Characterization of a novel oligodendrocyte cell surface molecule.

Abstract

Cell-type-specific reagents have proven useful in the analysis of central nervous system (CNS) development and function. Most markers of oligodendrocytes are components of myelin sheath, which in the CNS is the specific product of oligodendrocytes. We have isolated a novel monoclonal antibody termed 2B10 which was raised against embryonic rat spinal cord tissue. In adult rat cerebrum, cerebellum, and spinal cord, 2B10 immunoreactivity is predominantly localized in white matter. 2B10 immunoreactivity is absent from peripheral nerve, suggesting that in the nervous system the 2B10 antigen is restricted to the CNS. Dissociated cell culture studies indicate that 2B10 labels a cell surface molecule, and its cellular distribution is coincident with O1 and myelin basic protein-positive oligodendrocytes. By contrast, 2B10 does not label GFAP-positive astrocytes. These data suggest that in the CNS the 2B10 antigen is expressed specifically on oligodendrocytes. Biochemical analysis indicates that 2B10 recognizes a protein with an apparent molecular weight of approximately 79,000 in reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Developmentally, 2B10 immunoreactivity is detectable in rat spinal cord at as early as embryonic day 14. The relative abundance of this molecule decreases during myelination, but is maintained at a sustained level throughout adulthood. The 2B10 antigen appears not to be a myelin-associated protein since it is not detected in purified myelin fractions. 2B10 immunoreactivity is not detectable in extracts of rat sciatic nerve, heart, kidney, muscle, and skin, but is detectable in extracts of spleen and thymus. These data suggest that the 2B10 antigen is a novel cell surface molecule that is expressed on oligodendrocyte lineage cells throughout development.