Difference between revisions of "Hancock 2016 Amino Acids"
(Created page with "{{Publication |title=Hancock CN, Liu W, Alvord WG, Phang JM (2016) Co-regulation of mitochondrial respiration by proline dehydrogenase/oxidase and succinate. Amino Acids 48:85...") Β |
Β |
||
Line 13: | Line 13: | ||
|organism=Mouse | |organism=Mouse | ||
|tissues=Liver | |tissues=Liver | ||
|preparations=Intact cells, Isolated mitochondria | |preparations=Intact cells, Isolated mitochondria, Oxidase;biochemical oxidation | ||
|couplingstates=LEAK, ROUTINE, ET | |couplingstates=LEAK, ROUTINE, ET | ||
|pathways=S, Other combinations, ROX | |pathways=S, Other combinations, ROX | ||
}} | }} | ||
::::* [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4969956/ Erratum] to: Co-regulation of mitochondrial respiration by proline dehydrogenase/oxidase and succinate | ::::* [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4969956/ Erratum] to: Co-regulation of mitochondrial respiration by proline dehydrogenase/oxidase and succinate |
Latest revision as of 13:29, 19 February 2019
Hancock CN, Liu W, Alvord WG, Phang JM (2016) Co-regulation of mitochondrial respiration by proline dehydrogenase/oxidase and succinate. Amino Acids 48:859-72. |
Hancock CN, Liu W, Alvord WG, Phang JM (2016) Amino Acids
Abstract: Proline dehydrogenase/oxidase (PRODH/POX) is a mitochondrial protein critical to multiple stress pathways. Because of the roles of PRODH/POX in signaling, and its shared localization to the mitochondrial inner membrane with the electron transport chain (ETC), we investigated whether there was a direct relationship between PRODH/POX and regulation of the ETC. We found that PRODH/POX binds directly to CoQ1 and that CoQ1-dependent PRODH/POX activity required functional Complex III and Complex IV. PRODH/POX supported respiration in living cells during nutrient stress; however, expression of PRODH/POX resulted in an overall decrease in respiratory fitness. Effects on respiratory fitness were inhibited by DHP and NAC, indicating that these effects were mediated by PRODH/POX-dependent reactive oxygen species (ROS) generation. PRODH/POX expression resulted in a dose-dependent down-regulation of Complexes I-IV of the ETC, and this effect was also mitigated by the addition of DHP and NAC. We found that succinate was an uncompetitive inhibitor of PRODH/POX activity, inhibited ROS generation by PRODH/POX, and alleviated PRODH/POX effects on respiratory fitness. The findings demonstrate novel cross-talk between proline and succinate respiration in vivo and provide mechanistic insights into observations from previous animal studies. Our results suggest a potential regulatory loop between PRODH/POX and succinate in regulation of mitochondrial respiration. β’ Keywords: Proline β’ Bioblast editor: Gnaiger E
Labels: MiParea: Respiration
Organism: Mouse
Tissue;cell: Liver
Preparation: Intact cells, Isolated mitochondria, Oxidase;biochemical oxidation
Coupling state: LEAK, ROUTINE, ET
Pathway: S, Other combinations, ROX
- Erratum to: Co-regulation of mitochondrial respiration by proline dehydrogenase/oxidase and succinate