INTERACTION OF RAB3A W/ SYNAPTIC VESICLES

我们以前表明，钙离子和钙离子结合蛋白， 钙调蛋白，可以共同作用，取代GTP结合蛋白， Rab3A，来自猕猴脑前额叶皮层突触囊泡 膜。 这一新发现的生理相关性 还有待确定，但对整个大鼠大脑突触体的研究 其他研究者对它们的匀浆进行了研究， 一种特殊的机制可能会增加当地的 激活的神经末梢中的Ca 2+钙调素浓度， Rab3A在突触形成过程中可能与突触囊泡分离， 神经递质分泌 去年我们研究了去极化 猕猴大脑前额叶皮层的突触体， 试图重现大鼠研究中的发现， 大脑准备 我们能够制备猕猴突触体， 可以显示出剧烈的神经分泌反应，但是当我们试图 为了使它们均匀化，去极化突触体被证明是 出乎意料的稳定。 因此，我们停止了实验， 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.