Comparison of Oxygen Radical Generation from the Reductive Activation of Doxorubicin, Streptonigrin, and Menadione by Xanthine Oxidase and Xanthine Dehydrogenase

Yee, Steven B.; Pritsos, Chris A.

doi:10.1006/abbi.1997.0340

Cited by 54 publications

(24 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Within the cell, bioreductive activation of ADR is possible through interaction with several oxidoreductases (Bachur et al, 1982). NADPHdependent cytochrome P450 reductases of the endoplasmic reticulum (Bachur et al, 1977) and nuclear envelope (Bachur et al, 1982), along with NADH dehydrogenase (complex I) of the mitochondrial electron transport chain (ETC) Doroshow et al, 1986) and cytosolic xanthine oxidase (Pan et al, 1980;Yee et al, 1997), are all capable of converting ADR to a semiquinone radical via univalent reduction. This semiquinone radical can rapidly auto-oxidize using molecular oxygen as an electron acceptor, reverting to the parent compound with no net metabolism of the drug (Figure 2).…”

Section: Generation Of Ros Through Redox Cycling Of Adrmentioning

confidence: 97%

Adriamycin-induced oxidative mitochondrial cardiotoxicity

2006

View full text Add to dashboard Cite

The anticancer agent Adriamycin (ADR) has long been recognized to induce a dose-limiting cardiotoxicity. Numerous studies have attempted to characterize and elucidate the mechanism(s) behind its cardiotoxic effect. Despite a wealth of data covering a wide-range of effects mediated by the drug, the definitive mechanism remains a matter of debate. However, there is consensus that this toxicity is related to the induction of reactive oxygen species (ROS). Induction of ROS in the heart by ADR occurs via redox cycling of the drug at complex I of the electron transport chain. Many studies support the theory that mitochondria are a primary target of ADR-induced oxidative stress, both acutely and long-term. This review focuses on the effects of ADR redox cycling on the mitochondrion, which support the hypothesis that these organelles are indeed a major factor in ADR cardiotoxicity. This review has been constructed with particular emphasis on studies utilizing cardiac models with clinically relevant doses or concentrations of ADR in the hope of advancing our understanding of the mechanisms of ADR toxicity. This compilation of current data may reveal valuable insights for the development of therapeutic strategies better tailored to minimizing the dose-limiting effect of ADR.

show abstract

Section: Generation Of Ros Through Redox Cycling Of Adrmentioning

confidence: 97%

Adriamycin-induced oxidative mitochondrial cardiotoxicity

2006

View full text Add to dashboard Cite

show abstract

“…Doxorubicin has been shown to enhance the activity of http://dx.doi.org/10.1016/j.cbi.2015.05.013 0009-2797/Ó 2015 Elsevier Ireland Ltd. All rights reserved. xanthine oxidase, which is considered as one of the mechanisms responsible for the generation of free radicals on administration of doxorubicin [8,9].…”

Section: Introductionmentioning

confidence: 99%

Febuxostat ameliorates doxorubicin-induced cardiotoxicity in rats

Krishnamurthy

Rani

Bharti

et al. 2015

Chemico-Biological Interactions

View full text Add to dashboard Cite

“…Kume et al [9] reported that doxorubicin (DXR) could induce HSR, which attenuated hepatic warm ischemia reperfusion injury. DXR is a kind of cytotoxic agent and may induce HSR [10] . Being administered intravenously, DXR was accumulated and metabolized in liver.…”

Section: Introductionmentioning

confidence: 99%

Protective effect of doxorubicin induced heat shock protein 72 on cold preservation injury of rat livers

Chen

Yu²,

Zhang³

et al. 2004

WJG

View full text Add to dashboard Cite

AIM:To observe the protective effect of heat shock protein 72 (HSP 72) induced by pretreatment of doxorubicin (DXR) on long-term cold preservation injury of rat livers. METHODS:Sprague-Dawley rats were administered intravenously DXR at a dose of 1 mg/kg body mass in DXR group and saline in control group. After 48 h, the rat liver was perfused with cold Linger's and University of Wisconsin (UW) solutions and then was preserved in UW solution at 4 for 24, 36 and 48 h. AST, ALT, LDH and hyaluronic acid in preservative solution were determined. Routine HE, immunohistochemical staining for HSP 72 and electron microscopic examination of hepatic tissues were performed. RESULTS:After 24, 36 and 48 h, the levels of AST, ALT and hyaluronic acid in preservative solution were significantly higher in control group than in DXR group (P<0.05), while LDH level was not significantly different between the 2 groups (P>0.05). Hepatic tissues in DXR group were morphologically normal and significantly injured in control group. HSP 72 was expressed in hepatocytes and sinusoidal endothelial cells in DXR group but not in control group.CONCLUSION: Pretreatment of DXR may extend the time of rat liver cold preservation and keep liver alive. The expression of HSP 72 in liver can prevent hepatocytes and sinusoidal endothelial cells from long-term cold preservation injury.

show abstract

Comparison of Oxygen Radical Generation from the Reductive Activation of Doxorubicin, Streptonigrin, and Menadione by Xanthine Oxidase and Xanthine Dehydrogenase

Cited by 54 publications

References 26 publications

Adriamycin-induced oxidative mitochondrial cardiotoxicity

Adriamycin-induced oxidative mitochondrial cardiotoxicity

Febuxostat ameliorates doxorubicin-induced cardiotoxicity in rats

Protective effect of doxorubicin induced heat shock protein 72 on cold preservation injury of rat livers

Contact Info

Product

Resources

About