Yamagata Yoko
Department of Information Physiology, National Institute for Physiological Sciences, and The Graduate University for Advanced Studies (SOKENDAI), Okazaki, Japan.
J Pharmacol Sci. 2003 Sep;93(1):22-9. doi: 10.1254/jphs.93.22.
Synapsin I is a synaptic vesicle-associated protein that is phosphorylated at multiple sites by various protein kinases. It has been proposed to play an important role in the regulation of neurotransmitter release and the organization of cytoskeletal architecture in the presynaptic terminal. In the present minireview, I describe the dynamic changes in synapsin I phosphorylation induced by acute neuronal excitation in vivo, and discuss its regulation by protein kinases and phosphatases and its functional significance in vivo. When acute neuronal excitation was induced by electroconvulsive treatment (ECT) in rats, phosphorylation of synapsin I at multiple sites was decreased during brief seizure activity in hippocampal and parieto-cortical homogenates. After termination of the seizure activity, phosphorylation at mitogen-activated protein kinase-dependent sites was increased dramatically. Phosphorylation at a Ca(2+)/calmodulin-dependent protein kinase II-dependent site was also increased moderately afterwards. The dynamic and differential changes in synapsin I phosphorylation induced by acute neuronal excitation may be involved in plastic changes induced by ECT and may have some role in its effectiveness for the treatment of psychiatric diseases in humans.
突触素I是一种与突触小泡相关的蛋白质，可被多种蛋白激酶在多个位点磷酸化。有人提出它在神经递质释放的调节和突触前终末细胞骨架结构的组织中起重要作用。在本综述中，我描述了体内急性神经元兴奋诱导的突触素I磷酸化的动态变化，并讨论了其受蛋白激酶和磷酸酶的调节及其在体内的功能意义。当通过电惊厥治疗（ECT）在大鼠中诱导急性神经元兴奋时，在海马和顶叶皮质匀浆的短暂癫痫发作活动期间，突触素I在多个位点的磷酸化减少。癫痫发作活动终止后，丝裂原活化蛋白激酶依赖性位点的磷酸化显著增加。之后，钙/钙调蛋白依赖性蛋白激酶II依赖性位点的磷酸化也适度增加。急性神经元兴奋诱导的突触素I磷酸化的动态和差异变化可能参与了ECT诱导的可塑性变化，并且可能在其对人类精神疾病的治疗效果中起一定作用。
