INTERACTION OF RAB3A W/ SYNAPTIC VESICLES

我们以前表明，钙离子和钙离子结合蛋白，钙调素，可以一起行动，取代GTP结合蛋白，Rab3A，从猕猴脑前额叶皮层突触囊泡膜。 这一新的观察结果的生理相关性仍有待确定，但研究整个大鼠脑突触体和他们的匀浆由其他调查人员提出了一种特殊的机制可能会增加激活的神经末梢中的局部浓度的Ca 2+钙调素和Rab3A可能会从突触囊泡在神经递质分泌的过程中解离的可能性。 去年，我们研究了猕猴大脑前额叶皮层的去极化突触体，试图重现在大鼠大脑制备研究中取得的发现。 我们能够制备猕猴突触体，可以显示出戏剧性的神经分泌反应，但当我们试图将它们均质化时，去极化的突触体被证明是出乎意料的稳定。 因此，我们停止了实验，并在《生物化学杂志》上发表了我们的发现。

We showed previously that Ca2+ and the Ca2+-binding protein, calmodulin, can act together to displace the GTP-binding protein, Rab3A, from macaque brain prefrontal cortex synaptic vesicle membranes. The physiological relevance of this new observation remains to be determined, but studies of whole rat brain synaptosomes and their homogenates by other investigators have raised the possibilities that a special mechanism may increase the local concentration of Ca2+ calmodulin in activated nerve terminals and that Rab3A may dissociate from synaptic vesicles during the process of neurotransmitter secretion. Last year we studied depolarized synaptosomes from the prefrontal cortex of macaque brains in an attempt to reproduce the findings that had been made in studies of rat brain preparations. We were able to prepare macaque synaptosomes that could show a dramatic neurosecretory response, but when we attempted to homogenize them, the depolarized synaptosomes proved to be unexpectedly stable. We therefore discontinued the experiments and published our findings in the Journal of Biological Chemistry.