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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Regulation of calcium-dependent (3H)noradrenaline release from rat cerebrocortical synaptosomes by protein kinase C and modulation of the actin cytoskeleton.
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Regulation of calcium-dependent (3H)noradrenaline release from rat cerebrocortical synaptosomes by protein kinase C and modulation of the actin cytoskeleton.

机译：调节蛋白激酶C和肌动蛋白细胞骨架从大鼠脑皮质突触小体释放钙依赖性（3H）去甲肾上腺素的作用。

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摘要

The effects that active phorbol esters, staurosporine, and changes in actin dynamics, might have on Ca2+ -dependent exocytosis of [3H]-labelled noradrenaline, induced by either membrane-depolarizing agents or a Ca2+ ionophore, have been examined in isolated nerve terminals in vitro. Depolarization-induced openings of voltage-dependent Ca2+ channels with 30 mM KCl or 1 mM 4-aminopyridine induced limited exocytosis of [3H]noradrenaline, presumably from a readily releasable vesicle pool. Application of the Ca2+ ionophore calcimycin (10 microM) induced more extensive [3H]noradrenaline release, presumably from intracellular reserve vesicles. Stimulation of protein kinase C with phorbol 12-myristate,13-acetate increased release evoked by all secretagogues. Staurosporine (1 microM) had no effect on depolarization-induced release, but decreased ionophore-induced release and reversed all effects of the phorbol ester. When release was induced by depolarization, internalization of the actin-destabilizing agent DNAase I into the synaptosomes gave a slight increase in [3H]NA release and strongly increased the potentiating effect of the phorbol ester. In contrast, when release was induced by the Ca2+ ionophore, DNAase I had no effect, either in the absence or presence of phorbol ester. The results indicate that depolarization of noradrenergic rat synaptosomes induces Ca2+ -dependent release from a releasable pool of staurosporine-insensitive vesicles. Activation of protein kinase C increases this release by staurosporine-sensitive mechanisms, and destabilization of the actin cytoskeleton further increases this effect of protein kinase C. In contrast, ionophore-induced noradrenaline release originates from a pool of staurosporine-sensitive vesicles, and although activation of protein kinase C increases release from this pool, DNAase I has no effect and also does not change the effect of protein kinase C. The results support the existence of two functionally distinct pools of secretory vesicles in noradrenergic CNS nerve terminals, which are regulated in distinct ways by protein kinase C and the actin cytoskeleton.
机译：在膜的去极化剂或Ca2 +离子载体中，已经研究了活性佛波酯，星形孢菌素和肌动蛋白动力学变化可能对由膜去极化剂或Ca2 +离子载体诱导的[3H]标记的去甲肾上腺素对Ca2 +依赖的胞吐作用的影响。体外。用30 mM KCl或1 mM 4-氨基吡啶进行的去极化诱导的电压依赖性Ca2 +通道的开放诱导了[3H]去甲肾上腺素的有限胞吐作用，可能是由于易于释放的囊泡池引起的。 Ca2 +离子载体降钙素（10 microM）的应用诱导了[3H]去甲肾上腺素的广泛释放，可能是从细胞内储备小泡释放出来的。佛波醇12-肉豆蔻酸酯，13-乙酸酯对蛋白激酶C的刺激增加了所有促分泌素的释放。星形孢菌素（1 microM）对去极化诱导的释放没有影响，但是减少了离子载体诱导的释放并逆转了佛波酯的所有作用。当通过去极化诱导释放时，肌动蛋白去稳定剂DNAase I内化到突触小体中，[3H] NA释放略有增加，并大大增强了佛波酯的增强作用。相反，当Ca2 +离子载体诱导释放时，无论是否存在佛波酯，DNAase I均无作用。结果表明，去甲肾上腺素能大鼠突触小体的去极化诱导了从可释放的对星形孢菌素不敏感的囊泡中Ca 2+依赖性释放。蛋白激酶C的激活通过对星形孢菌素敏感的机制增加了释放，肌动蛋白细胞骨架的不稳定进一步增强了蛋白激酶C的这种作用。相反，离子载体诱导的去甲肾上腺素释放源自对星形孢菌素敏感的囊泡，尽管活化蛋白激酶C的增加增加了该池的释放，DNA酶I没有作用，也没有改变蛋白激酶C的作用。结果支持在去甲肾上腺素能中枢神经系统神经末梢中存在两个功能不同的分泌小泡库。通过蛋白激酶C和肌动蛋白细胞骨架的不同方式。

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