The impact of the thermal sensitivity of cytochrome c oxidase on the respiration rate of Arctic charr red muscle mitochondria

Blier, Pierre; Lemieux, Hélène

doi:10.1007/s003600000169

Cited by 57 publications

(53 citation statements)

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“…The activity of this enzyme varied little across temperatures, differing by at most 30% across a 14°C range of assay temperatures and generally peaking between 27 and 32°C (Figs 3, 9). Similar patterns have been observed in some fish, amphibian and reptile species (Godiksen and Jessen, 2001;Glanville and Seebacher, 2006;Niehaus et al, 2011), but not in others (Caldwell, 1969;Blier and Lemieux, 2001). Furthermore, there were clear differences in thermal optima between the 22°C T E group (T opt of 27°C) and the 32°C T E group (T opt of 32°C).…”

Section: Developmental Plasticity Of Enzyme Activities and Thermal Opsupporting

confidence: 82%

Temperature during embryonic development has persistent effects on metabolic enzymes in the muscle of zebrafish

Schnurr

Scott

2013

Journal of Experimental Biology

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Global warming is intensifying interest in the physiological consequences of temperature change in ectotherms, but we still have a relatively poor understanding of the effects of temperature on early life stages. This study determined how embryonic temperature (T E ) affects development and the activity of metabolic enzymes in the swimming muscle of zebrafish. Embryos developed successfully to hatching (survival ≥88%) from 22 to 32°C, but suffered sharp increases in mortality outside of this range. Embryos that were incubated until hatching at a control T E (27°C) or near the extremes for successful development (22 or 32°C) were next raised to adulthood under control conditions at 27°C. Growth trajectories after hatching were altered in the 22°C and 32°C T E groups compared with 27°C T E controls, but growth slowed after 3 months of age in all groups. Maximal enzyme activities of cytochrome c oxidase (COX), citrate synthase (CS), hydroxyacyl-coA dehydrogenase (HOAD), pyruvate kinase (PK) and lactate dehydrogenase (LDH) were measured across a range of assay temperatures (22, 27, 32 and 36°C) in adults from each T E group that were acclimated to 27 or 32°C. Substrate affinities (K m ) were also determined for COX and LDH. In adult fish acclimated to 27°C, COX and PK activities were higher in 22°C and 32°C T E groups than in 27°C T E controls, and the temperature optimum for COX activity was higher in the 32°C T E group than in the 22°C T E group. Warm acclimation reduced COX, CS and/or PK activities in the 22 and 32°C T E groups, possibly to compensate for thermal effects on molecular activity. This response did not occur in the 27°C T E controls, which instead increased LDH and HOAD activities. Warm acclimation also increased thermal sensitivity (Q 10 ) of HOAD to cool temperatures across all T E groups. We conclude that the temperature experienced during early development can have a persistent impact on energy metabolism pathways and acclimation capacity in later life.

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Section: Developmental Plasticity Of Enzyme Activities and Thermal Opsupporting

confidence: 82%

Temperature during embryonic development has persistent effects on metabolic enzymes in the muscle of zebrafish

Schnurr

Scott

2013

Journal of Experimental Biology

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“…The decrease of coupling ratios with temperature was elicited by different thermal sensitivities of oxidative phosphorylation capacity (state III) and proton leakage capacity (state IV ol ) showing lower Arrhenius activation energies for state III than for state IV ol . Progressive uncoupling with rising temperature was also reported by Hardewig et al (1999) and by Po¨rtner et al(1999b) for Antarctic species, whereas studies carried out with temperate zone eurytherms showed coupling ratios to be stable and independent of temperature (Blier et al 2001, Fischer 2002 or fairly insensitive to temperature (van den Thillart and Modderkolk 1978, Moyes et al 1988, Blier and.…”

Section: Respiratory Properties Of Liver Mitochondriamentioning

confidence: 79%

Aerobic mitochondrial capacities in Antarctic and temperate eelpout (Zoarcidae) subjected to warm versus cold acclimation

2005

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Capacities and effects of cold or warm acclimation were investigated in two zoarcid species from the North Sea (Zoarces viviparus) and the Antarctic (Pachycara brachycephalum) by investigating temperature dependent mitochondrial respiration and activities of citrate synthase (CS) and NADP + -dependent isocitrate dehydrogenase (IDH) in the liver. Antarctic eelpout were acclimated to 5°C and 0°C (controls) for at least 10 months, whereas boreal eelpout, Z. viviparus (North Sea) were acclimated to 5°C and to 10°C (controls). Liver sizes were found to be increased in both species in the cold, with a concomitant rise in liver mitochondrial protein content. As a result, total liver state III rates were elevated in both cold-versus and warm-exposed P. brachycephalum and Z. viviparus, with the highest rates in boreal eelpout acclimated to 5°C. CS and IDH activities in the total liver were similar in Z. viviparus acclimated to 5°C and 10°C, but decreased in those warm acclimated versus control P. brachycephalum. Enzyme capacities in the total liver were higher in eelpout from Antarctica than those from the North Sea. In conclusion, cold compensation of aerobic capacities in the liver seems to be linked to an increase in organ size with unchanged specific mitochondrial protein content. Despite its life in permanently cold climate, P. brachycephalum was able to reduce liver aerobic capacities in warm climate and thus, displayed a capacity for temperature acclimation.

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“…This complex is thought to act as an electron sink and to limit the ETS capacity (Arnold, 2012), and it has been suggested that thermally induced changes in COX affect respiratory regulation mainly through an impact on the redox state of the ETS (Blier and Lemieux, 2001). However, this complex is usually found to have an excess capacity that is required for adequate functioning of mitochondria at the different temperatures encountered by the species, thus allowing the ETS to be mainly in an oxidized state and to ensure a sharp thermodynamic gradient in the ETS under most thermal conditions (Blier and Lemieux, 2001;Blier et al, 2013;Hilton et al, 2010). Surprisingly, we did not find such an excess as the values for COX were only slightly higher than those for CI+CII-OXPHOS.…”

Section: Discussionmentioning

confidence: 99%

Dynamic changes in cardiac mitochondrial metabolism during warm acclimation in rainbow trout

Pichaud

Ekström

Hellgren

et al. 2017

Journal of Experimental Biology

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Although the mitochondrial metabolism responses to warm acclimation have been widely studied in fish, the time course of this process is less understood. Here, we characterized the changes of rainbow trout (Oncorhynchus mykiss) cardiac mitochondrial metabolism during acute warming from 10 to 16°C, and during the subsequent warm acclimation for 39 days. We repeatedly measured mitochondrial oxygen consumption in cardiac permeabilized fibers and the functional integrity of mitochondria (i.e. mitochondrial coupling and cytochrome c effect) at two assay temperatures (10 and 16°C), as well as the activities of citrate synthase (CS) and lactate dehydrogenase (LDH) at room temperature. LDH and CS activities significantly increased between day 0 (10°C acclimated fish) and day 1 (acute warming to 16°C) while mitochondrial oxygen consumption measured at respective in vivo temperatures did not change. Enzymatic activities and mitochondrial oxygen consumption rates significantly decreased by day 2, and remained stable during warm acclimation (days 2-39). The decrease in rates of oxygen between day 0 and day 1 coincided with an increased cytochrome c effect and a decreased mitochondrial coupling, suggesting a structural/ functional impairment of mitochondria during acute warming. We suggest that after 2 days of warm acclimation, a new homeostasis is reached, which may involve the removal of dysfunctional mitochondria. Interestingly, from day 2 onwards, there was a lack of differences in mitochondrial oxygen consumption rates between the assay temperatures, suggesting that warm acclimation reduces the acute thermal sensitivity of mitochondria. This study provides significant knowledge on the thermal sensitivity of cardiac mitochondria that is essential to delineate the contribution of cellular processes to warm acclimation.

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The impact of the thermal sensitivity of cytochrome c oxidase on the respiration rate of Arctic charr red muscle mitochondria

Cited by 57 publications

References 0 publications

Temperature during embryonic development has persistent effects on metabolic enzymes in the muscle of zebrafish

Temperature during embryonic development has persistent effects on metabolic enzymes in the muscle of zebrafish

Aerobic mitochondrial capacities in Antarctic and temperate eelpout (Zoarcidae) subjected to warm versus cold acclimation

Dynamic changes in cardiac mitochondrial metabolism during warm acclimation in rainbow trout

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