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应用PCS和AFM研究单价阳离子和通道功能状态对兔骨骼肌ryanodine受体(钙释放通道)相互作用的影响 总被引:1,自引:0,他引:1
Ryanodine受体(RyR)是位于细胞内钙库膜上的一种钙释放通道。对骨骼肌和心肌的肌浆网的电镜研究表明RyR在膜上相互连接在一起,形成大片规则的二维晶格排列。近年来理论模型和试验证据表明,排列在一起的RyR在通道打开和关闭时存在协同效应,即具有“门控偶联”的调控机制。研究RyR之间相互作用的基本规律及其调控因素对于深入了解这种机制具有重要意义。在我们的工作中,主要采用两种互补的手段:光子相关光谱法(PCS)和原子力显微镜(AFM)来研究溶液中RyR的相互作用。初步的研究主要集中在细胞内两种主要的单价阳离子Na’和K’,以及RyR的功能状态对该通道相互作用的影响。 相似文献
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Using Arsenazo Ⅲ as a myoplasmic calcium indicator, we have studied the calcium transients evoked by voltage-clamp depolarizing pulses in frog twitch muscle fibres which had been temporarily depolarized by 80 mmol/LK~+ in the absence or presence of myoplasmic Li~+. After the high K~+ exposure, for either a short (15 rain) or long(1 h) time, the post-K~+ calcium transients could gradually be restored to the level of the pre-K~+ ones, if the fibres were not loaded with Li~+.In contrast, the post-K~+ calcium transients of Li~+-loaded fibres could not fully recover,and were depressed in a Li~+ concentration-dependent manner.The mean amplitude of the post-K~+ responses recorded more than 3.5 h after 15 min high K~+ exposure was reduced to 56% of pre-K~+ control in the fibres which had been loaded with Li~+ in 20 mmol/L Li~+ Ringer's solution.This depression could be prevented or partially reversed by exogenous myo-inositol.More depression could be induced by 1 h high K~+ exposure, but the presence of exogen 相似文献
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It is shown in rats that cross-innervation of the fast-twitch muscle extensor digitorumlongus (EDL) by the nerve of the slow-twitch muscle soleus (SOL) can cause a complete trans-formation of the Z-band width from the fast to the slow muscle fibre type within two weeksand that it can still induce such a transformation, though usually less completely, even whenimpulse activity is excluded by chronical tetrodotoxin (TTX) block of the nerve. Thisprovides a piece of clear-cut evidence for the presence of some activity-independent trophicfactor in the neural determination of skeletal muscle fibre type. 相似文献
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兔骨骼肌ryanodine受体/钙释放通道的AFM研究 总被引:1,自引:0,他引:1
Ryanodine受体(RyR)是位于细胞内质网膜上的钙释放通道,在肌细胞的兴奋-收缩偶联中发挥重要作用。RyR难于结晶,以往主要是用电镜和计算机三维重组相结合的方法来获得其高级结构的信息。由于RyR结构庞大,易于水解,在提取的过程中需要加入外源性磷脂以保护其结构,而磷脂的存在对电镜的分辨率有影响,所以电镜研究的RyR在提 过程中一般不添加外源性磷脂,这样得到的结构信息并没有反映RyR在生理状况下的真实情况,我们用原子力显微镜(AFM)对RyR进行研究,经过了空气中RyR成像,液体中RyR成像,重组到脂双层中的RyR研究几个阶段,提供了RyR在接近生理条件下的结构信息,并为进一步研究其结构和功能的关系打下了基础。 相似文献