Department of Biochemistry, Kitasato University School of Medicine, Sagamihara, Kanagawa 252-0374, Japan.
Department of Biochemistry, Kitasato University School of Medicine, Sagamihara, Kanagawa 252-0374, Japan.
Neurosci Lett. 2014 Feb 21;561:182-7. doi: 10.1016/j.neulet.2013.12.044. Epub 2013 Dec 27.
Synaptosomal-associated protein of 25 kDa (SNAP-25), a t-SNARE protein, plays a crucial role in neurotransmitter release by exocytosis. Protein kinase C phosphorylates SNAP-25 at Ser(187), however the physiological significance of this phosphorylation event in brain function remains unclear. In the present study, we found that SNAP-25 phosphorylation increased rapidly in the mouse brain following cold-water restraint stress. Both basal and stress-induced phosphorylation of SNAP-25 were high in stress-related brain regions, including the cerebral cortex, hippocampus, and amygdala, and the extent of phosphorylation increased with increasing amounts of stress. Intravenous administration of adrenaline increased SNAP-25 phosphorylation, although stress-induced phosphorylation was still observed in adrenalectomized mice. These results indicate that SNAP-25 phosphorylation is regulated in a stress-dependent manner through both central and peripheral mechanisms.
突触相关蛋白 25kDa（SNAP-25）是一种 t-SNARE 蛋白，在神经递质释放的胞吐作用中发挥着关键作用。蛋白激酶 C 可使 SNAP-25 的丝氨酸 187 位发生磷酸化，然而，这种磷酸化事件在大脑功能中的生理意义尚不清楚。在本研究中，我们发现冷水束缚应激后，小鼠大脑中的 SNAP-25 磷酸化迅速增加。应激相关脑区（包括大脑皮层、海马和杏仁核）中的 SNAP-25 的基础磷酸化和应激诱导的磷酸化水平均较高，且随着应激程度的增加，磷酸化程度也随之增加。静脉内给予肾上腺素可增加 SNAP-25 的磷酸化，尽管在肾上腺切除的小鼠中仍观察到应激诱导的磷酸化。这些结果表明，SNAP-25 的磷酸化通过中枢和外周机制以应激依赖的方式进行调节。
