التفاصيل البيبلوغرافية
| العنوان: |
Long-Chain and Medium-Chain Fatty Acids in Energy Metabolism of Murine Kidney Mitochondria |
| المؤلفون: |
Panov, Alexander V. V., Mayorov, Vladimir I. I., Dikalova, Anna E. E., Dikalov, Sergey I. I. |
| المصدر: |
https://www.mdpi.com/1422-0067/24/1/379Test. |
| بيانات النشر: |
International Journal Of Molecular Sciences |
| سنة النشر: |
2022 |
| المجموعة: |
Vanderbilt University, Nashville: DiscoverArchive |
| مصطلحات موضوعية: |
kidney, kidney mitochondria, respiration, oxidative phosphorylation, beta-oxidation, fatty acids, palmitoylcarnitine, ctanoylcarnitine, uccinate, uccinate dehydrogenase, respirasome |
| الوصف: |
Scientists have long established that fatty acids are the primary substrates for kidney mitochondria. However, to date we still do not know how long-chain and middle-chain fatty acids are oxidized at the mitochondrial level. Our previous research has shown that mitochondria from the heart, brain, and kidney oxidize palmitoylcarnitine at a high rate only in the presence of succinate, glutamate, or pyruvate. In this paper, we report properties of the isolated kidney mitochondria and how malate and succinate affect the oxidation of C16 and C8 acylcarnitines. The isolated kidney mitochondria contain very few endogenous substrates and require malate to oxidize pyruvate, glutamate, and C16 or C8 acylcarnitines. We discovered that with 10 mu M of C16 or C8 acylcarnitines, low concentrations of malate (0.2 mM) or succinate (0.5 mM) enhance the States 4 and 3 respiratory rates several times. The highest respiration rates were observed with C16 or C8 acylcarnitines and 5 mM succinate mixtures. Results show that kidney mitochondria, unlike the heart and brain mitochondria, lack the intrinsic inhibition of succinate dehydrogenase. Additionally, results show that the oxidation of fatty acid by the small respirasome's supercomplex generates a high level of CoQH2, and this makes SDH in the presence of succinate reverse the flow of electrons from CoQH2 to reduce fumarate to succinate. Finally, we report evidence that succinate dehydrogenase is a key mitochondrial enzyme that allows fast oxidation of fatty acids and turns the TCA cycle function from the catabolic to the anabolic and anaplerotic metabolic pathways. ; This work was supported by funding from the National Institutes of Health (R01HL144943 and RO1HL157583) and a Navicent Health Foundation grant (Mercer University School of Medicine). |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
English |
| الإتاحة: |
http://hdl.handle.net/1803/17990Test |
| حقوق: |
© 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0Test/). |
| رقم الانضمام: |
edsbas.F88A80D9 |
| قاعدة البيانات: |
BASE |
