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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of clofibrate treatment on hepatic ketogenic capacity was studied in rats. Ketogenesis from octanoate and oleate was increased 2- and 4,5-fold, respectively, in hepatocytes from fed, treated rats. In contrast to controls ketogenic rates did not increase upon starvation. While ketogenesis from oleate was higher in fed, treated animals than in fasted controls, endogenous ketogenesis was lower and increased upon starvation. Ketogenesis from octanoate and oleate was stimulated approx. 2-fold in homogenates from treated animals. Labeled pyruvate and succinate oxidation was unaltered. [1-14C]Oleate oxidation was severely inhibited by cyanide, both in homogenates from controls and treated animals. Clofibrate caused a 3-fold increase in hepatic carnitine levels. Catalase and glutamate dehydrogenase activities were also increased by the drug. Cytochrome c oxidase did not change. Despite their increased ketogenic capacity hepatocytes from treated rats esterified as much oleate as controls. The increased oxidation was matched by an increased oleate uptake. Plasma ketones were increased 2-fold in fasted, treated animals. Plasma free fatty acids were unaffected. It is concluded that the enhanced ketogenic capacity induced by clofibrate is the result of an increase in mitochondrial beta-oxidation, an increase in the activity of carnitine palmitoyltransferase and possibly of the observed increases in hepatic carnitine content and fatty acid uptake.
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PMID:Hepatic fatty acid oxidation and ketogenesis after clofibrate treatment. 65 51

The effects of the hepatic peroxisome proliferators (HPPs) clofibrate, di-(2-ethylhexyl)-phthalate (DEHP), mono-(2-ethylhexyl)phthalate (MEHP) and 2,4-dichlorophenoxy acetic acid (2,4-D) on the activities of some peroxisome-associated enzymes and marker enzymes for other organelles, have been studied in primary Syrian hamster embryo (SHE) cells and Wistar rat embryo (WRE) cells. The majority of the cells are fibroblast-like. 12-O-Tetradecanoyl phorbol-13-acetate (TPA) was included as it has been suggested that it may act as a peroxisome proliferator. The specific activities of catalase, fatty acyl-CoA oxidase (FAO) and peroxisomal beta-oxidation were approximately 100-fold lower in the embryonic cells than in rat hepatocytes. Other peroxisome-associated oxidases were not detected. The dihydroxyacetone-phosphate acyltransferase (DHAPAT) activity was comparable to that in rat liver. Marker enzymes for other organelles had specific activities comparable to rat hepatocytes. Catalase was shown by digitonin titration to be contained in a peroxisome-like compartment in both SHE and WRE cells. Clofibrate, DEHP and MEHP increased the catalase activity, which might suggest peroxisome proliferation. However, the findings that FAO and peroxisomal beta-oxidation did not increase or only very slightly, argue against peroxisome proliferation. 2,4-D and TPA induced no or only a very slight increase in the catalase activity.
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PMID:Effects of hepatic peroxisome proliferators and 12-O-tetradecanoyl phorbol-13-acetate on catalase and other enzyme activities of embryonic cells in vitro. 230 65

Catalase activity in the heart of male rabbits was 21% of that found in the liver; clofibrate feeding (0.3% w/w for 10 days) resulted in an 80% increase in both cardiac and hepatic catalase activities. Fatty acyl-CoA oxidase activity in control heart was 11% of that found in control liver; this peroxisomal activity did not increase subsequent to clofibrate feeding. Only acyl-CoA hydrolase activity in the cardiac supernatant was elevated by clofibrate feeding. Acylcarnitine hydrolase activity was increased significantly in the homogenate, extract and supernatant of both heart and liver from the clofibrate-fed rabbit. Clofibrate feeding increased CoASH and carnitine tissue levels in heart and liver.
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PMID:Cardiac and hepatic acyl-CoA and acylcarnitine hydrolase activities in clofibrate-fed rabbits. 286 Oct 21

The intracellular localization of soluble epoxide hydrolase and catalase was investigated in hepatocytes from untreated and clofibrate-treated male C57B1/6 mice and from untreated male Sprague-Dawley rats. Polyclonal rabbit antibodies directed against purified mouse liver cytosolic epoxide hydrolase and rat liver catalase were used and their specificity ascertained by Ouchterlony immunodiffusion and immunoblotting. The IgG fraction was purified and incubated with cryosections of isolated hepatocytes or liver tissue, priorly fixed in 4% paraformaldehyde, and protein-A gold conjugates were used to visualize the antigen-antibody reaction. The soluble form(s) of epoxide hydrolase was found to be localized in the matrix of peroxisomes in hepatocytes from normal and clofibrate-treated mice and normal rats. No significant reactivity was found against plasma membrane, nuclei, mitochondria, the Golgi apparatus, endoplasmic reticulum, lysosomes, or cytosol. Catalase was also localized to peroxisomes in all samples investigated. Accordingly, both the catalase and the epoxide hydrolase activities routinely recovered in the high-speed supernatant after subfractionation of rat and mouse liver tissue mostly seemed to be due to extensive matrix leakage from peroxisomes, and this phenomenon may also be found in other species. Rat hepatocytes contained less epoxide hydrolase than mouse hepatocytes, as judged by both immunocytochemical labeling and biochemical data. Clofibrate treatment of mice decreased the labeling density of epoxide hydrolase and catalase in hepatocytes peroxisomes, as expected, and more unlabeled peroxisomes were observed.
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PMID:Immunocytochemical analysis of soluble epoxide hydrolase and catalase in mouse and rat hepatocytes demonstrates a peroxisomal localization before and after clofibrate treatment. 318 Nov 62