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A vertebrate globin expressed in the brain


Haemoglobins and myoglobins constitute related protein families that function in oxygen transport and storage in humans and other vertebrates1,2. Here we report the identification of a third globin type in man and mouse. This protein is predominantly expressed in the brain, and therefore we have called it neuroglobin. Mouse neuroglobin is a monomer with a high oxygen affinity (half saturation pressure, P50 ≈ 2 torr). Analogous to myoglobin, neuroglobin may increase the availability of oxygen to brain tissue. The human neuroglobin gene (NGB), located on chromosome 14q24, has a unique exon–intron structure. Neuroglobin represents a distinct protein family that diverged early in metazoan evolution, probably before the Protostomia/Deuterostomia split.

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Figure 1: Comparison of human and mouse neuroglobin (HsaNGB and MmuNgb) with myglobins (HsaMB, accession number M14603; MmuMb, P04247) and haemoglobins α and β (HsaHBA, J00153; HsaHBB, M36640; MmuHba, A45964; MmuHbb, P02088).
Figure 2: Neuroglobin expression in adult mouse brain (sagittal section) was studied by in situ hybridization using a digoxigenin-labelled oligonucleotide probe.
Figure 3: Neighbour-joining tree of selected globins.


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We wish to thank R. Gebhardt and N. Hellmann for their help with the oxygen-binding studies; G. Ungerechts for his assistance in the cloning; E. Jaenicke for running the FPLC; L. Moens and S. Dewilde for sharing experimental protocols and for discussions; and H. Decker, E. R. Schmidt and J. Markl for excellent working facilities, continuous support and valuable suggestions. This work is supported by the Deutsche Forschungsgemeinschaft (DFG) and the Naturwissenschaftlich-Medizinisches Forschungszentrum (NMFZ) Mainz.

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Burmester, T., Weich, B., Reinhardt, S. et al. A vertebrate globin expressed in the brain. Nature 407, 520–523 (2000).

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