Force-velocity characteristics and metabolism of carp muscle fibres following temperature acclimation.

Common carp (Cyprinus carpio L.), 1 kg body weight, were acclimated for 1-2 months to water temperatures of either 7-8 degrees C (cold-acclimated group) or 23-24 degrees C (warm-acclimated group). Single fast fibres and small bundles of slow fibres were isolated from the myotomal muscles and chemically skinned. Force-velocity (P-V) characteristics were determined at 7 degrees C and 23 degrees C. The contractile properties of carp muscle fibres are dependent on acclimation temperature. In the warm-acclimated group maximum isometric tensions (P0, kN m-2) are 47 +/- 6 and 64 +/- 5 for slow muscle fibres and 76 +/- 10 and 209 +/- 21 for fast muscle fibres at 7 degrees C and 23 degrees C, respectively. Maximum contraction velocities (Vmax, muscle lengths-1), are 0.4 +/- 0.05 and 1.5 +/- 0.1 at 7 degrees C (slow fibres) and 0.6 +/- 0.04 and 1.9 +/- 0.4 at 23 degrees C (fast fibres). All values represent mean +/- S.E. P0 and Vmax at 7 degrees C are around 1.5-2.0 times higher for slow and fast muscle fibres isolated from the cold-acclimated group. Fibres from 7 degrees C-acclimated carp fail to relax completely following maximal activations at 23 degrees C. The resulting Ca-insensitive force component (50-70% P0) is associated with the development of abnormal crossbridge linkages and very slow contraction velocities. Activities of enzymes associated with energy metabolism were determined at a common temperature of 15 degrees C. Marker enzymes of the electron transport system (cytochrome oxidase), citric acid cycle (citrate synthase), fatty acid metabolism (carnitine palmitoyl transferase, beta-hydroxyacyl CoA dehydrogenase) and aerobic glucose utilization (hexokinase) have 30-60% higher activities in slow muscle from cold-acclimated than from warm-acclimated fish. Activities of cytochrome oxidase and citrate synthase in fast muscle are also elevated following acclimation to low temperature. It is concluded that thermal compensation of mechanical power output by carp skeletal muscle is matched by a concomitant increase in the potential to supply aerobically-generated ATP at low temperatures.

[1]  G. Goldspink,et al.  Compensation limits of fish muscle myofibrillar ATPase enzyme to environmental temperature , 1979 .

[2]  A. Hill The heat of shortening and the dynamic constants of muscle , 1938 .

[3]  R. Reeves The interaction of body temperature and acid-base balance in ectothermic vertebrates. , 1977, Annual review of physiology.

[4]  I. Johnston,et al.  Power output and force-velocity relationship of red and white muscle fibres from the Pacific blue marlin (Makaira nigricans). , 1984, The Journal of experimental biology.

[5]  B. Sidell,et al.  Changes in mitochondrial distribution and diffusion distances in muscle of goldfish upon acclimation to warm and cold temperatures , 1984 .

[6]  K. D. Hardman,et al.  Isolation of sperm whale myoglobin by low temperature fractionation with ethanol and metallic ions. , 1966, The Journal of biological chemistry.

[7]  L C Rome,et al.  Muscle fiber activity in carp as a function of swimming speed and muscle temperature. , 1984, The American journal of physiology.

[8]  W. Driedzic The fish heart as a model system for the study of myoglobin. , 1983, Comparative biochemistry and physiology. A, Comparative physiology.

[9]  J. Wittenberg,et al.  Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. , 1970, Physiological reviews.

[10]  B. Sidell Responses of Goldfish (Carassius auratus, L.) Muscle to Acclimation Temperature: Alterations in Biochemistry and Proportions of Different Fiber Types , 1980, Physiological Zoology.

[11]  I. Johnston,et al.  Temperature acclimation in crucian carp, Carassius carassius L., morphometric analyses of muscle fibre ultrastructure , 1980 .

[12]  B. Sidell,et al.  Metabolic responses of striped bass (Morone saxatilis) to temperature acclimation. II. Alterations in metabolic carbon sources and distributions of fiber types in locomotory muscle , 1982 .

[13]  I. Johnston,et al.  The pCa‐tension and force‐velocity characteristics of skinned fibres isolated from fish fast and slow muscles , 1982, The Journal of physiology.

[14]  C. Prosser,et al.  Molecular mechanisms of temperature compensation in poikilotherms. , 1974, Physiological reviews.

[15]  J. J. Connell The relative stabilities of the skeletal-muscle myosins of some animals. , 1961, The Biochemical journal.

[16]  C. Prosser,et al.  Molecular aspects of temperature acclimation in fish: contributions of changes in enzyme activities and isozyme patterns to metabolic reorganization in the green sunfish. , 1977, The Journal of experimental zoology.

[17]  M. Bárány,et al.  ATPase Activity of Myosin Correlated with Speed of Muscle Shortening , 1967, The Journal of general physiology.

[18]  I. Johnston Temperature, muscle energetics and locomotion in inshore antarctic fish , 1985 .

[19]  B. Sidell,et al.  Atlantic hagfish cardiac muscle: metabolic basis of tolerance to anoxia. , 1983, The American journal of physiology.

[20]  I. Johnston,et al.  Adaptations in Mg2+‐activated myofibrillar ATPase activity induced by temperature acclimation , 1975, FEBS letters.

[21]  I. Johnston,et al.  Differences in temperature dependence of muscle contractile properties and myofibrillar ATPase activity in a cold-temperature fish. , 1984, The Journal of experimental biology.