Pichaud 2010 J Exp Biol: Difference between revisions
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|organism=Drosophila | |organism=Drosophila | ||
|tissues=Skeletal muscle | |tissues=Skeletal muscle | ||
|preparations=Isolated | |preparations=Isolated mitochondria | ||
|enzymes=Complex IV; | |enzymes=Complex IV;cytochrome c oxidase, Marker enzyme | ||
|couplingstates=OXPHOS, ETS | |couplingstates=OXPHOS, ETS | ||
|substratestates=CI, | |substratestates=CI, CGpDH | ||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
|additional=Drosophila | |additional=Drosophila | ||
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Revision as of 12:31, 13 February 2015
Pichaud N, Chatelain HE, Ballard JW, Tanguay R, Morrow G, Blier PU (2010)Thermal sensitivity of mitochondrial metabolism in two distinct mitotypes of Drosophila simulans: Evaluation of mitochondrial plasticity. J Exp Biol 213:1665-75. |
Pichaud N, Chatelain HE, Ballard JW, Tanguay R, Morrow G, Blier PU (2010) J Exp Biol
Abstract: The overall aim of this study was to (1) evaluate the adaptive value of mitochondrial DNA by comparing mitochondrial performance in populations possessing different haplotypes and distribution, and to (2) evaluate the sensitivity of different enzymes of the electron transfer system (ETS) during temperature-induced changes. We measured the impact of temperature of mitochondrial respiration and several key enzymes of mitochondrial metabolism in two mitotypes (siII and siIII) of Drosophila simulans. The temperature dependencies of oxygen consumption for mitochondria isolated from flight muscle was assessed with Complex I substrates (pyruvate + malate + proline) and with sn glycerol-3-phosphate (to reduce Complex III via glycerophosphate dehydrogenase) in both coupled and uncoupled states. Activities of citrate synthase, cytochrome c oxidase (COX), catalase and aconitase, and the excess capacity of COX at high convergent pathway flux were also measured as a function of temperature. Overall, our results showed that functional differences between the two mitotypes are few. Results suggest that differences between the two mitotypes could hardly explain the temperature-specific differences measured in mitochondria performances. It suggests that some other factor(s) may be driving the maintenance of mitotypes. We also show that the different enzymes of the ETS have different thermal sensitivities. The catalytic capacities of these enzymes vary with temperature changes, and the corresponding involvement of the different steps on mitochondrial regulation probably varies with temperature. For example, the excess COX capacity is low, even non-existent, at high and intermediate temperatures (18 ยฐC, 24 ยฐC and 28 ยฐC) whereas it is quite high at a lower temperature (12 ยฐC), suggesting release of respiration control by COX at low temperature.
Supplementary material available online โข Keywords: Drosophila simulans, metabolism, mitochondrial DNA, mitochondrial respiration, temperature, thermal sensitivity.
โข O2k-Network Lab: CA_Rimouski_Blier PU, AU Sydney Ballard JW
Labels: MiParea: mtDNA;mt-genetics, Genetic knockout;overexpression
Organism: Drosophila
Tissue;cell: Skeletal muscle
Preparation: Isolated mitochondria
Enzyme: Complex IV;cytochrome c oxidase, Marker enzyme
Coupling state: OXPHOS, ETS"ETS" is not in the list (LEAK, ROUTINE, OXPHOS, ET) of allowed values for the "Coupling states" property.
HRR: Oxygraph-2k
Drosophila