Connecting Filaments, Core Filaments, and Side-Struts: A Proposal to Add Three New Load-Bearing Structures to the Sliding Filament Model

  • Alan Magid
  • H. P. Ting-Beall
  • Melanie Carvell
  • Theda Kontis
  • Carmen Lucaveche
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 37)


This report concerns structural forces in resting muscle and proposes three additions to the sliding filament model to account for these mechanical properties. The proposal includes: connecting filaments (C-filaments) which connect the ends of each thick filament to the neighboring Z-lines, core filaments which support the myosin of the thick filament and which attach to the C-filaments, and side-struts which bind the thick filaments together along their length and restrict their radial movement. C-filaments would act as the parallel elastic element and transmit the passive tension to the thick filaments.

Isolated myofibrils (mechanically-skinned and detergent-treated frog semitendinosus fibers) when stretched progressively showed exponentially-increasing passive tension which did not disappear when filament overlap was exceeded, but continued to rise. SL was monitored with a HeNe laser. Passive tension phasically exceeded 3x105 N/M2.

Electron microscopy (thin-sectioned and freeze-fracture/deep-etch specimens) of non-overlap fibers showed orderly fibril structure with clear separation of A- and I-bands. In the gap between them could be seen filaments, 4.0-50 Å in diameter, connected to the thick filament ends. Unlike actin, these filaments did not become decorated by myosin S-1.

Equatorial X-ray measurements showed that stretching relaxed skinned muscles squeezed the thick filaments closer; this radial compression continued beyond filament overlap.

Extreme stretch of fibers caused the thick filaments to strain several-fold.

Treatment of non-overlap fibers with a high ionic strength pyrophosphate myosin solvent caused a large drop in passive tension and stiffness, but no change in SL was detected nor was myofibril continuity detectably affected.

Non-overlap fibrils, when treated with elastase, released A-segments which retain three-dimensional coherency. Deep-etch EM’s of non-overlap fibers disclosed abundant structures (about 75 Å) wide attaching adjacent thick filaments.


Thin Filament Sarcomere Length Thick Filament Passive Tension Skinned Fiber 
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Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • Alan Magid
    • 1
  • H. P. Ting-Beall
    • 1
  • Melanie Carvell
    • 1
  • Theda Kontis
    • 1
  • Carmen Lucaveche
    • 1
  1. 1.Department of AnatomyDuke University Medical CenterDurhamUSA

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