作者: Yoko Yamagata , Angus C. Nairn
DOI: 10.1016/J.BRAINRES.2015.08.023
关键词: Synapsin 、 Synapsin I 、 Kainic acid 、 Biology 、 Phosphorylation 、 Dephosphorylation 、 Ca2+/calmodulin-dependent protein kinase 、 Endocrinology 、 Substrate-level phosphorylation 、 Hippocampus 、 Internal medicine
摘要: Extracellular signal-regulated kinase 1/2 (ERK1/2) plays diverse roles in the central nervous system. Activation of ERK1/2 has been observed various types neuronal excitation, including seizure activity vivo and vitro. However, studies examining its substrate phosphorylation parallel are scarce especially models. We have studying state presynaptic protein, synapsin I at ERK1/2-dependent -independent sites models showed that was indeed under control vivo. To further expand our study, here we examined effects prolonged on by using status epilepticus induced kainic acid (KA-SE) rats In KA-SE, robust activation hippocampus, a representative limbic structure, with lesser parietal cortex, non-limbic structure. contrast, level phospho-site 4/5 profoundly decreased, extent which much larger hippocampus than cortex. addition, other ERK1/2-independent phospho-sites also an even decrease. All these changes disappeared after recovery from KA-SE. These results indicate is dynamically regulated balance between phosphatase activities. The contrasting features yet dephosphorylation may be indicative irreversible pathological outcome epileptic