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• W2074034799 abstract "By feeding rats a diet containing 20% (w/w) partially hydrogenated fish oil (PHFO), an apparent 6.3-fold increase in the cyanide insensitive palmitoyl-CoA-dependent NAD+ reduction was observed for the heart peroxisomal fractions. This finding was confirmed by a 7.6-fold and 7.9-fold increase in the specific activity of fatty acyl-CoA oxidase, with palmitoyl-CoA and erucoyl-CoA as the substrates, respectively. Immunoblots after SDS-PAGE of rat heart peroxisomal fractions revealed a 12-fold increase in the 52 kDa fatty acyl-CoA oxidase (FAO) subunit for PHFO-fed rats, whereas the 72 kDa subunit of FAO and several other peroxisomal proteins (including the trifunctional enzyme Δ3, Δ2-enoyl-CoA isomerase, 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase) increased only 2- to 3-fold. The increase in the 52 kDa subunit was markedly higher than the increase in the steady-state mRNA level of FAO (2.0-fold), and is most likely caused by a rather selective stabilization of the 52 kDa FAO subunit. Interestingly, PHFO feeding caused a larger increase in fatty acyl-CoA oxidase and catalase activities than did clofibrate in the heart. The opposite was the case in the liver, especially for fatty acyl-CoA oxidase. Rats fed a semisynthetic diet containing 6% (w/w) erucic acid (C22:1(n − 9), cis) or brassidic acid (C22:1(n − 9), trans) revealed a 5-fold and 3-fold increase vs. the control (pellet fed) rats in heart FAO activity, respectively, as well as a proportional and selective increase in the specific content of 52 kDa FAO subunit. Thus, the relatively high content of C22 monoene fatty acids appears to be one of the main factors responsible for the increase in rat heart peroxisomal FAO activity during PHFO feeding. However, the PHFO diet increased the heart peroxisomal FAO activity more than diets containing a similar amount of C22:1 in the form of erucic or brassidic acid, and additional compounds of lipid or a more xenobiotic nature may also play a role. SDS-PAGE electrophoresis of highly purified rat liver peroxisomes revealed that the specific content of polypeptides with mobilities corresponding to that of the β-oxidation enzyme system, increased by a factor of < 2 as a result of feeding the PHFO diet. The 3.1-fold increase in cyanide insensitive palmitoyl-CoA-dependent NAD+ reduction was comparable to the increase (4.1-fold) in the acyl-CoA oxidase activity. Immunoblots of 1-D SDS-PAGE of rat heart peroxisomal fractions revealed a p48 protein which increased 8- to 10-fold after PHFO feeding, but only 2.2-fold after clofibrate administration. This may represent the same protein as the membrane protein of 48 kDa demonstrated to increase in isolated liver peroxisomes as a result of PHFO feeding, but not after clofibrate administration. It is concluded that PHFO feeding increases heart peroxisomal β-oxidation activity partly by an induction of the peroxisomal ,0-oxidation enzymes, but mainly by a rather selective stabilization of the 52 kDa subunit of acyl-CoA oxidase. The regulation of the peroxisomal β-oxidation system is different in the heart and liver." @default.
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• W2074034799 date "1995-03-01" @default.
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• W2074034799 title "On the mechanism of stimulation of peroxisomal β-oxidation in rat heart by partially hydrogenated fish oil" @default.
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• W2074034799 doi "https://doi.org/10.1016/0005-2760(94)00207-f" @default.
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