. In this study, we report a role for protein phosphatase 5 (PP5) in the TGFβ pathway. We identified PP5 as an interactor of SMAD2/3. Interestingly, in mouse embryonic fibroblast cells derived from PP5-null mice, TGFβ-induced transcriptional responses were significantly enhanced. This enhancement is due to the increased levels of SMAD3 protein observed in PP5-null MEFs compared to the wild type. No differences in the levels of SMAD3 transcripts were observed between the wild type and PP5-null MEFs. While PP5 is capable of dephosphorylating SMAD3-tail in overexpression assays, we demonstrate that its activity is essential in controlling SMAD3 protein levels in MEFs. We propose that PP5 regulates the TGFβ pathway in MEFs by regulating the expression of SMAD3 protein levels.

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“…Under oxidative stress, ROS, including free radicals such as superoxide (O 2 -), hydroxyl radical (HO -) and H 2 O 2 , are generated at high levels (12,30). Excessive amounts of ROS induced by oxidative stress may modify protein, lipids and DNA and alter their functions, resulting in apoptosis of neuronal cells (19,31).…”

Section: Discussionmentioning

confidence: 99%

“…In neuronal cells, the p38 signaling pathway is preferentially activated by inflammatory cytokines and environmental stress, such as osmotic stress, ultraviolet light, heat shock and hypoxia. It can also be activated by ROS (12,(18)(19)(20)(21). Previous studies have demonstrated that p38MAPK activation is implicated in neuronal damage associated with ischemia and neurodegenerative disease (32), and it is one of the apoptotic markers during PC12 cell death induced by a variety of stimuli (15)(16)(17)(18).…”

Section: Discussionmentioning

confidence: 99%

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Interaction between ROS and p38MAPK contributes to chemical hypoxia-induced injuries in PC12 cells

et al. 2011

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Abstract. The present study investigated whether there is an interaction between reactive oxygen species (ROS) and p38 mitogen-activated protein kinase (MAPK) during chemical hypoxia-induced injury in PC12 cells. The results of the present study showed that cobalt chloride (CoCl 2 ), a chemical hypoxia agent, markedly induced ROS generation and phosphorylation of p38MAPK, as well as neuronal injuries. N-acetylcysteine (NAC), a ROS scavenger, blocked CoCl 2 -induced phosphorylation of p38MAPK. In addition, SB203580, an inhibitor of p38MAPK attenuated not only CoCl 2 -induced activation of p38MAPK, but also ROS production. These results suggest that ROS and p38MAPK are capable of interacting positively during chemical hypoxia. Furthermore, NAC and SB203580 markedly prevented CoCl 2 -induced cytotoxicity, apoptosis and a loss of mitochondrial membrane potential. Taken together, our findings suggest that the positive interaction between CoCl 2 induction of ROS and p38MAPK activation may play a significant role in CoCl 2 -induced neuronal injuries. We provide new insights into the mechanisms responsible for CoCl 2 -induced injuries in PC12 cells.

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Cadmium activates the mitogen-activated protein kinase (MAPK) pathway via induction of reactive oxygen species and inhibition of protein phosphatases 2A and 5

Cited by 246 publications

References 55 publications

The role of vitamin E or clay in growing Japanese quail fed diets polluted by cadmium at various levels

The role of vitamin E or clay in growing Japanese quail fed diets polluted by cadmium at various levels

Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor‐β pathway

Interaction between ROS and p38MAPK contributes to chemical hypoxia-induced injuries in PC12 cells

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