Inhibition of Palmitate Oxidation in Mitochondria by Lipid Hydroperoxides1

التفاصيل البيبلوغرافية
العنوان: Inhibition of Palmitate Oxidation in Mitochondria by Lipid Hydroperoxides1
المؤلفون: Takahide Watanabe, Toshiaki Imagawa, Takao Nakamura
المصدر: The Journal of Biochemistry. 95:771-778
بيانات النشر: Oxford University Press (OUP), 1984.
سنة النشر: 1984
مصطلحات موضوعية: endocrine system, Hexokinase, Cellular respiration, fungi, Substrate (chemistry), Acyl CoA dehydrogenase, General Medicine, Metabolism, Biology, equipment and supplies, Biochemistry, body regions, Palmitoyl-CoA, chemistry.chemical_compound, chemistry, medicine, biology.protein, Carnitine, Molecular Biology, Palmitoylcarnitine, medicine.drug
الوصف: Linoleate monohydroperoxide (L-HPO), methyl linoleate monohydroperoxide (ML-HPO), and methyl hydroperoxy-epoxy-octadecenoate (ML-X) inhibited state 3 respiration of mitochondria when palmitate, palmitoyl CoA, or L-palmitoylcarnitine was used as a substrate. L-HPO was the most effective, and 50% inhibition of palmitate-supported respiration was observed with 2, 3.3, and 6.5 nmol/mg protein of L-HPO, ML-X, and ML-HPO, respectively. Almost the same values were obtained when palmitoyl CoA or L-palmitoylcarnitine was used in place of palmitate. L-HPO inhibited the reaction of beta-oxidation in mitochondria in a similar concentration range (4 nmol/mg protein for 50% inhibition) when L-palmitoylcarnitine was used as a substrate. L-HPO also inhibited the formation of 3-hydroxypalmitoylcarnitine from the same substrate. Carnitine palmitoyltransferase activity of mitochondria was inhibited by L-HPO, 50% inhibition occurring at 12 nmol/mg protein. These inhibitory effects of L-HPO were weaker when ATP was removed by hexokinase and glucose. ATP-dependent formation of carnitine ester of L-HPO was also suggested. It was deduced that L-HPO (and ML-X and ML-HPO after hydrolysis) was converted to carnitine ester and inhibited the palmitate metabolism at the site(s) of intramitochondrial carnitine palmitoyltransferase (and possibly acyl CoA dehydrogenase).
تدمد: 1756-2651
0021-924X
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_________::b7150255d89e3e2c2bc0adc3fb688580Test
https://doi.org/10.1093/oxfordjournals.jbchem.a134668Test
رقم الانضمام: edsair.doi...........b7150255d89e3e2c2bc0adc3fb688580
قاعدة البيانات: OpenAIRE