| 1. |
- Basu, Samar, et al.
(author)
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Time course and attenuation of ischaemia-reperfusion induced oxidative injury by propofol in human renal transplantation
- 2007
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In: Redox report. - 1351-0002 .- 1743-2928. ; 12:4, s. 195-202
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Journal article (peer-reviewed)abstract
- Ischaemia-reperfusion injury resulting from interruption and restoration of blood flow might be related to free radical mediated oxidative stress and inflammation, and subsequently to post-surgery related complications. We studied the impact of renal transplantation on oxidative stress and inflammation by measuring F2-isoprostanes and prostaglandin F2α, respectively, during transplantation and post-surgery. Additionally, due to earlier observations, two dissimilar anaesthetic agents (thiopentone and propofol) were compared to determine their antioxidative capacity rather than their anaesthetic properties. Blood samples were collected before, post-intubation, immediately, 30, 60,120, 240 min, and 12 and 24 h after reperfusion. Oxidative stress and inflammatory response were detected by measuring 8-iso-PGF2α (a major F2-isoprostane and a biomarker of oxidative stress) and 15-keto-dihydro-PGF2α (a major metabolite of PGF2α and a biomarker of COX-mediated inflammatory response), respectively. Reperfusion of the transplanted graft significantly increased plasma levels of 8-iso-PGF2α. PGF2α metabolite levels, although elevated, did not reach statistical significance. In addition, significantly lower levels of 8-iso-PGF2a were observed in the propofol group compared to the thiopentone group. Together, these findings underline an augmented oxidative stress activity following an inflammatory response after human renal transplantation. Furthermore, propofol a well-known anaesthetic, counteracted oxidative stress by lowering the formation of a major F2-isoprostane.
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| 2. |
- Neuzil, J., et al.
(author)
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Mitochondria transmit apoptosis signalling in cardiomyocyte-like cells and isolated hearts exposed to experimental ischemia-reperfusion injury
- 2007
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In: Redox report. - 1351-0002 .- 1743-2928. ; 12:3, s. 148-162
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Journal article (peer-reviewed)abstract
- Ischemia-reperfusion (I/R) is a condition leading to serious complications due to death of cardiac myocytes. We used the cardiomyocyte-like cell line H9c2 to study the mechanism underlying cell damage. Exposure of the cells to simulated I/R lead to their apoptosis. Over-expression of Bcl-2 and Bcl-xL protected the cells from apoptosis while over-expression of Bax sensitized them to programmed cell death induction. Mitochondria-targeted coenzyme Q (mitoQ) and superoxide dismutase both inhibited accumulation of reactive oxygen species (ROS) and apoptosis induction. Notably, mtDNA-deficient cells responded to I/R by decreased ROS generation and apoptosis. Using both in situ and in vivo approaches, it was found that apoptosis occurred during reperfusion following ischemia, and recovery was enhanced when hearts from mice were supplemented with mitoQ. In conclusion, I/R results in apoptosis in cultured cardiac myocytes and heart tissue largely via generation of mitochondria-derived superoxide, with ensuing apoptosis during the reperfusion phase. © W. S. Maney & Son Ltd.
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| 3. |
- Rodgers, Kenneth J, et al.
(author)
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Heat shock proteins : keys to healthy ageing?
- 2009
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In: REDOX REPORT. - 1351-0002. ; 14:4, s. 147-153
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Research review (other academic/artistic)abstract
- Organisms produce reactive species throughout their lives, and this may result in damage to proteins and other biological molecules. Oxidatively damaged proteins are normally selectively degraded and replaced, but this process appears to be less efficient in senescent, long-lived post-mitotic cells, as is evidenced by their accumulation in the form of lipofuscin inside the lysosomal compartment. A great deal of research has focused on changes to the proteolytic machinery in the ageing cells in particular the proteasomes although failure of heat shock proteins (HSPs) to bind and deliver oxidised proteins efficiently to the degradation machinery could also contribute to their aggregation and accumulation. Oxidised proteins can be protease-resistant and may even directly inhibit the proteolytic machinery of the cellu The critical role that is played by HSPs in preventing accumulation of oxidised proteins is often overlooked. In this reviews we examine the key role played by HSPs in recognising, removing and preventing the formation of oxidised and damaged proteins in cells. We also examine the evidence supporting the view that failure of one of these pathways could underlie ageing and age-related diseases. Finally, we discuss how modulation of HSP-activity could influence the ageing process and the progression of age-related diseases.
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