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Related Experiment Videos

Myofilament diameters: an ultrastructural re-evaluation.

T F Robinson, L Cohen-Gould

    Advances in Experimental Medicine and Biology
    |January 1, 1984
    PubMed
    Summary

    Ultrastructural measurements reveal new muscle filament diameters. These findings, using unstained de-embedded sections, challenge previous data on skeletal and heart muscle contractile filaments.

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    Area of Science:

    • Muscle physiology
    • Cellular ultrastructure
    • Biophysics

    Background:

    • Previous ultrastructural measurements of muscle contractile filaments used stained epoxy sections.
    • These methods may have introduced artifacts affecting diameter measurements.
    • Discrepancies exist in reported filament diameters, impacting models of muscle contraction.

    Purpose of the Study:

    • To obtain accurate in situ ultrastructural measurements of muscle filament diameters.
    • To compare results from unstained, de-embedded sections with previous findings.
    • To reassess muscle lattice geometry and its implications for cross-bridge theory.

    Main Methods:

    • Muscle samples (rat atrium, frog sartorius) were fixed and embedded in polyethylene glycol.
    • Sections were de-embedded, critical point dried, and viewed via electron microscopy without staining.
    • Filament backbone and thin filament diameters were measured in specific muscle regions.

    Main Results:

    • Thick filament backbone diameters averaged 25 nm (corrected for shrinkage).
    • Thin filament diameters ranged from 6.5-9.5 nm.
    • Thick filament profiles in overlap regions varied, with diameters up to 36 nm and non-circular shapes observed.

    Conclusions:

    • New measurements using unstained sections provide revised filament diameter data.
    • The observed lattice geometry suggests close filament proximity.
    • Findings support existing data from rotary shadowing and osmotic compression studies, impacting cross-bridge theory.

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