Molecular mechanisms underlying the plasticity of muscle contractile properties with temperature acclimation in the marine fish Myoxocephalus scorpius

Derek Ball*, Ian A. Johnston

*Corresponding author for this work

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Single fibres were isolated from the fast myotomal muscle of the short- horned sculpin (Myoxocephalus scorpius L.). Fish were acclimated to either 5°C (10 h:14 h light:dark) or 15 °C (12h:12h light:dark) for 1- 2 months. Isometric tension (F(max)) and unloaded contraction velocity (V(slack)) were determined in maximally activated skinned fibres over the range 0 to 20°C. Fibres isolated from 5 °C-acclimated and 15°C-acclimated fish failed to relax completely following activations at 15°C and 20°C respectively. In 5 °C-acclimated fish, F(max) increased from 75kN m-2 at 0°C to 123 kN m- 2 at 10°C and was not significantly higher at 15 or 20°C. The relationship between F(max) and temperature was not significantly different for cold- and warm-acclimated fish. V(slack) was around 2.8 fibre lengths s-1 in both acclimation groups at 0°C, but it increased at a significantly faster rate with temperature in 15°C- than in 5°C-acclimated fish. At 20°C, V(max) was significantly higher in 15°C-acclimated (8.7 fibre lengths s- 1) than in 5°C-acclimated fish (5.3 fibrelengths s-1). In order to investigate the molecular mechanism(s) underlying changes in V(max), myosin was purified by ion-exchange chromatography. No difference in myosin heavy chain composition could be detected on the basis of peptide mapping with four different proteolytic enzymes. Two-dimensional polyacrylamide gel electrophoresis revealed no myofibrillar protein isoforms unique to either acclimation temperature. However, the ratio of myosin alkali light chain contents (LC3(f):LC1(f)), as determined by capillary electrophoresis, was significantly lower in muscle from 15°C-acclimated (0.73) than from 5°C- acclimated fish (1.66). The results suggest that changes in V(max) are achieved via altered expression of myosin light chains independently of myosin heavy chain composition. In support of this hypothesis, the myofibrillar ATPase activity of fast muscle was not altered by temperature acclimation.

Original languageEnglish
Pages (from-to)1363-1373
Number of pages11
JournalJournal of Experimental Biology
Volume199
Issue number6
Publication statusPublished - Jun 1996

Fingerprint

Acclimatization
acclimation
marine fish
plasticity
Fishes
muscle
Muscles
muscles
Temperature
fish
temperature
myosin light chains
Myosin Light Chains
Myosin Heavy Chains
myosin heavy chains
electrokinesis
Myosin Type V
peptide mapping
Light
protein isoforms

Keywords

  • myosin light chains
  • Myoxocephalus scorpius
  • skinned muscle fibres
  • teleost
  • temperature acclimation

ASJC Scopus subject areas

  • Medicine(all)
  • Physiology
  • Ecology, Evolution, Behavior and Systematics
  • Aquatic Science
  • Molecular Biology
  • Animal Science and Zoology
  • Insect Science

Cite this

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title = "Molecular mechanisms underlying the plasticity of muscle contractile properties with temperature acclimation in the marine fish Myoxocephalus scorpius",
abstract = "Single fibres were isolated from the fast myotomal muscle of the short- horned sculpin (Myoxocephalus scorpius L.). Fish were acclimated to either 5°C (10 h:14 h light:dark) or 15 °C (12h:12h light:dark) for 1- 2 months. Isometric tension (F(max)) and unloaded contraction velocity (V(slack)) were determined in maximally activated skinned fibres over the range 0 to 20°C. Fibres isolated from 5 °C-acclimated and 15°C-acclimated fish failed to relax completely following activations at 15°C and 20°C respectively. In 5 °C-acclimated fish, F(max) increased from 75kN m-2 at 0°C to 123 kN m- 2 at 10°C and was not significantly higher at 15 or 20°C. The relationship between F(max) and temperature was not significantly different for cold- and warm-acclimated fish. V(slack) was around 2.8 fibre lengths s-1 in both acclimation groups at 0°C, but it increased at a significantly faster rate with temperature in 15°C- than in 5°C-acclimated fish. At 20°C, V(max) was significantly higher in 15°C-acclimated (8.7 fibre lengths s- 1) than in 5°C-acclimated fish (5.3 fibrelengths s-1). In order to investigate the molecular mechanism(s) underlying changes in V(max), myosin was purified by ion-exchange chromatography. No difference in myosin heavy chain composition could be detected on the basis of peptide mapping with four different proteolytic enzymes. Two-dimensional polyacrylamide gel electrophoresis revealed no myofibrillar protein isoforms unique to either acclimation temperature. However, the ratio of myosin alkali light chain contents (LC3(f):LC1(f)), as determined by capillary electrophoresis, was significantly lower in muscle from 15°C-acclimated (0.73) than from 5°C- acclimated fish (1.66). The results suggest that changes in V(max) are achieved via altered expression of myosin light chains independently of myosin heavy chain composition. In support of this hypothesis, the myofibrillar ATPase activity of fast muscle was not altered by temperature acclimation.",
keywords = "myosin light chains, Myoxocephalus scorpius, skinned muscle fibres, teleost, temperature acclimation",
author = "Derek Ball and Johnston, {Ian A.}",
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T1 - Molecular mechanisms underlying the plasticity of muscle contractile properties with temperature acclimation in the marine fish Myoxocephalus scorpius

AU - Ball, Derek

AU - Johnston, Ian A.

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N2 - Single fibres were isolated from the fast myotomal muscle of the short- horned sculpin (Myoxocephalus scorpius L.). Fish were acclimated to either 5°C (10 h:14 h light:dark) or 15 °C (12h:12h light:dark) for 1- 2 months. Isometric tension (F(max)) and unloaded contraction velocity (V(slack)) were determined in maximally activated skinned fibres over the range 0 to 20°C. Fibres isolated from 5 °C-acclimated and 15°C-acclimated fish failed to relax completely following activations at 15°C and 20°C respectively. In 5 °C-acclimated fish, F(max) increased from 75kN m-2 at 0°C to 123 kN m- 2 at 10°C and was not significantly higher at 15 or 20°C. The relationship between F(max) and temperature was not significantly different for cold- and warm-acclimated fish. V(slack) was around 2.8 fibre lengths s-1 in both acclimation groups at 0°C, but it increased at a significantly faster rate with temperature in 15°C- than in 5°C-acclimated fish. At 20°C, V(max) was significantly higher in 15°C-acclimated (8.7 fibre lengths s- 1) than in 5°C-acclimated fish (5.3 fibrelengths s-1). In order to investigate the molecular mechanism(s) underlying changes in V(max), myosin was purified by ion-exchange chromatography. No difference in myosin heavy chain composition could be detected on the basis of peptide mapping with four different proteolytic enzymes. Two-dimensional polyacrylamide gel electrophoresis revealed no myofibrillar protein isoforms unique to either acclimation temperature. However, the ratio of myosin alkali light chain contents (LC3(f):LC1(f)), as determined by capillary electrophoresis, was significantly lower in muscle from 15°C-acclimated (0.73) than from 5°C- acclimated fish (1.66). The results suggest that changes in V(max) are achieved via altered expression of myosin light chains independently of myosin heavy chain composition. In support of this hypothesis, the myofibrillar ATPase activity of fast muscle was not altered by temperature acclimation.

AB - Single fibres were isolated from the fast myotomal muscle of the short- horned sculpin (Myoxocephalus scorpius L.). Fish were acclimated to either 5°C (10 h:14 h light:dark) or 15 °C (12h:12h light:dark) for 1- 2 months. Isometric tension (F(max)) and unloaded contraction velocity (V(slack)) were determined in maximally activated skinned fibres over the range 0 to 20°C. Fibres isolated from 5 °C-acclimated and 15°C-acclimated fish failed to relax completely following activations at 15°C and 20°C respectively. In 5 °C-acclimated fish, F(max) increased from 75kN m-2 at 0°C to 123 kN m- 2 at 10°C and was not significantly higher at 15 or 20°C. The relationship between F(max) and temperature was not significantly different for cold- and warm-acclimated fish. V(slack) was around 2.8 fibre lengths s-1 in both acclimation groups at 0°C, but it increased at a significantly faster rate with temperature in 15°C- than in 5°C-acclimated fish. At 20°C, V(max) was significantly higher in 15°C-acclimated (8.7 fibre lengths s- 1) than in 5°C-acclimated fish (5.3 fibrelengths s-1). In order to investigate the molecular mechanism(s) underlying changes in V(max), myosin was purified by ion-exchange chromatography. No difference in myosin heavy chain composition could be detected on the basis of peptide mapping with four different proteolytic enzymes. Two-dimensional polyacrylamide gel electrophoresis revealed no myofibrillar protein isoforms unique to either acclimation temperature. However, the ratio of myosin alkali light chain contents (LC3(f):LC1(f)), as determined by capillary electrophoresis, was significantly lower in muscle from 15°C-acclimated (0.73) than from 5°C- acclimated fish (1.66). The results suggest that changes in V(max) are achieved via altered expression of myosin light chains independently of myosin heavy chain composition. In support of this hypothesis, the myofibrillar ATPase activity of fast muscle was not altered by temperature acclimation.

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KW - skinned muscle fibres

KW - teleost

KW - temperature acclimation

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