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Possible Contribution of Titin Filaments to the Compliant Series Elastic Component in Horseshoe Crab Skeletal Muscle Fibers

  • Haruo Sugi
  • Tsuyoshi Akimoto
  • Takakazu Kobayashi
  • Suechika Suzuki
  • Mitsuyo Shimada
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 481)

Abstract

In horseshoe crab skeletal muscle fibers, the extension of SEC at the maximum isometric force P 0 is about 6% of the slack fiber length L 0 (sarcomere length, 7 μm), i.e., about 210 nm per half-sarcomere, being too large to be explained by the cross-bridge and the thin filament elasticities. Cinematographic studies of isometrically contracting myofibril bundes indicate that the highly compliant SEC mostly originates from the “elastic” thick filament misalignment in each A-band during isometric force generation. Possible contribution of the titin filaments to the “elastic” thick filament misalignment is discussed.

Keywords

Thin Filament Isometric Force Horseshoe Crab Sarcomere Length Thick Filament 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 2000

Authors and Affiliations

  • Haruo Sugi
    • 1
  • Tsuyoshi Akimoto
    • 1
  • Takakazu Kobayashi
    • 1
  • Suechika Suzuki
    • 1
  • Mitsuyo Shimada
    • 1
  1. 1.Department of Physiology, School of MedicineTeikyo UniversityItabashi-ku, TokyoJapan

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