Myocardial H2O2 production in the unanaesthetized rat Influence of fasting, myocardial load and inhibition of superoxide dismutase and monoamine oxidase

Kerckaert, Ingrid; Roels, Frank

doi:10.1007/bf01907430

Cited by 10 publications

(5 citation statements)

References 54 publications

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“…This is in accordance with a previous in vivo study with rats in which MAO inhibition by phenelzine failed to decrease myocardial basal production of H 2 O 2 (Kerckaert and Roels 1986). Nevertheless, MAO inhibition prevented d-amphetamineinduced production of H 2 O 2 in the heart.…”

Section: Discussionsupporting

confidence: 81%

Hydrogen peroxide production in mouse tissues after acute d -amphetamine administration. Influence of monoamine oxidase inhibition

Carvalho

Duarte

Neuparth

et al. 2001

Archives of Toxicology

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The toxicity of amphetamines is conditioned by a complex array of mechanisms, involving the increase of neurotransmission (e.g. leading to hyperthermia) and enzymatic and non-enzymatic oxidation of amphetamines and biogenic amines. Considering that all these processes may increase the generation of hydrogen peroxide (H2O2) by metabolic or non-metabolic redox pathways, the main objective of this work was to evaluate d-amphetamine-induced H2O2 production in mice liver, kidney and heart. The contribution of monoamine oxidase (MAO) to H2O2 production after d-amphetamine administration was studied using the MAO inhibitor pargyline. H2O2 production was measured indirectly using the catalase-H2O2 complex I irreversible inhibitor 3-amino-1,2,4-triazole (AT). Using this method, the measurement of residual catalase activity following administration of AT permits the monitoring of H2O2 production in vivo. Charles River CD-1 mice (30-35 g body weight) were injected with AT just before the injection of d-amphetamine sulphate (20 mg/kg). d-Amphetamine stimulated the production of H2O2 in all tissues studied, although to different degrees. MAO inhibition by itself led to a remarkable decrease of basal H2O2 production in the kidney and a slight decrease in the liver, although no effect was observed in the heart. d-Amphetamine-induced H2O2 production in the heart and kidney was reduced in MAO-inhibited mice. However, in the liver, H2O2 production was transiently potentiated at 30 min under MAO inhibition. In conclusion, d-amphetamine administration leads to an increase in H2O2 production in mouse liver, kidney and heart, and monoamine oxidase plays an important role in this effect.

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Section: Discussionsupporting

confidence: 81%

Hydrogen peroxide production in mouse tissues after acute d -amphetamine administration. Influence of monoamine oxidase inhibition

Carvalho

Duarte

Neuparth

et al. 2001

Archives of Toxicology

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“…Endocardium, in contrast to other types of endothelium, is surrounded by incessantly active myocardium, a tissue with unusually rapid aerobic metabolism. It has been estimated that as much as 5% of all 02 consumption in heart mitochondria is attributable to "leakage" of electrons from the electron transport chain to reduce 02 to O2-, leading to H202 production (43), and others have documented high rates of myocardial H202 References production (44,45) . Intracellular levels of H202 in tissue with rapid aerobic metabolism have been estimated to be as high as 10-7 M (46), perilously close to the 10 -6 M we infused to cause acute heart failure in our rat heart model (Fig.…”

Section: Discussionmentioning

confidence: 99%

Bromide-dependent toxicity of eosinophil peroxidase for endothelium and isolated working rat hearts: a model for eosinophilic endocarditis.

Slungaard

Mahoney

1991

The Journal of Experimental Medicine

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SummaryEosinophilic endocarditis is a potentially lethal complication of chronic peripheral blood hypereosinophilia. We hypothesized that eosinophil peroxidase (EPO), an abundant eosinophil (EO) cationic granule protein, promotes eosinophilic endocarditis by binding to negatively charged endocardium, and there generating cytotoxic oxidants. Using an immunocytochemical technique, we demonstrated endocardial deposition ofEPO in the heart of a patient with hypereosinophilic heart disease. Because EPO preferentially oxidizes Br-to hypobromous acid (HOBr) rather than Cl-to hypochlorous acid (HOCI) at physiologic halide concentrations, we characterized the Br--dependent toxicity of both activated EOs and purified human EPO towards several types of endothelial cells and isolated working rat hearts . In RPMI supplemented with 100 1,M Br-, phorbol myristate acetate-activated EOs, but not polymorphonuclear leukocytes, caused 1.8-3.6 times as much 51Cr release from four types of endothelial cell monolayers as in RPMI alone. H202 and purified human EPO, especially when bound to cell surfaces, mediated extraordinarily potent, completely Br--dependent cytolysis of endothelial cells that was reversed by peroxidase inhibitors, HOBr scavengers, and competitive substrates. We further modeled eosinophilic endocarditis by instilling EPO into the left ventricles of isolated rat hearts, flushing unbound EPO, then perfusing them with a buffer containing 100 jAM Br -and 1 p,M H202. Acute congestive heart failure (evidenced by a precipitous decrement in rate pressure product, stroke volume work, aortic output, and MV02 to 0-33% of control values) ensued over 20 min, which deletion of EPO, Br-, or H202 completely abrogated . These findings raise the possibility that EPO bound to endocardial cells might utilize H202 generated either by overlying phagocytes or endogenous cardiac metabolism along with the virtually inexhaustible supply of Br-from flowing blood to fuel HOBr-mediated cell damage. By this mechanism, EPO may play an important role in the pathogenesis of eosinophilic endocarditis.

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“…In mice, starvation increases the H 2 O 2 production by liver, likely due to increased fatty acid plasma levels (Van den Branden et al, 1984 ). However, in cardiac tissue there is no change (Kerckaert and Roels, 1986 ). Treatment with fibrates increases the rate of H 2 O 2 production in hepatocytes (Mannaerts et al, 1979 ; Foerster et al, 1981 ; Yamada et al, 1987 ; Leighton et al, 1989 ; Yoshida et al, 1990 ).…”

Section: The Redox Metabolism Of Peroxisomesmentioning

confidence: 99%

Redox interplay between mitochondria and peroxisomes

Lismont

Nordgren

Veldhoven

et al. 2015

Front. Cell Dev. Biol.

160

139

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Reduction-oxidation or “redox” reactions are an integral part of a broad range of cellular processes such as gene expression, energy metabolism, protein import and folding, and autophagy. As many of these processes are intimately linked with cell fate decisions, transient or chronic changes in cellular redox equilibrium are likely to contribute to the initiation and progression of a plethora of human diseases. Since a long time, it is known that mitochondria are major players in redox regulation and signaling. More recently, it has become clear that also peroxisomes have the capacity to impact redox-linked physiological processes. To serve this function, peroxisomes cooperate with other organelles, including mitochondria. This review provides a comprehensive picture of what is currently known about the redox interplay between mitochondria and peroxisomes in mammals. We first outline the pro- and antioxidant systems of both organelles and how they may function as redox signaling nodes. Next, we critically review and discuss emerging evidence that peroxisomes and mitochondria share an intricate redox-sensitive relationship and cooperate in cell fate decisions. Key issues include possible physiological roles, messengers, and mechanisms. We also provide examples of how data mining of publicly-available datasets from “omics” technologies can be a powerful means to gain additional insights into potential redox signaling pathways between peroxisomes and mitochondria. Finally, we highlight the need for more studies that seek to clarify the mechanisms of how mitochondria may act as dynamic receivers, integrators, and transmitters of peroxisome-derived mediators of oxidative stress. The outcome of such studies may open up exciting new avenues for the community of researchers working on cellular responses to organelle-derived oxidative stress, a research field in which the role of peroxisomes is currently highly underestimated and an issue of discussion.

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Myocardial H2O2 production in the unanaesthetized rat Influence of fasting, myocardial load and inhibition of superoxide dismutase and monoamine oxidase

Cited by 10 publications

References 54 publications

Hydrogen peroxide production in mouse tissues after acute d -amphetamine administration. Influence of monoamine oxidase inhibition

Hydrogen peroxide production in mouse tissues after acute d -amphetamine administration. Influence of monoamine oxidase inhibition

Bromide-dependent toxicity of eosinophil peroxidase for endothelium and isolated working rat hearts: a model for eosinophilic endocarditis.

Redox interplay between mitochondria and peroxisomes

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