Structural changes following the photolytic release of ATP were observed in single, permeabilised fibres of frog skeletal muscle at 5-6 C, using time-resolved, low-angle X-ray diffraction. The structural order in the fibres and their isometric function were preserved by cross-linking 10-20 % of the myosin cross-bridges to the thin filaments. 2. The time courses of the change in force, stiffness and in intensity of the main equatorial reflections (1,0) and (1,1), of the third myosin layer line (M3) at a reciprocal spacing of (14.5 nm)-1 on the meridian and of the first myosin-actin layer line (LL1) were measured with 1 ms time resolution. 3. In the absence of Ca2+, photolytic release of ATP in muscle fibres initially in the rigor state caused the force and stiffness to decrease monotonically towards their values in relaxed muscle fibres. 4. In the presence of Ca2+, photolytic release of ATP resulted in an initial rapid decrease in force, followed by a slower increase to the isometric plateau. Muscle fibre stiffness decreased rapidly to approximately 65 % of its value in rigor. 5. In the absence of Ca2+, changes on the equator, in LL1 and in M3 occurred with a time scale comparable to that of the changes in tension and stiffness. 6. In the presence of Ca2+, the changes on the equator and LL1 occurred simultaneously with the early phase of tension decrease. The changes in the intensity of M3 (IM3) occurred on the time scale of the subsequent increase in force. The time courses of the changes in tension and IM3 were similar following the photolytic release of 0. 33 or 1.1 mM ATP. However the gradual return towards the rigor state began earlier when only 0.33 mM ATP was released. 7. In the presence of Ca2+, the time course of changes in IM3 closely mimicked that of force development following photolytic release of ATP. This is consistent with models that propose that force development results from a change in the average orientation of cross-bridges, although other factors, such as their redistribution, may also be involved.
摘要
在5-6摄氏度下,使用时间分辨低角度X射线衍射,在单个通透的青蛙骨骼肌纤维中观察到ATP光解释放后的结构变化。通过将10%-20%的肌球蛋白横桥交联到细肌丝上,纤维中的结构秩序及其等长功能得以保留。2. 以1毫秒的时间分辨率测量了力、刚度以及主要赤道反射(1,0)和(1,1)、子午线处倒数间距为(14.5纳米)-1的第三肌球蛋白层线(M3)和第一肌动蛋白-肌球蛋白层线(LL1)强度变化的时间进程。3. 在没有Ca2+的情况下,最初处于僵直状态的肌肉纤维中ATP的光解释放导致力和刚度朝着其在松弛肌肉纤维中的值单调下降。4. 在有Ca2+的情况下,ATP的光解释放导致力最初迅速下降,随后缓慢增加至等长平台期。肌肉纤维刚度迅速下降至其在僵直状态下值的约65%。5. 在没有Ca2+的情况下,赤道、LL1和M3上的变化发生的时间尺度与张力和刚度变化的时间尺度相当。6. 在有Ca2+的情况下,赤道和LL1上的变化与张力下降的早期阶段同时发生。M3强度(IM3)的变化发生在随后力增加的时间尺度上。在光解释放0.33或1.1 mM ATP后,张力和IM3变化的时间进程相似。然而,当仅释放0.33 mM ATP时,向僵直状态的逐渐恢复开始得更早。7. 在有Ca2+的情况下,IM3变化的时间进程紧密模仿了ATP光解释放后力发展的时间进程。这与提出力发展源于横桥平均取向变化的模型一致,尽管其他因素,如它们的重新分布,也可能参与其中。