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Evolutionary temperature adaptation of fish sarcoplasmic reticulum

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Summary

Sarcoplasmic reticulum has been isolated from the white muscle of 15 species of teleost fish adapted to diverse thermal environments. Evidence has been obtained that the Ca2+-dependent ATPase of fish sarcoplasmic reticulum has undergone evolutionary modification for function at different temperatures. Compared with tropical fish, cold adapted species have higher rates of Ca2+ transport and Ca2+-ATPase activities at low temperatures. Most species have linear Arrhenius plots over the temperature range 0–30°C. Activation enthalpies (ΔH ) of the ATPase ranged from 53–190 kJ mol−1 and were positively correlated with environment temperature. Activation entropy (ΔS ) varied from negative values in cold adapted species to positive values in tropical fish.

In contrast to the Ca2+-ATPase, the “basal” ATPase of fish sarcoplasmic reticulum showed no relationship between either ATPase activity or thermodynamic activation parameters and environmental temperature.

Only the Ca2+-dependent ATPase is coupled to Ca2+ transport. The percentage of “total” ATPase activity which is Ca2+ activated is higher at low temperatures in cold than in warm adapted species. For example, ratios of Ca2+-dependent/total ATPase at 2°C varied from 80–98% in Arctic, Antarctic and North Sea species to only 2–50% in various tropical fish. Above 20°C, similar ratios in the range 80–98% were obtained for all species. The nature of the “basal” ATPase and mechanisms of temperature adaptation of fish sarcoplasmic reticulum are discussed.

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Abbreviations

ET :

environmental temperature

EGTA :

ethylene glycol-bis (β-aminolethyl ether)-N, N′-tetraacetic acid

HEPES :

N-2-hydroxylpiperazine-N′-2-ethanesulfonic acid

SR :

sarcoplasmic reticulum

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McArdle, H.J., Johnston, I.A. Evolutionary temperature adaptation of fish sarcoplasmic reticulum. J Comp Physiol B 135, 157–164 (1980). https://doi.org/10.1007/BF00691205

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