Temperature adaptation by the myotomal muscle of fish

Penney, R.K.; Goldpink, G.

doi:10.1016/0306-4565(81)90018-8

Cited by 23 publications

(9 citation statements)

References 24 publications

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“…Following acclimation to a lower temperature the rate at which myofibrils split ATP is increased in the red and white muscle of goldfish (Penney and Goldspink 1981) and other cyprinids . This adjustment in ATPase activity maintains locomotory ability at low environmental temperatures.…”

Section: Discussionmentioning

confidence: 99%

“…Goldfish and other Cyprinidae show an alteration in the thermal'stability and specific activity of the myofibrillar ATPase (Penney and Goldspink 1981;Heap et al 1985). In these species the enzyme from cold acclimated fish had a decreased Arrhenius activation energy (Ea) compared to the enzyme from warm acclimated fish (Johnston and Walesby 1977).…”

Section: Introductionmentioning

confidence: 97%

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Protein synthesis in tissues of fed and starved carp, acclimated to different temperatures

Watt

Marshall

Heap

et al. 1988

Fish Physiol Biochem

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The temperature dependence of the rates of protein synthesis in the red and white skeletal muscle of the carp (Cyprinus carpio) was measured using a method which involved a single injection of tritiated phenylalanine. Plasma and muscle-free phenylalanine quickly reached a plateau level at all temperatures. During the plateau phase the incorporation of label into protein was liner. Muscle from fish previously acclimated to either a low temperature (8°C) or a high temperature (28°C), showed marked differences in the rates of protein synthesis. The results show that cold acclimation is associated with significantly higher rates of protein synthesis (p<0.001) in both red and white muscle. Arrhenius activation energies, derived from the rates of protein synthesis at the different experimental temperatures, were similar for both red and white muscle in fish acclimated to warm or cold temperatures. Measurements for both acclimated groups over the temperature range 8-34°C showed that the activation energy for the process of protein synthesis was 86.7 kJ/mol and 78.7 kJ/mol for the red and white muscle respectively.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

Protein synthesis in tissues of fed and starved carp, acclimated to different temperatures

Watt

Marshall

Heap

et al. 1988

Fish Physiol Biochem

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“…Salmon (Salmo salar) was the most resistant of the salmonid fish to high temperature: when acclimated to 20°C, tolerated temperatures up to 28°C (Fry, 1947after Brett, 1952. Salmonid fish choose a very low range of preferred temperatures independent of the acclimation temperature, whereas cyprinid fish showed a strictly defined temperature preference after 2 months of acclimation (Penney and Goldspink 1981). The reason for the decreased swimming speed in cold water is clear if one considers the acclimation temperature does not change the contraction time of muscle, that contraction rate decreases exponentially with temperature increases (Wardle, 1980).…”

Section: Effect Of Temperaturementioning

confidence: 98%

“…However, in cyprinids which are more evolutionary advanced than stenothermal salmonids, the key enzyme in muscle contraction (miofibrillar ATP-ase) has a much higher specific activity in cold water than one would expect from Qto. This is due to regulatory proteins (Penney and Goldspink 1981). Even so, in cold water, carp recruits a greater number of fast, white fibres than it would recruit in warm water in order to achieve the same swimming speed (Rome et al 1984).…”

Section: Effect Of Temperaturementioning

confidence: 98%

Active metabolism in larval and juvenile fish: ontogenetic changes, effect of water temperature and fasting

Dąbrowski¹

1986

Fish Physiol Biochem

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Oxygen consumption, ammonia excretion and fish swimming speed were measured in fish induced to swim by optomotor reaction in a circular metabolism chamber. The relationship between the swimming speed and fish metabolism described by exponential equations allowed the extrapolation to the standard metabolism, i.e. at zero swimming speed. The partitioning of the catabolised protein in the energy supply was estimated based on AQ (volume of ammonia/ volume of oxygen) values. Weight specific standard metabolism, as expressed by the ammonia excretion rate, decreased by one order of magnitude in coregonids as the fish grew from 20 to 780 mg body weight. The slope of the relationship between oxygen uptake and swimming speed decreased in coregonid ontogenesis. In salmon, after 12 days of fasting 28% of energy used was derived from protein, whilst coregonid juveniles utilized mostly lipid. Active swimming in fasted juveniles of coregonid, as well as in salmon, led to the accelerated utilization of protein as a source of energy, based on AQ coefficients. In juveniles acclimated to a range of water temperatures from 14 to 26°C, the changes in standard or active metabolic rate (expressed as oxygen uptake or ammonia excretion) were described by Q10 coefficients. They were generally higher for the ammonia excretion rate than for the oxygen uptake rate and for active metabolism than for standard metabolism. Utilization of protein as energy for swimming differed significantly between the species, being in general one order of magnitude higher in coregonids than in salmon. The use of protein for swimming activity tended to decrease during coregonid ontogenesis.

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“…Intraspecific variation also occurs. Goldfish acclimated at temperatures between 5 and 35°C showed adaptation of the myofibrillar ATPase within the range 10-30°C (Penney & Goldspink, 1981~).…”

Section: 'I Introductionmentioning

confidence: 99%

Consequences of thermal change on the myofibrillar ATPase of five freshwater teleosts

Heap¹,

Watt

Goldspink³

1985

Journal of Fish Biology

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Myofibrillar ATPase activity was measured in the epaxial musculature of five freshwater species of fish acclimated to extremes of temperature within their tolerance ranges. Changes in the enzyme activity were apparent in carp, tench and roach, cold acclimated fish (10°C) having higher enzyme activity levels than hot acclimated fish (28°C). Such changes were not apparent in eels or brook trout. Alteration of the enzyme activity took less than 4 weeks, and was totally reversible. This suggests that seasonal adaptation to environmental temperatures is possible, thus maintaining locomotory efficiency.

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Temperature adaptation by the myotomal muscle of fish

Cited by 23 publications

References 24 publications

Protein synthesis in tissues of fed and starved carp, acclimated to different temperatures

Protein synthesis in tissues of fed and starved carp, acclimated to different temperatures

Active metabolism in larval and juvenile fish: ontogenetic changes, effect of water temperature and fasting

Consequences of thermal change on the myofibrillar ATPase of five freshwater teleosts

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