» Articles » PMID: 2213594

The Influence of Temperature on Mechanics of Red Muscle in Carp

Overview
Journal J Physiol
Specialty Physiology
Date 1990 Aug 1
PMID 2213594
Citations 8
Authors
Affiliations
Soon will be listed here.
Abstract

1. We measured the influence of temperature on maximum velocity of shortening (Vmax) of red muscle in carp in order to better understand the influence of temperature on locomotory performance. 2. A stable red muscle bundle preparation containing about 100 muscle fibres was developed. The bundles could not be activated directly by electrical stimulation, but rather contained sufficient nervous tissue so that acetylcholine released from the nerve terminals caused activation of the muscle. A high level of activation was achieved (116 kN/m2) by adding a combination of a 1 mM-caffeine and 10(-5) g/ml eserine to physiological Ringer solution and electrically stimulating the preparation. 3. Force-velocity characteristics were determined at 10 and 20 degrees C by the force clamp method. The data were well fitted by a hyperbola not constrained to pass through P0 = 1 (where P0 is the isometric force). The mean Vmax at 10 degrees C was 3.55 +/- 0.26 muscle lengths/s (ML/s) (n = 6) and at 20 degrees C, 5.71 +/- 0.29 ML/s (n = 6). The mean Q10 for Vmax was 1.63 +/- 0.07 (n = 6). The a/P0* (Hill constant) and Po* (where P0* is the extrapolated load at zero velocity) were 0.49 +/- 0.06 (n = 6) and 1.19 +/- 0.04 (n = 6) respectively at 10 degrees C and 0.29 +/- 0.06 (n = 6) and 1.51 +/- 0.20 (n = 6) respectively at 20 degrees C. 4. The mean Q10 for maximum isometric tension was 1.13 +/- 0.02 (n = 6). The maximal power generation was 59.7 +/- 2.3 W/kg (n = 6) at 10 degrees C and 94.3 +/- 3.2 W/kg (n = 6) at 20 degrees C representing a Q10 of 1.58. The Q10 is less than the product of Q10s for P0 and Vmax because of the greater curvature of the force-velocity curve at 20 degrees C. 5. The 1.63-fold higher Vmax at 20 degrees C than at 10 degrees C enables fish to swim with a 1.6-fold faster muscle shortening velocity, V, at the higher temperature. Thus at both 10 and 20 degrees C, red muscle is used only over the same narrow range of V/Vmax (0.18-0.36), where isolated muscle experiments suggest that power and efficiency are maximal. Thus V/Vmax appears to be an effective design constraint which limits the range of velocities over which muscle is used in vivo at different temperatures.

Citing Articles

Molecular Events of the Crossbridge Cycle Reflected in the Force-Velocity Relationship of Activated Muscle.

Seow K, Seow C Front Physiol. 2022; 13:846284.

PMID: 35360243 PMC: 8960716. DOI: 10.3389/fphys.2022.846284.


Physiological mechanisms linking cold acclimation and the poleward distribution limit of a range-extending marine fish.

Wolfe B, Fitzgibbon Q, Semmens J, Tracey S, Pecl G Conserv Physiol. 2020; 8(1):coaa045.

PMID: 32494362 PMC: 7248536. DOI: 10.1093/conphys/coaa045.


Thermal Resilience of Feeding Kinematics May Contribute to the Spread of Invasive Fishes in Light of Climate Change.

Turingan R, Sloan T Biology (Basel). 2016; 5(4).

PMID: 27897997 PMC: 5192426. DOI: 10.3390/biology5040046.


Force per cross-sectional area from molecules to muscles: a general property of biological motors.

Rospars J, Meyer-Vernet N R Soc Open Sci. 2016; 3(7):160313.

PMID: 27493785 PMC: 4968477. DOI: 10.1098/rsos.160313.


A review of the thermal sensitivity of the mechanics of vertebrate skeletal muscle.

James R J Comp Physiol B. 2013; 183(6):723-33.

PMID: 23483325 DOI: 10.1007/s00360-013-0748-1.


References
1.
Woledge R . The energetics of tortoise muscle. J Physiol. 1968; 197(3):685-707. PMC: 1351756. DOI: 10.1113/jphysiol.1968.sp008582. View

2.
Guth L, SAMAHA F . Procedure for the histochemical demonstration of actomyosin ATPase. Exp Neurol. 1970; 28(2):365-7. View

3.
Rome L, Loughna P, Goldspink G . Temperature acclimation: improved sustained swimming performance in carp at low temperatures. Science. 1985; 228(4696):194-6. DOI: 10.1126/science.228.4696.194. View

4.
EDMAN K, MULIERI L . Non-hyperbolic force-velocity relationship in single muscle fibres. Acta Physiol Scand. 1976; 98(2):143-56. DOI: 10.1111/j.1748-1716.1976.tb00234.x. View

5.
Ranatunga K . The force-velocity relation of rat fast- and slow-twitch muscles examined at different temperatures. J Physiol. 1984; 351:517-29. PMC: 1193132. DOI: 10.1113/jphysiol.1984.sp015260. View