Effect of Lipid Peroxides on Fat Absorption and Folic Acid Status in the Rat

Cutler, Margaret G.; Hayward, M.

doi:10.1159/000175476

Cited by 7 publications

(2 citation statements)

References 18 publications

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“…Monitoring and control of lipid peroxidation in food are of great importance due to increasing demand for good quality products. Lipid peroxidation, the oxidative deterioration of the polyunsaturated lipids of food, leads through formation of hydroperoxides to short-chain aldehydes, ketones, and other oxygenated compounds which are considered to be responsible for the development of rancidity in stored foods (Gray, 1978;Melton, 1983;Wong, 1989) and related to experimental heart disease, cancer, and aging in animals (Ohio and Tappel, 1969;Kaunitz and Johnson, 1973;Cutler and Hayward, 1974). Malondialdehyde (MDA), a major degradation product of lipid hydroperoxides, has attracted much attention as a marker for assessing the extent of lipid peroxidation (Raharjo and Sofos, 1993).…”

Section: Introductionmentioning

confidence: 99%

Rapid, Sensitive, and Specific Thiobarbituric Acid Method for Measuring Lipid Peroxidation in Animal Tissue, Food, and Feedstuff Samples

Botsoglou¹,

Fletouris²,

Παπαγεωργίου³

et al. 1994

J. Agric. Food Chem.

819

466

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Section: Introductionmentioning

confidence: 99%

Rapid, Sensitive, and Specific Thiobarbituric Acid Method for Measuring Lipid Peroxidation in Animal Tissue, Food, and Feedstuff Samples

Botsoglou¹,

Fletouris²,

Παπαγεωργίου³

et al. 1994

J. Agric. Food Chem.

819

466

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“…Thus, high peroxide values occur after prolonged storage, exposure to sunlight, increased temperatures, and contact with iron or copper as in cooking vessels (Frazer, 1962). Dietary fatty acid hydroperoxides can be toxic to the gastrointestinal tract and can be carcinogenic (Cutler and Hayward, 1974; Cutler and Schneider, 1973). The identification of the catalysts in animal tissues which are responsible for the oxidation of unsaturated fats is therefore important, not only because of its pertinence to food preservation, but also for health reasons.…”

mentioning

confidence: 99%

Involvement of cytochrome P-450 in the intracellular formation of lipid peroxides

O’Brien¹,

Rahimtula²

1975

J. Agric. Food Chem.

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The radical intermediates and the nonradical products of peroxidized lipids are both effective in polymerizing RNase. The radicals formed by the fission of LAHPO may initiate a chain reaction resulting in the formation of protein radicals. These protein radicals react together to form polymeric products. This conclusion is in agreement with the observation of Roubal (1966), who suggested that the radical intermediates initiate the production of protein radicals which in turn polymerize as P-(P)re-P•• This mechanism is further strengthened by the effects of AsA and BHT on the polymer formation of RNase by LAHPO. The pronounced effect of AsA on the polymer formation of RNase by LAHPO suggests that AsA has increased the rate of the production of alkoxy or peroxy radicals. These radicals react with the proteins, affecting the formation of the protein radicals, which are also being degraded to SP. The antioxidative behavior of BHT further supports the radical mechanism of LAHPO.The reaction of SP is time dependent and SP did not produce polymers within a short incubation period but showed a relatively high fluorescence in contrast to LAHPO. LAHPO did not produce the fluorescence at 425 nm, which is due to a carbonylamine condensation reaction resulting in the formation of a conjugated chromophoric Schiff s base system (Ohio and Tappel, 1969). From the differences observed in the incorporation, inactivation, and relative damage to the amino acid residues with respect to LAHPO and SP, it was deduced that different amino acid residues are able to be attached by LAHPO or SP. Among the four enzymes under consideration, the structural conformations are different. This results in differences of the surface exposed groups susceptible to attachment by LAHPO or SP, and such exposed groups may be influenced by pH. For instance, at pH 8.0 amino groups of protein would be more unprotonated and better nucleophiles than at pH 5.0. The occurrence of a conformational change of protein structure can also be expected from a change in pH. Also, pH may affect the formation of reactive groups, for instance, the differences of radical formation by the decomposition of LAHPO at pH 5.0 and 8.0.The specific interactions are very complicated, and it can only be said that specific interactions of oxidized products of linoleic acid and proteins are caused by several factors, pH, specific structure of proteins, etc. LITERATURE CITED

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Lipid peroxide catalyzed chemical carcinogenesis

O’Brien

1984

J Americ Oil Chem Soc

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Peroxides, including lipid peroxides, with heme catalysts cause the binding of C14-acetylaminofluorene to DNA if microsomes are present. This binding was 96% inhibited by paraoxon, a deacetylase inhibitor. It is concluded that peroxide-peroxidase systems rapidly oxidize acetylated arylamines to proximate carcinogens following deacetylation by microsomal deacetylases. The DNA binding observed was greater than that observed with the liver microsomal mixed function oxidase catalyzed activation to N-OH-acetylaminofluorene, which binds to DNA following deacetylation by microsomal deacetylase. Lipid peroxidation or prostaglandin synthesis should therefore enhance carcinogenesis induced by arylamides.

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Effect of Lipid Peroxides on Fat Absorption and Folic Acid Status in the Rat

Cited by 7 publications

References 18 publications

Rapid, Sensitive, and Specific Thiobarbituric Acid Method for Measuring Lipid Peroxidation in Animal Tissue, Food, and Feedstuff Samples

Rapid, Sensitive, and Specific Thiobarbituric Acid Method for Measuring Lipid Peroxidation in Animal Tissue, Food, and Feedstuff Samples

Involvement of cytochrome P-450 in the intracellular formation of lipid peroxides

Lipid peroxide catalyzed chemical carcinogenesis

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