Complex-type glycoproteins synthesized in the subcommissural organ of mammals |
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Authors: | Dr. Annie Meiniel Jean-Louis Molat Robert Meiniel |
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Affiliation: | (1) Laboratoire de Biologie animale et UA CNRS 677, Université Blaise Pascal, Clermont-Ferrand, France;(2) Laboratoire de Biologie animale, BP 45, F-63170 Aubière, France |
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Abstract: | ![]() Summary The secretory activity in the subcommissural organ (SCO) of the sheep and cow was examined by means of lectin histochemistry and cytochemistry. Among the various lectins tested, Concanavalin A (Con A) revealed glycoproteins rich in mannosyl residues in the rough endoplasmic reticulum of ependymal and hypendymal cells. One of these Con A-positive glycoproteins may represent the precursor of the specific secretory component elaborated in the SCO, giving rise to Reissner's fiber. Lens culinaris agglutinin (LCA) and Phaseolus vulgaris hemagglutinins (E-PHA and L-PHA), known to bind to oligosaccharides, as well as wheat-germ agglutinin (WGA) revealing neuraminic acid, labeled secretory granules located in the apical part of ependymal and hypendymal cells of ruminants, and also Reissner's fiber. Electron-microscopic visualization of WGA-positive material in the Golgi complex shows that complex-type glycoproteins are synthesized in the subcommissural organ of mammals. The electron-dense material is mainly secreted into the ventricular cavity and gives rise to Reissner's fiber. On the basis of lectin affinity for oligosaccharides, a structure of the complex-type oligosaccharide is proposed. |
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Keywords: | Subcommissural organ Reissner's fiber Glycoproteins Lectins Mammals (sheep, cow) |
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