4.7 Article

Force produced by isolated sarcomeres and half-sarcomeres after an imposed stretch

Journal

AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
Volume 302, Issue 1, Pages C240-C248

Publisher

AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpcell.00208.2011

Keywords

myofibrils; myosin; titin; cross-bridges

Funding

  1. Canadian Institutes for Health Research (CIHR)

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Rassier DE, Pavlov I. Force produced by isolated sarcomeres and half-sarcomeres after an imposed stretch. Am J Physiol Cell Physiol 302: C240-C248, 2012. First published October 12, 2011; doi: 10.1152/ajpcell.00208.2011.-When a stretch is imposed to activated muscles, there is a residual force enhancement that persists after the stretch; the force is higher than that produced during an isometric contraction in the corresponding length. The mechanisms behind the force enhancement remain elusive, and there is disagreement if it represents a sarcomeric property, or if it is associated with length nonuniformities among sarcomeres and half-sarcomeres. The purpose of this study was to investigate the effects of stretch on single sarcomeres and myofibrils with predetermined numbers of sarcomeres (n = 2, 3 ..., 8) isolated from the rabbit psoas muscle. Sarcomeres were attached between two precalibrated microneedles for force measurements, and images of the preparations were projected onto a linear photodiode array for measurements of half-sarcomere length (SL). Fully activated sarcomeres were subjected to a stretch (5-10% of initial SL, at a speed of 0.3 mu m.s(-1) . SL-1) after which they were maintained isometric for at least 5 s before deactivation. Single sarcomeres showed two patterns: 31 sarcomeres showed a small level of force enhancement after stretch (10.46 +/- 0.78%), and 28 sarcomeres did not show force enhancement (-0.54 +/- 0.17%). In these preparations, there was not a strong correlation between the force enhancement and half-sarcomere length nonuniformities. When three or more sarcomeres arranged in series were stretched, force enhancement was always observed, and it increased linearly with the degree of half-sarcomere length nonuniformities. The results show that the residual force enhancement has two mechanisms: 1) stretch-induced changes in sarcomeric structure(s); we suggest that titin is responsible for this component, and 2) stretch-induced nonuniformities of half-sarcomere lengths, which significantly increases the level of force enhancement.

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