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Cross-bridge attachment in relaxed muscle.

M Schoenberg, B Brenner, J M Chalovich

Advances in Experimental Medicine and Biology

|January 1, 1984

Summary

Rabbit muscle fiber stiffness depends on stretch speed and ionic strength, indicating dynamic cross-bridge interactions. These cross-bridges are sensitive to nucleotide binding, influencing muscle contraction mechanics.

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Area of Science:

Muscle physiology
Biophysics
Skeletal muscle mechanics

Background:

Understanding the mechanical properties of muscle fibers is crucial for comprehending muscle function.
The role of cross-bridges in muscle stiffness, particularly under varying conditions, requires detailed investigation.

Purpose of the Study:

To quantify the stiffness of relaxed, skinned rabbit psoas muscle fibers.
To investigate the influence of stretch velocity and ionic strength on fiber stiffness.
To elucidate the nature of cross-bridge attachments in relaxed muscle.

Main Methods:

Measurements of force and sarcomere length changes in skinned rabbit psoas fibers during controlled stretches.
Experiments conducted at 5°C in low ionic strength relaxing solution (μ = 0.02 M).
Varying stretch velocities from slow (0.5% in >30 ms) to fast (0.5% in 150 μs) and ionic strengths (0.02 M to 0.17 M).

Main Results:

Fiber stiffness is negligible at very slow stretch velocities but increases significantly with faster stretches.
Stiffness is highly sensitive to ionic strength, decreasing over 20-fold from 0.02 M to 0.17 M.
Ionic strength-dependent stiffness correlates with actin-myosin filament overlap, suggesting cross-bridge involvement.

Conclusions:

The observed stiffness in relaxed muscle fibers is primarily due to attached cross-bridges.
The velocity dependence of stiffness indicates that cross-bridges are in a dynamic equilibrium between attached and detached states.
Nucleotide interactions, as suggested by experiments with adenylyl-imido-diphosphate, modulate the rates of cross-bridge attachment and detachment.

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