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4. Sarcomere-length dependence of lattice volume and radial mass transfer of myosin cross-bridges in rat papillary muscle.

Author

Naoto Yagi, Hiroshi Okuyama, Hiroko Toyota, Junichi Araki, Juichiro Shimizu, Gentaro Iribe, Kazufumi Nakamura, Satoshi Mohri, Katsuhiko Tsujioka, Hiroyuki Suga, and Fumihiko Kajiya

Subjects
CYTOPLASMIC filaments, MYOSIN, MUSCLES, CYTOPLASM, MUSCLE proteins, X-ray diffraction
Abstract

We examined the sarcomere length-dependence of the spacing of the hexagonal lattice of the myofilaments and the mass transfer of myosin cross-bridges during contraction of right ventricular papillary muscle of the rat. The lattice spacing and mass transfer were measured by using X-ray diffraction, and the sarcomere length was monitored by laser diffraction at the same time. Although the lattice spacing and the sarcomere length were inversely related, their relationship was not exactly isovolumic. The cell volume decreased by about 15% when the sarcomere length was shortened from 2.3 µm to 1.8 µm. Twitch tension increased with sarcomere length (the Frank–Starling law). At the peak tension, the ratio of the intensity of the (1,0) equatorial reflection to that of the (1,1) reflection was smaller when the tension was greater, showing that the larger tension at a longer sarcomere length accompanies a larger amount of mass transfer of cross-bridges from the thick to the thin filament. The result suggests that the Frank–Starling law is due to an increase in the number of myosin heads attached to actin, not in the average force produced by each head. [ABSTRACT FROM AUTHOR]

Published
2004
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