Meiniel R, Meiniel A
Cell Tissue Res. 1985;239(2):359-64. doi: 10.1007/BF00218016.
The glycoprotein secretions of the subcommissural organ were analyzed with the use of nine fluorescent lectins, specific to different sugar moieties. After exposure to Concanavalin A a bright fluorescence was observed in the ependymal cells of the subcommissural organs of all vertebrates studied (Lampetra planeri, Ameiurus nebulosus, Bufo bufo, Lacerta vivipara, Gallus gallus, Rattus norvegicus, Ovis aries). The fluorescence is abolished by the competitive sugar, alpha-D-mannopyranosyl. The intensity of the lectin fluorescence decreases from the phylogenetically lower to the higher forms, paralleled by a change in polarity of the secretion from a vascular (lower vertebrates) to a ventricular (higher vertebrates) direction. The strong affinity for Concanavalin A suggests the presence of a glycoprotein rich in mannosyl residues in the ependymal cells and a similarity of composition of this glycoprotein among the vertebrates. Lens culinaris agglutinin and wheat germ agglutinin revealed fluorescent "rosettes" in the hypendymal cells of the sheep. Binding of both these lectins suggests the presence of a glycoprotein rich in N-acetyl-D-glucosamine. In the underlying ventricular cavity, no fluorescence could be observed, suggesting that the Reissner's fiber does not possess the same carbohydrate constitution as the ependymal secretion of the subcommissural organ.
