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A globin for the brain
Author(s) -
Brunori M.,
Vallone B.
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.06-6643rev
Subject(s) - neuroglobin , myoglobin , globin , neuroprotection , chemistry , heme , microbiology and biotechnology , ligand (biochemistry) , signal transduction , biophysics , biochemistry , neuroscience , biology , receptor , hemoglobin , enzyme
The discovery that a myoglobin‐like hemeprotein (called neuroglobin) is expressed in our brain raised considerable curiosity from the standpoints of biochemistry and pathophysiology alike. Neuroglobin is involved in neuroprotection from damage due to hypoxia or ischemia in vitro and in vivo ; overexpression of neuroglobin ameliorates the recovery from stroke in experimental animals. The mechanism underlying this remarkable effect is still mysterious. Structural studies revealed that neuroglobin has a typical globin fold, and despite being hexacoordinated, it binds reversibly O 2 , CO, and NO, undergoing a substantial conformational change of the heme and of the protein. The possible mechanisms involved in neuroprotection are briefly reviewed. Neuroglobin is unlikely to be involved in O 2 transport (like myoglobin), although it seems to act as a sensor of the O 2 /NO ratio in the cell, possibly regulating the GDP/GTP exchange rate forming a specific complex with the G αβγ ‐protein when oxidized but not when bound to a gaseous ligand. Thus it appears that neuroglobin is a stress‐responsive sensor for signal transduction in the brain, mediated by a ligand‐linked conformational change of the protein.—Brunori, M., Vallone, B. A globin for the brain. FASEB J. 20, 2192–2197 (2006)