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M402011200v1
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Papers In Press, published online ahead of print March 31, 2004
J. Biol. Chem, 10.1074/jbc.M402011200
Submitted on February 24, 2004
Revised on March 22, 2004
Accepted on March 31, 2004

Zebrafish reveals different and conserved features of vertebrate neuroglobin gene structure, expression pattern and ligand binding

Christine Fuchs, Valeska Heib, Laurent Kiger, Mark Haberkamp, Anja Roesner, Marc Schmidt, Djemel Hamdane, Michael C. Marden, Thomas Hankeln, and Thorsten Burmester

Institute of Zoology, University of Mainz, Mainz D-55099

Corresponding Author: burmeste{at}mail.uni-mainz.de

Neuroglobin has been identified as a respiratory protein that is primarily expressed in the mammalian nervous system. Here we present the first detailed analysis of neuroglobin from a non-mammalian vertebrate, the zebrafish Danio rerio. The zebrafish neuroglobin gene reveals a mammalian-type exon-intron pattern in the coding region (B12.2, E11.0, G7.0), plus an additional 5' non-coding exon. Like the mammalian neuroglobin, the zebrafish protein displays a hexacoordinate deoxy-binding scheme. Flash photolysis kinetics show the competitive binding on the ms timescale of external ligands and the distal histidine, resulting in an oxygen affinity of 1 torr. Western blotting, immune staining and mRNA in situ hybridization demonstrate neuroglobin expression in the fish central nervous system, the retina, but also in the gills. Neurons containing neuroglobin have a widespread distribution in the brain, but are also present in the olfactory system. In the fish retina, neuroglobin is mainly present in the inner segments of the photoreceptor cells. In the gills, the chloride cells were identified to express neuroglobin. Neuroglobin appears to be associated with mitochondria-rich cell types and thus oxygen consumption rates, suggesting a myoglobin-like function of this protein in facilitated oxygen diffusion.


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