Temperature-dependent expression of cytochrome-c oxidase in Antarctic and temperate fish.

Seasonal acclimation versus permanent adaptation to low temperatures leads to a differential response in the expression of cytochrome-c oxidase (CCO) in temperate and Antarctic eelpouts. Although eurythermal eelpout from the North Sea (Zoarces viviparus) displayed a cold-induced rise of CCO activity in white muscle, enzyme activity in the cold stenothermal Antarctic eelpout Pachycara brachycephalum failed to reflect such a compensatory increase. In Antarctic eelpout, CCO activity correlates with transcript levels of mitochondrial encoded subunits of CCO (CCO I and CCO II), whereas cold-acclimated eelpout from the North Sea show lower enzyme activities than expected on the basis of mitochondrial mRNA levels. In these animals, CCO expression at low temperatures may be limited either by nuclear CCO transcripts or by posttranscriptional processes. These may comprise translation of the subunits or assembly of the CCO holoenzyme. mRNA levels of CCO IV, one of the nuclear encoded subunits, increased strongly during cold acclimation, indicating that the expression of CCO is likely not message limited in cold-acclimated Z. viviparus. Our data suggest that seasonal cold acclimation of Z. viviparus results in a modification of the relationship between transcription and translation or posttranslational processes. In permanently cold-adapted P. brachycephalum, on the other hand, CCO expression shows similar characteristics as in the warm-acclimated confamilial species, e.g., low levels of enzyme activity correlated with low levels of mitochondrial message.

High-energy turnover at low temperatures: recovery from exhaustive exercise in Antarctic and temperate eelpouts.

Earlier work on Notothenioids led to the hypothesis that a reduced glycolytic capacity is a general adaptation to low temperatures in Antarctic fish. In our study this hypothesis was reinvestigated by comparing changes in the metabolic status of the white musculature in two related zoarcid species, the stenothermal Antarctic eelpout Pachycara brachycephalum and the eurythermal Zoarces viviparus during exercise and subsequent recovery at 0 degreesC. In both species, strenuous exercise caused a similar increase in white muscle lactate, a drop in intracellular pH (pHi) by about 0.5 pH units, and a 90% depletion of phosphocreatine. This is the first study on Antarctic fish that shows an increase in white muscle lactate concentrations. Thus the hypothesis that a reduced importance of the glycolytic pathway is characteristic for cold-adapted polar fish cannot hold. The recovery process, especially the clearance of white muscle lactate, is significantly faster in the Antarctic than in temperate eelpout. Based on metabolite data, we calculated that during the first hour of recovery aerobic metabolism is increased 6.6-fold compared with resting rates in P. brachycephalum vs. an only 2.9-fold increase in Z. viviparus. This strong stimulation of aerobic metabolism despite low temperatures may be caused by a pronounced increase of free ADP levels, in the context of higher levels of pHi and ATP, which is observed in the Antarctic species. Although basal metabolic rates are identical in both species, the comparison of metabolic rates during situations of high-energy turnover reveals that the stenothermal P. brachycephalum shows a higher degree of metabolic cold compensation than the eurythermal Z. viviparus. Muscular fatigue after escape swimming may be caused by a drop of the free energy change of ATP hydrolysis, which is shown to fall below critical levels for cellular ATPases in exhausted animals of both species.

Temperature-dependent shift of pHi in fish white muscle: contributions of passive and active processes.

This study was designed to determine the mechanisms causing temperature-induced pH shifts in the white muscle of the marine teleost Zoarces viviparus. The white musculature undergoes an intracellular acidification with increasing body temperature at a slope of the pH-temperature relationship equal to -0.016 +/- 0.003 U/degree C. This is in good accordance with the overall relationship between the change in pK and the change in temperature of the intracellular proteins, which was determined to be -0.013 +/- 0.001 U/degree C. Thus the dissociation state of muscle proteins is kept fairly constant in white muscle of Zoarces viviparus. The passive component of the observed pH shift, which is due to the physicochemical response of the intracellular buffers to temperature change, accounts for only 35% of the pH transition. Ventilatory adjustment of intracellular PCO2 does not contribute to the temperature-induced shift of intracellular pH (pHi) in Zoarces viviparus. Therefore, the remaining 65% of pH adjustment must be ascribed to ion exchange mechanisms. The nonbicarbonate buffer value amounted to 34.4 +/- 2.3 meq.pH-1 kg cell water-1 at 12 degrees C and decreased slightly but not significantly with temperature. On the basis of our data we calculated that a removal of 0.52 mmol base equivalents.kg cell water-1.degree C-1 was necessary to shift pHi to its new steady state.