In vivo cooperation between hepatic catalase and superoxide dismutase demonstrated by diethyldithiocarbamate

Geerts, Albert; Roels, Frank

doi:10.1016/0014-5793(82)80904-6

Cited by 20 publications

(12 citation statements)

References 43 publications

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“…Administration of DDC, as used in myocardium by Guarnieri et al (17), results in an increase of RCA: less H202 is reaching catalase. Similar results were found in the liver of rats (28) and guinea-pig (13). Although SOD is localized outside the peroxisomes, H202 produced by it reaches catalase.…”

Section: Conditions (At + Methanol)supporting

confidence: 90%

“…In order to determine whether SOD contributes to the production of H202 which will be broken down by catalase, we used diethyldithiocarbamate (DDC), an inhibitor of SOD (17,20). In vivo cooperation between catalase and SOD was demonstrated in the liver by means of DDC (13,28). Whether MAO is partially responsible for the production of H202, was examined by means of phenelzine ([3-phenylethylhydrazine), an inhibitor of MAO, belonging to the group of hydrazine derivatives (49).…”

Section: Introductionmentioning

confidence: 99%

“…The formation of this intermediate complex is thus dependent upon H202 production. By measuring the residual catalase activity (RCA), the amount of compound I and hence, H202 production, can be evaluated in vivo (13,61). When H202…”

Section: Introductionmentioning

confidence: 99%

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

Kerckaert

Roels

1986

Basic Res Cardiol

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Myocardial H2O2 production was studied by means of the in vivo administration of aminotriazole (AT), which inactivates the catalase-H2O2 complex compound I. Measurements of the residual catalase activity in male and female rats indicate that beta-oxidation of fatty acids in peroxisomes does not contribute in a substantial way to energy production in response to fasting or to an increased myocardial load, despite previous data on peroxisomes in myocardium. Superoxide dismutase (SOD) inhibition by diethyldithiocarbamate demonstrates that SOD participates in the production of H2O2 in physiological conditions. Such a role was not demonstrated for monoamine oxidase through inhibition by phenelzine.

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Section: Conditions (At + Methanol)supporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

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

Kerckaert

Roels

1986

Basic Res Cardiol

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“…Although catalase activity has been detected in the cytoplasm of sheep, guinea pig, and rhesus monkey liver (Roels, 1976;Roels et al, 1977;Geerts & Roels, 1982;Geerts et al, 1984;Yamamoto et al, 1988), the enzyme is generally considered to be localized mainly in peroxisomes. Under normal physiological conditions, the enzyme and its activity are present in all (micro) peroxisomes, except in human foetus (Espeel et al, 1993a) (Table 4).…”

Section: Catalasementioning

confidence: 99%

In situ heterogeneity of peroxisomal oxidase activities: An update

Munchof

1996

Histochem J

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Oxidases are a widespread group of enzymes. They are present in numerous organisms and organs and in various tissues, cells, and subcellular compartments, such as mitochondria. An important source of oxidases, which is investigated and discussed in this study, are the (micro)peroxisomes. Oxidases share the ability to reduce molecular oxygen during oxidation of their substrate, yielding an oxidized product and hydrogen peroxide. Besides the hydrogen peroxide-catabolizing enzyme catalase, peroxisomes contain one or more hydrogen peroxide-generating oxidases, which participate in different metabolic pathways. During the last four decades, various methods have been developed and elaborated for the histochemical localization of the activities of these oxidases. These methods are based either on the reduction of soluble electron acceptors by oxidase activity or on the capture of hydrogen peroxide. Both methods yield a coloured and/or electron dense precipitate. The most reliable technique in peroxisomal oxidase histochemistry is the cerium salt capture method. This method is based on the direct capture of hydrogen peroxide by cerium ions to form a fine crystalline, insoluble, electron dense reaction product, cerium perhydroxide, which can be visualized for light microscopy with diaminobenzidine. With the use of this technique, it became clear that oxidase activities not only vary between different organisms, organs, and tissues, but that heterogeneity also exists between different cells and within cells, i.e. between individual peroxisomes. A literature review, and recent studies performed in our laboratory, show that peroxisomes are highly differentiated organelles with respect to the presence of active enzymes. This study gives an overview of the in situ distribution and heterogeneity of peroxisomal enzyme activities as detected by histochemical assays of the activities of catalase, and the peroxisomal oxidases D-amino acid oxidase, L-alpha-hydroxy acid oxidase, polyamine oxidase and uric acid oxidase.

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“…In addition, acetaldehyde, the first product of the ethanol degradation, may also stimulate the formation of oxygen-derived free radicals and H20 ~ through aldehyde oxidase and xanthine oxidase [29,64]. Finally, H202 is detoxified by peroxisomal or cytoplasmic catalase [19,42].…”

Section: Discussionmentioning

confidence: 99%

Variations in peroxisomal catalase of neonatal rat hepatocyte subpopulations

Tolosa¹,

Azorı́n

Sancho‐Tello³

et al. 1995

Vichows Archiv A Pathol Anat

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Alcohol consumption during pregnancy is teratogenic and induces severe alterations in hepatocytes. In the hepatocyte peroxisomal system, ethanol is converted in the presence of H2O2 to acetaldehyde and water. Therefore, peroxisomal catalase also acts as an antioxidant defence mechanism by removing H2O2 and preventing the formation of hydroxyl radicals in the cell. Alterations in peroxisomal catalase after pre- and pre+postnatal alcohol exposure were investigated in the rat. The effect of pre- and postnatal exposure to ethanol on hepatocyte subpopulations was analysed in isolated hepatocytes originating from periportal, intermediate and perivenous zones. Analysis of catalase revealed that the total activity and content of this enzyme were higher in 12-day-old cells than in cells from newborns and that this increment was more pronounced in treated cells. In controls, the amount of peroxisomal catalase increased mainly in periportal cells, whereas alcohol exposure induced a significant increase in the catalase of perivenous hepatocytes. We conclude that pre- and postnatal alcohol exposure mainly affects the perivenous hepatocyte peroxisomes and that the increase in peroxisomal catalase could constitute a defence mechanism against free radical generation induced by alcohol exposure during the perinatal period.

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In vivo cooperation between hepatic catalase and superoxide dismutase demonstrated by diethyldithiocarbamate

Cited by 20 publications

References 43 publications

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

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

In situ heterogeneity of peroxisomal oxidase activities: An update

Variations in peroxisomal catalase of neonatal rat hepatocyte subpopulations

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