Lea T J, Ashley C C
University Laboratory of Physiology, Oxford, Great Britain.
Pflugers Arch. 1989 Feb;413(4):401-6. doi: 10.1007/BF00584490.
Isometric tension and aequorin light were recorded from isolated myofibrillar bundles (diameter 0.2 mm) of barnacle muscle fibres to examine Ca release from the sarcoplasmic reticulum (SR). Transfer of a bundle from a pCa 6.7 solution to a pCa 5.8 solution, both buffered with 0.1 mM EGTA, resulted in a phasic increase in myofibrillar free Ca2+ which was superimposed on a slow rise to a steady level and a fast rise in tension. The peak of the free Ca2+ response was higher than the free Ca2+ in the bulk solution. Treatment of the bundle with the detergent Brij to destroy the SR membranes abolished the phasic rise in Ca2+ and considerably reduced the amplitude of contraction. A second challenge of a bundle to the pCa 5.8 solution without prior reloading of the SR Ca store gave a much reduced phasic component. When a pCa 5.8 solution with 1.0 mM EGTA buffering was used, the phasic rise in myofibrillar free Ca2+ could not be detected and the rise in tension was four times slower than with 0.1 mM EGTA. The results are consistent with the operation of a Ca-induced Ca release mechanism in the SR membrane of this crustacean muscle.
从藤壶肌纤维的离体肌原纤维束(直径0.2毫米)记录等长张力和水母发光蛋白荧光,以研究肌浆网(SR)的钙释放。将一束肌原纤维从用0.1 mM乙二醇双四乙酸(EGTA)缓冲的pCa 6.7溶液转移至pCa 5.8溶液,导致肌原纤维游离Ca2+呈阶段性增加,该增加叠加在缓慢上升至稳定水平以及张力快速上升之上。游离Ca2+反应的峰值高于总体溶液中的游离Ca2+。用去污剂Brij处理肌原纤维束以破坏SR膜,消除了Ca2+的阶段性上升,并显著降低了收缩幅度。在未预先重新加载SR钙库的情况下,将一束肌原纤维再次置于pCa 5.8溶液中,阶段性成分大幅减少。当使用用1.0 mM EGTA缓冲的pCa 5.8溶液时,未检测到肌原纤维游离Ca2+的阶段性上升,且张力上升速度比使用0.1 mM EGTA时慢四倍。这些结果与这种甲壳类动物肌肉的SR膜中钙诱导钙释放机制的运作相一致。