FASEB J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Brunori, M.
Right arrow Articles by Vallone, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Brunori, M.
Right arrow Articles by Vallone, B.
(The FASEB Journal. 2006;20:2192-2197.)
© 2006 FASEB

A Globin for the Brain

M. Brunori1 and B. Vallone

Istituto Pasteur-Fondazione Cenci Bolognetti and Department of Biochemical Sciences, University of Rome "La Sapienza," Rome, Italy

1Correspondence: Dipartimento di Scienze Biochimiche "A. Rossi Fanelli," Università di Roma "La Sapienza," Piazzale A. Moro 5, 00185 Rome, Italy. E-mail: maurizio.brunori{at}uniroma1.it

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 O2, 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 O2 transport (like myoglobin), although it seems to act as a sensor of the O2/NO ratio in the cell, possibly regulating the GDP/GTP exchange rate forming a specific complex with the G{alpha}ß{gamma}-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.


Key Words: neuroprotection • O2/NO binding • structure




This article has been cited by other articles:


Home page
 Biophys. JHome page
M. Anselmi, M. Brunori, B. Vallone, and A. Di Nola
Molecular Dynamics Simulation of Deoxy and Carboxy Murine Neuroglobin in Water
Biophys. J., July 15, 2007; 93(2): 434 - 441.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2006 by The Federation of American Societies for Experimental Biology.