Possible neuroprotective mechanism of human neuroglobin
Possible neuroprotective mechanism of human neuroglobin
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DOI：
10.1196/annals.1344.020
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发表时间：
2005-01-01
期刊：
影响因子：
--
通讯作者：
Morishima, I
中科院分区：
文献类型：
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作者：
Wakasugi, K;Kitatsuji, C;Morishima, I
神经珠蛋白（Neuroglobin, Ngb）是一种新发现的六坐标珠蛋白，在脊椎动物大脑中表达，具有可逆结合氧的功能。在体外和体内，Ngb的表达增加对缺氧的反应，并保护神经元免受缺氧。本文综述了近年来有关人Ngb神经保护机制的研究进展。人类铁Ngb已被发现作为鸟嘌呤核苷酸解离抑制剂的a亚基异三聚体G蛋白。此外，还鉴定了其他ngb结合蛋白。这些发现表明，人类Ngb可能作为大脑信号转导的调节剂。
Neuroglobin (Ngb) is a newly discovered hexacoordinate globin that is expressed in vertebrate brain and can reversibly bind oxygen. Expression of Ngb increases in response to oxygen deprivation and protects neurons from hypoxia in vitro and in vivo. Recent work on human Ngb has shed light on the mechanism of this neuroprotection by human Ngb, as discussed in this review. Human ferric Ngb has been found to act as a guanine nucleotide dissociation inhibitor for the a subunit of heterotrimeric G proteins. Moreover, other Ngb-binding proteins also have been identified. These findings suggest that human Ngb may function as a regulator of signal transduction in the brain.