Cecchi G, Griffiths P J, Taylor S
Adv Exp Med Biol. 1984;170:455-72. doi: 10.1007/978-1-4684-4703-3_41.
Calcium transients, monitored by aequorin, and force were recorded simultaneously during tetanic contractions of isolated frog skeletal muscle fibers. Quick length changes were applied to the fibers during contractions at sarcomere lengths on the descending limb of the length-tension relationship. Previous experiments showed that regulatory Ca2+ binding sites are apparently saturated during a plateau of tetanic force development at these sarcomere lengths. However, quick releases of greater than 4 to 5% of fiber length produced a momentary fall in the calcium transient that followed a time course similar to the redevelopment of force. The fall in the Ca2+ transient after a release was maximum at striation spacings about half way along the descending limb (2.6-2.7 microns), which suggests it is not related to an increase in the number of Ca2+ binding sites distributed uniformly along the filaments. The effect was absent or barely detectable when highly stretched fibers were released during contraction. The fall in the Ca2+ transient was unrelated to the time during a tetanus that a release was made or to the velocity of the release. One explanation of these results is that complexes between actin and myosin are broken by a sudden reduction of length, and as they reform during the recovery of force the affinity of troponin for Ca2+ increases. Quick stretch had no effect on the rapid decay of Ca2+ transients, but stretch increased peak force and slowed relaxation for almost a second after the end of stimulation. Evidently the decrease in the rate of relaxation produced by stretch is unrelated to changes in the amount of Ca2+ released or the rate of Ca2+ removal, which supports suggestions that the kinetics of muscle relaxation are determined by more than one mechanism. The apparent increase in the overall duration of mechanical activity after stretch probably results from the longitudinal inhomogeneity in the duration of activity - known to occur during relaxation - coupled with the decreased compliance of stretched fibers.
在离体青蛙骨骼肌纤维的强直收缩过程中,使用水母发光蛋白监测钙瞬变,并同时记录肌力。在长度-张力关系下降支的肌节长度处进行收缩时,对纤维施加快速长度变化。先前的实验表明,在这些肌节长度的强直力发展平台期,调节性Ca²⁺结合位点明显饱和。然而,大于纤维长度4%至5%的快速释放会导致钙瞬变瞬间下降,其时间进程与力的重新发展相似。释放后Ca²⁺瞬变的下降在下降支大约一半处的条纹间距(2.6 - 2.7微米)处最大,这表明它与沿细丝均匀分布的Ca²⁺结合位点数量增加无关。当在收缩过程中释放高度拉伸的纤维时,这种效应不存在或几乎检测不到。Ca²⁺瞬变的下降与强直收缩期间释放的时间或释放速度无关。这些结果的一种解释是,肌动蛋白和肌球蛋白之间的复合物因长度突然缩短而断裂,并且在力恢复过程中它们重新形成时,肌钙蛋白对Ca²⁺的亲和力增加。快速拉伸对Ca²⁺瞬变的快速衰减没有影响,但拉伸增加了峰值力,并在刺激结束后使松弛减慢了近一秒。显然,拉伸引起的松弛速率降低与Ca²⁺释放量的变化或Ca²⁺去除速率无关,这支持了肌肉松弛动力学由多种机制决定的观点。拉伸后机械活动总持续时间的明显增加可能是由于活动持续时间的纵向不均匀性(已知在松弛过程中会发生)与拉伸纤维顺应性降低相结合所致。