Tamagawa T, Niki H, Niki A
FEBS Lett. 1985 Apr 22;183(2):430-2. doi: 10.1016/0014-5793(85)80825-5.
The role of cytosolic free Ca2+ in insulin release was evaluated using isolated rat pancreatic islets permeabilized with digitonin and incubated in Ca-EGTA buffers to fix free Ca2+ concentration at arbitrary levels. Ca2+ induced insulin release in a concentration-dependent manner with the threshold being between 0.1 and 1 microM. The hormone release was increased by forskolin and 12-O-tetradecanoyl phorbol-13-acetate (TPA), a potent activator of adenylate cyclase and that of protein kinase C, respectively. The findings suggest that activation of both protein kinase A and protein kinase C modulate insulin release without a concomitant increase in cytosolic free Ca2+.
利用用洋地黄皂苷通透处理的大鼠分离胰岛,在Ca-EGTA缓冲液中孵育以将游离Ca2+浓度固定在任意水平,评估了胞质游离Ca2+在胰岛素释放中的作用。Ca2+以浓度依赖的方式诱导胰岛素释放,阈值在0.1至1微摩尔之间。分别作为腺苷酸环化酶和蛋白激酶C的有效激活剂的福斯高林和12-O-十四酰佛波醇-13-乙酸酯(TPA)可增加激素释放。这些发现表明,蛋白激酶A和蛋白激酶C的激活均可调节胰岛素释放,而不会伴随胞质游离Ca2+的增加。