Monitoring the structural behavior of troponin and myoplasmic free Ca2+ concentration during twitch of frog skeletal muscle.

Biophysical Journal
Tatsuhito MatsuoNaoto Yagi

Abstract

The interaction of troponin molecules on the thin filament with Ca(2+) plays a key role in regulating muscle contraction. To characterize the structural changes of troponin caused by Ca(2+) and crossbridge formation, we recorded the small-angle x-ray intensity and the myoplasmic free Ca(2+) concentration using fluo-3 AM in the same frog skeletal muscle during twitch elicited by a single electrical pulse at 16 degrees C. In an overstretched muscle, the intensity of the meridional reflection from troponin at 1/38.5 nm(-1) began to change at 4 ms after the stimulus, reached a peak at 10 ms, and returned to the resting level with a halftime of 25 ms. The concentration of troponin-bound Ca(2+) began to increase at 1-2 ms after the stimulus, reached a peak at 5 ms, and returned to the resting level with a halftime of 40 ms, indicating that troponin begins to change conformation only after a sizable amount of Ca(2+) has bound to it, and returns to the resting structure even when there is still some bound Ca(2+). In a muscle with a filament overlap, crossbridge formation appears to slow down Ca(2+) release from troponin and have a large effect on its conformation.

References

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Citations

Apr 13, 2011·Proceedings of the National Academy of Sciences of the United States of America·Massimo ReconditiMalcolm Irving
Mar 13, 2014·Proceedings of the National Academy of Sciences of the United States of America·Luca FusiMalcolm Irving
Dec 18, 2013·The Journal of Physiology·Massimo ReconditiGabriella Piazzesi
Oct 26, 2010·Progress in Biophysics and Molecular Biology·N Yagi
Oct 7, 2016·Frontiers in Physiology·Henry G Zot, Javier E Hasbun
Feb 4, 2014·Journal of Physics. Conference Series·Bipin SinghVivek V Nagarkar

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