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Observing cycling of a few cross-bridges during isometric contraction of skeletal muscle.


ABSTRACT: During muscle contraction a myosin cross-bridge imparts periodic force impulses to actin. It is possible to visualize those impulses by observing a few molecules of actin or myosin. We have followed the time course of orientation change of a few actin molecules during isometric contraction by measuring parallel polarized intensity of its fluorescence. The orientation of actin reflects local bending of a thin filament and is different when a cross-bridge binds to, or is detached from, F-actin. The changes in orientation were characterized by periods of activity during which myosin cross-bridges interacted normally with actin, interspersed with periods of inactivity during which actin and myosin were unable to interact. The periods of activity lasted on average 1.2 +/- 0.4 s and were separated on average by 2.3 +/- 1.0 s. During active period, actin orientation oscillated between the two extreme values with the ON and OFF times of 0.4 +/- 0.2 and 0.7 +/- 0.4 s, respectively. When the contraction was induced by a low concentration of ATP both active and inactive times were longer and approximately equal. These results imply that cross-bridges interact with actin in bursts and suggest that during active period, on average 36% of cross-bridges are involved in force generation.

SUBMITTER: Mettikolla P 

PROVIDER: S-EPMC2896876 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature

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Observing cycling of a few cross-bridges during isometric contraction of skeletal muscle.

Mettikolla P P   Calander N N   Luchowski R R   Gryczynski I I   Gryczynski Z Z   Borejdo J J  

Cytoskeleton (Hoboken, N.J.) 20100601 6


During muscle contraction a myosin cross-bridge imparts periodic force impulses to actin. It is possible to visualize those impulses by observing a few molecules of actin or myosin. We have followed the time course of orientation change of a few actin molecules during isometric contraction by measuring parallel polarized intensity of its fluorescence. The orientation of actin reflects local bending of a thin filament and is different when a cross-bridge binds to, or is detached from, F-actin. Th  ...[more]

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