Neuroglobin co-localize and migrate with mitochondria in neural cells
作者单位：Laboratory For Functional study of astrocytes Neuroscience Research Institute Key Laboratory for Neuroscience of the Ministry of Education
会议名称：《中国神经科学学会第十二届全国学术会议》
会议日期：2017年
学科分类：0710[理学-生物学] 07[理学] 071006[理学-神经生物学]
关 键 词：neuroglobin mitochondria astrocytes neurons
摘 要：Human brain constitutes 2 % of the total body weight, but utilizes over 20 % of the body oxygen at rest. The discovery of neuroglobin（Ngb） in both neurons and astrocytes suggest that Ngb might be closely involved in brain oxygen homeostasis. In the present study, we have investigated the expression, distribution and mobility of Ngb compared to cytoglobin（Cygb）, a universal cellular respiratory globin, in primary astrocytes and neurons. Unlike Cygb, the expression levels of Ngb in astrocytes and neurons increased under both ischemia and rotenone treatment. A co-localization of either endogenous or recombinant Ngb with mitochondria was evidenced using immunostaining and western blot. Furthermore, the L136 P Ngb mutant enhances the colocalization of Ngb and mitochondria under both normoxic and ischemic conditions. A co-migration of L136 P Ngb with mitochondria in the neurite of neurons was also observed. More interestingly, the co-migration and co-localization of L136 P Ngb with mitochondrial was abolished when cultures were treated with cytoskeleton inhibitors such as cytochalasin D, colchicine and nocodazole. Overall, our data demonstrated that Ngb is a migratory protein in cytoplasm that co-localize with mitochondria under both physiological and pathological conditions. In addition, the co-migration of Ngb with mitochondria requires microfilament. Based on our investigation, we propose the hypothesis that Ngb might have distinctive roles during oxygen transportation in comparison to Cygb and serve as an ‘emergency and mobile’ intrinsic protective protein in nervous system.