Y. Yamamoto, H. Yoshikawa and S. Nagano contributed equally to this work.
Myelin-associated oligodendrocytic basic protein is essential for normal arrangement of the radial component in central nervous system myelin
Article first published online: 24 DEC 2001
European Journal of Neuroscience
Volume 11, Issue 3, pages 847–855, March 1999
How to Cite
Yamamoto, Y., Yoshikawa, H., Nagano, S., Kondoh, G., Sadahiro, S., Gotow, T., Yanagihara, T. and Sakoda, S. (1999), Myelin-associated oligodendrocytic basic protein is essential for normal arrangement of the radial component in central nervous system myelin. European Journal of Neuroscience, 11: 847–855. doi: 10.1046/j.1460-9568.1999.00490.x
- Issue published online: 24 DEC 2001
- Article first published online: 24 DEC 2001
- Received 10 August 1998, revised 5 October 1998, accepted 12 October 1998
- major dense line;
- null mutant mice
We previously reported that myelin-associated oligodendrocytic basic protein (MOBP) was abundantly expressed in the central nervous system (CNS) myelin, and shared several characteristics with myelin basic protein (MBP). In particular, a cluster of positively charged amino acids was considered to facilitate compaction of the cytoplasmic face of the myelin sheath, as in the case of MBP. However, the contribution of MOBP in forming and maintaining the myelin sheath still remains unclear. Recent investigations showed that one isoform of MOBP was expressed in the embryo prior to myelination, and MOBP isoforms were colocalized with the microtubular network and nucleus in vitro. To explore the role of MOBP in vivo, we generated MOBP-deficient mice and analysed the CNS myelin. Surprisingly, the compact myelin was formed, however, the myelin from MOBP-deficient mice exposed to hexachlorophene, a known dysmyelinating agent, showed widening of the major dense lines. These results suggest that MOBP is not essential for myelin formation, but reinforces the apposition of the cytoplasmic faces of the myelin sheath. A striking phenotype of MOBP-deficient mice was the presence of the straight ‘condensed' radial component. This component has been described as a tight junction-like complex running radially and zig-zag through the CNS myelin sheath between inner and outer mesaxons. These results suggest that MOBP is essential for normal arrangement of the radial component.