Key result
Electron microscopy identifies thin elastic filament networks persisting in myosin-extracted striated muscle.
Why the study?
The ultrastructural characteristics of myosin-extracted striated muscle fibers and the nature of remaining thin filaments were not fully described.
Thin filaments bridge actin-myosin gaps and are likely elastic; leaves open their role in myocardial passive stiffness.
Electron microscope examination of myosin-extracted psoas muscle of the rabbit reveals a number of thin filaments, about 25 Ä in diameter, bridging the gap between the ends of the actins and the remaining myosin of the M band. Extraction of actin from the region of the Z disc shows similar thin filaments near the Z disc. Myosin-extraction of several invertebrate muscles reveals a remaining network of thin filaments in the region of the A band. These thin filaments are probably elastic, and could contribute to the functioning of these muscles.
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Walcott et al. (1967) studied this question. Myosin-extraction was evaluated on Observation of thin filaments. Electron microscopy of myosin-extracted striated muscle fibers from rabbits and invertebrates revealed remaining networks of thin elastic filaments that may contribute to muscle function.
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