Abstract
The subcommissural organ-spondin (SCO-spondin), a glycoprotein belonging to the thrombospondin family, is secreted by specialyzed cells located at the floor and roof plates during the ontogenetic development of the central nervous system, and by the subcommissural organ (SCO) in adulthood. The intracellular secretion of the bovine SCO was purified by immunoaffinity chromatography with monoclonal antibodies raised against the Reissner's fiber (RF), a fibrous structure present at the ventricular cavities and that results from the polymerization of the SCO-spondin apically released by the SCO secretory cells. The purified secretion was used as a SCO-spondin source and assayed on cultures of the rat neuroblastoma B104 cell line. High doses of SCO secretory glucoproteins inhibited the proliferation of cultured neuroblasts, while lower concentrations stimulated neurite outgrowth and cellular aggregation.
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