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Possible Neuroprotective Mechanism of Human Neuroglobin
Author(s) -
WAKASUGI KEISUKE,
KITATSUJI CHIHIRO,
MORISHIMA ISAO
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2005.tb00028.x
Subject(s) - neuroglobin , neuroprotection , hexacoordinate , microbiology and biotechnology , chemistry , globin , protein subunit , heterotrimeric g protein , biochemistry , biology , signal transduction , pharmacology , g protein , hemoglobin , gene , organic chemistry , silicon
A bstract : 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 α 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.