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Journal of Neuroscience, Vol 16, 467-477, Copyright © 1996 by Society for Neuroscience
Molecular and developmental characterization of novel cDNAs of the myelin-associated/oligodendrocytic basic protein
A Holz, N Schaeren-Wiemers, C Schaefer, U Pott, RJ Colello and ME Schwab
Brain Research Institute, University of Zurich, Switzerland.
Several novel myelin-associated/oligodendrocytic basic protein (MOBP)
isoforms were identified in this study by cDNA cloning. They are small,
highly basic polypeptides comprising 69, 81, and 99 amino acids (8.2, 9.7,
and 11.7 kDa, respectively) and show no significant homology with described
proteins or domain structures. All (as yet) identified MOBP isoforms are
identical in amino acids 1-68 but differ in the length and polarity of the
C-terminal region. One isoform, designated MOBP81, was shown to be
expressed abundantly during development. Interestingly, MOBP81 has a
significant clustering of positively charged residues at positions 69-81, a
feature that also has been observed for myelin basic protein (MBP) and Po.
As demonstrated by in situ hybridization, MOBP gene expression occurs
during development of the rat optic nerve later than that of MBP and
proteolipid protein and coincides exactly with the beginning of myelin
compaction. The 2.6 kb MOBP81-A transcript is localized in the processes of
oligodendrocytes, whereas the 3.8 kb MOBP81-B transcript is restricted to
the perinuclear region. Therefore, MOBP81-A and related mRNAs seem to be
transported to the periphery of the oligodendrocytes, as is known for the
transcripts of the MBP gene. The late developmental expression of the MOBP
gene suggests that the MOBP proteins act at the late steps of myelin
formation, possibly in myelin compaction and in the maintenance of the
myelin sheath.
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