The recently described single copy myelin-associated oligodendrocytic basic protein (Mobp) gene is expressed exclusively in the central nervous system (CNS). The gene encodes a family of small highly basic polypeptides with predicted amino acid lengths of 69, 71, 81, 99 and 170, all of which share a 68 residue amino terminal. Here we report on the subcellular distribution of two of these polypeptides termed MOBP81 and MOBP170 in transiently transfected Cos7 cells using an antibody raised against a region common to all isoforms of MOBP. Additionally, we describe MOBP trafficking in cultured mouse spinal cord oligodendrocytes. Immunostaining for MOBP81 is intense in the perinuclear region and extends throughout the cytoplasm colocalizing with the microtubular cytoskeletal network. Consistent with this we demonstrate that MOBP partitions with the cytoskeletal fraction prepared from myelin. In contrast, although MOBP170 is present in the cytoplasm it does not colocalize with the cytoskeleton and displays a greater variation in distribution. In the majority of transfectants immunostaining is present throughout the karyoplasm but with increased intensity around the nucleolus. Within mouse primary oligodendrocytes endogenous MOBP is present in the cell body and processes colocalizing with the microtubular network. Immunoreactivity is not detectable in the nucleus in these mature oligodendrocytes. These significant differences in MOBP81 and MOBP170 protein kinesis coupled to different expression profiles of their respective message populations may be indicative of both myelin structural and cellular/regulatory functions, respectively, for these polypeptides.

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