Cross-bridge kinetics of fast and slow fibres of cat jaw and limb muscles: Correlations with myosin subunit composition

Joseph F Y Hoh, Zhao Bo Li, Han Qin, Michael K H Hsu, Gunther H. Rossmanith

Research output: Contribution to journalArticle

Abstract

Mechanical properties of the jaw-closing muscles of the cat are poorly understood. These muscles are known to differ in myosin and fibre type compositions from limb muscles. This work aims to correlate mechanical properties of single fibres in cat jaw and limb muscles with their myosin subunit compositions. The stiffness minimum frequency, fmin, which reflects isometric cross-bridge kinetics, was measured in Ca2+- activated glycerinated fast and slow fibres from cat jaw and limb muscles for temperatures ranging between 15 and 30°C by mechanical perturbation analysis. At 15°C, fmin was 0.5 Hz for limb-slow fibres, 4-6 Hz for jaw-slow fibres, and 10-13 Hz for limb-fast and jaw-fast fibres. The activation energy for fmin obtained from the slope of the Arrhenius plot for limb-slow fibres was 30-40% higher than values for the other three types of fibres. SDS-PAGE and western blotting using highly specific antibodies verified that limb-fast fibres contained IIA or IIX myosin heavy chain (MyHC). Jaw-fast fibres expressed masticatory MyHC while both jaw-fast and jaw-slow fibres expressed masticatory myosin light chains (MLCs). The nucleotide sequences of the 3′ ends of the slow MyHC cDNAs isolated from cat masseter and soleus cDNA libraries showed identical coding and 3′-untranslated regions, suggesting that jaw-slow and limb-slow fibres express the same slow MyHC gene. We conclude that the isometric cross-bridge cycling kinetics of jaw-fast and limb-fast fibres detected by fmin are indistinguishable in spite of differences in MyHC and light chain compositions. However, jaw-slow fibres, in which the same slow MyHCs are found in combination with MLCs of the jaw type, show enhanced cross-bridge cycling kinetics and reduced activation energy for cross-bridge detachment.

Original languageEnglish (US)
Pages (from-to)329-341
Number of pages13
JournalJournal of Muscle Research and Cell Motility
Volume28
Issue number6
DOIs
StatePublished - Aug 2007
Externally publishedYes

Fingerprint

Myosins
Jaw
Muscle
Cats
Extremities
Muscles
Kinetics
Fibers
Chemical analysis
Myosin Heavy Chains
Myosin Light Chains
Activation energy
3' Untranslated Regions
Mechanical properties
Arrhenius plots
Gene Library
Polyacrylamide Gel Electrophoresis
Complementary DNA
Western Blotting
Nucleotides

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Endocrinology
  • Cell Biology

Cite this

Cross-bridge kinetics of fast and slow fibres of cat jaw and limb muscles : Correlations with myosin subunit composition. / Hoh, Joseph F Y; Li, Zhao Bo; Qin, Han; Hsu, Michael K H; Rossmanith, Gunther H.

In: Journal of Muscle Research and Cell Motility, Vol. 28, No. 6, 08.2007, p. 329-341.

Research output: Contribution to journalArticle

Hoh, Joseph F Y ; Li, Zhao Bo ; Qin, Han ; Hsu, Michael K H ; Rossmanith, Gunther H. / Cross-bridge kinetics of fast and slow fibres of cat jaw and limb muscles : Correlations with myosin subunit composition. In: Journal of Muscle Research and Cell Motility. 2007 ; Vol. 28, No. 6. pp. 329-341.
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AU - Hoh, Joseph F Y

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AU - Rossmanith, Gunther H.

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N2 - Mechanical properties of the jaw-closing muscles of the cat are poorly understood. These muscles are known to differ in myosin and fibre type compositions from limb muscles. This work aims to correlate mechanical properties of single fibres in cat jaw and limb muscles with their myosin subunit compositions. The stiffness minimum frequency, fmin, which reflects isometric cross-bridge kinetics, was measured in Ca2+- activated glycerinated fast and slow fibres from cat jaw and limb muscles for temperatures ranging between 15 and 30°C by mechanical perturbation analysis. At 15°C, fmin was 0.5 Hz for limb-slow fibres, 4-6 Hz for jaw-slow fibres, and 10-13 Hz for limb-fast and jaw-fast fibres. The activation energy for fmin obtained from the slope of the Arrhenius plot for limb-slow fibres was 30-40% higher than values for the other three types of fibres. SDS-PAGE and western blotting using highly specific antibodies verified that limb-fast fibres contained IIA or IIX myosin heavy chain (MyHC). Jaw-fast fibres expressed masticatory MyHC while both jaw-fast and jaw-slow fibres expressed masticatory myosin light chains (MLCs). The nucleotide sequences of the 3′ ends of the slow MyHC cDNAs isolated from cat masseter and soleus cDNA libraries showed identical coding and 3′-untranslated regions, suggesting that jaw-slow and limb-slow fibres express the same slow MyHC gene. We conclude that the isometric cross-bridge cycling kinetics of jaw-fast and limb-fast fibres detected by fmin are indistinguishable in spite of differences in MyHC and light chain compositions. However, jaw-slow fibres, in which the same slow MyHCs are found in combination with MLCs of the jaw type, show enhanced cross-bridge cycling kinetics and reduced activation energy for cross-bridge detachment.

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