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Media highlights in the Dec. 15 issue of Biophysical Journal
Date:12/7/2007

oring both individual sarcomeres using an inverted phase-contrast microscope, and by measuring their generated force. Contrary to the textbook version of the length-tension relationship, in which the generated force decreases with stretching muscle above its optimum length, a larger active force was generated at longer muscle lengths. Furthermore, the authors linked this cooperative force enhancement with the changes in three-dimensional structure of sarcomeres by monitoring the distance between the actin and myosin filaments. The authors find that the developed force is significantly modulated by tiny (less than 1 nm) changes in the interfilament distance. This property must be characteristic of striated muscles, in which the two filaments form a liquid crystal-like array. This discovery suggests a new chapter in our understanding of the regulation of muscle contraction by narrowing the focusing on the myosin molecules. This is a significant advance in the regulation of muscle contraction that was pioneered in 1972 by Professor M. Endo.


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Contact: Ellen R. Weiss
eweiss@biophysics.org
301-634-7176
Biophysical Society
Source:Eurekalert

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